BRPI0616923A2 - anticorpos monoclonais, seus usos e composição farmacêutica - Google Patents
anticorpos monoclonais, seus usos e composição farmacêutica Download PDFInfo
- Publication number
- BRPI0616923A2 BRPI0616923A2 BRPI0616923-6A BRPI0616923A BRPI0616923A2 BR PI0616923 A2 BRPI0616923 A2 BR PI0616923A2 BR PI0616923 A BRPI0616923 A BR PI0616923A BR PI0616923 A2 BRPI0616923 A2 BR PI0616923A2
- Authority
- BR
- Brazil
- Prior art keywords
- antibody
- myostatin
- seq
- monoclonal antibody
- human
- Prior art date
Links
- 239000008194 pharmaceutical composition Substances 0.000 title claims abstract description 19
- 108010056852 Myostatin Proteins 0.000 claims abstract description 243
- 241000282414 Homo sapiens Species 0.000 claims abstract description 146
- 230000027455 binding Effects 0.000 claims abstract description 103
- 150000001413 amino acids Chemical class 0.000 claims abstract description 53
- 239000012634 fragment Substances 0.000 claims abstract description 31
- 210000003205 muscle Anatomy 0.000 claims abstract description 30
- 230000001965 increasing effect Effects 0.000 claims abstract description 10
- 230000037182 bone density Effects 0.000 claims abstract description 6
- 108090000765 processed proteins & peptides Proteins 0.000 claims description 82
- 238000003556 assay Methods 0.000 claims description 56
- 102100040898 Growth/differentiation factor 11 Human genes 0.000 claims description 55
- 101710194452 Growth/differentiation factor 11 Proteins 0.000 claims description 52
- 125000003275 alpha amino acid group Chemical group 0.000 claims description 49
- 102000004196 processed proteins & peptides Human genes 0.000 claims description 43
- 229920001184 polypeptide Polymers 0.000 claims description 38
- 241001465754 Metazoa Species 0.000 claims description 29
- 230000000694 effects Effects 0.000 claims description 27
- 238000000338 in vitro Methods 0.000 claims description 18
- 238000011282 treatment Methods 0.000 claims description 16
- 102100039939 Growth/differentiation factor 8 Human genes 0.000 claims description 11
- 239000003814 drug Substances 0.000 claims description 10
- 108010054477 Immunoglobulin Fab Fragments Proteins 0.000 claims description 7
- 102000001706 Immunoglobulin Fab Fragments Human genes 0.000 claims description 7
- 206010006895 Cachexia Diseases 0.000 claims description 6
- 108010067060 Immunoglobulin Variable Region Proteins 0.000 claims description 6
- 102000017727 Immunoglobulin Variable Region Human genes 0.000 claims description 6
- 208000001145 Metabolic Syndrome Diseases 0.000 claims description 5
- 208000021642 Muscular disease Diseases 0.000 claims description 5
- 201000009623 Myopathy Diseases 0.000 claims description 5
- 208000001132 Osteoporosis Diseases 0.000 claims description 5
- 208000001647 Renal Insufficiency Diseases 0.000 claims description 5
- 201000000690 abdominal obesity-metabolic syndrome Diseases 0.000 claims description 5
- 201000006370 kidney failure Diseases 0.000 claims description 5
- 208000006545 Chronic Obstructive Pulmonary Disease Diseases 0.000 claims description 4
- 238000002360 preparation method Methods 0.000 claims description 4
- 230000002265 prevention Effects 0.000 claims description 4
- 208000001072 type 2 diabetes mellitus Diseases 0.000 claims description 4
- 239000003937 drug carrier Substances 0.000 claims description 3
- 208000017169 kidney disease Diseases 0.000 claims description 3
- 208000019423 liver disease Diseases 0.000 claims description 3
- 201000006938 muscular dystrophy Diseases 0.000 claims description 3
- 208000010428 Muscle Weakness Diseases 0.000 claims description 2
- 206010028372 Muscular weakness Diseases 0.000 claims description 2
- 235000013305 food Nutrition 0.000 claims description 2
- 206010019280 Heart failures Diseases 0.000 claims 1
- 102000004472 Myostatin Human genes 0.000 abstract description 234
- 239000000427 antigen Substances 0.000 abstract description 59
- 108091007433 antigens Proteins 0.000 abstract description 58
- 102000036639 antigens Human genes 0.000 abstract description 58
- 241000124008 Mammalia Species 0.000 abstract description 22
- 241000894007 species Species 0.000 abstract description 15
- 101000886562 Homo sapiens Growth/differentiation factor 8 Proteins 0.000 abstract description 14
- 102000054677 human MSTN Human genes 0.000 abstract description 9
- 230000003472 neutralizing effect Effects 0.000 abstract description 8
- 102000012946 Growth Differentiation Factor 1 Human genes 0.000 abstract 1
- 108010090296 Growth Differentiation Factor 1 Proteins 0.000 abstract 1
- 229940127121 immunoconjugate Drugs 0.000 abstract 1
- 210000004027 cell Anatomy 0.000 description 99
- 108090000623 proteins and genes Proteins 0.000 description 75
- 238000000034 method Methods 0.000 description 60
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 59
- 235000001014 amino acid Nutrition 0.000 description 58
- 229940024606 amino acid Drugs 0.000 description 53
- 102000004169 proteins and genes Human genes 0.000 description 38
- 235000018102 proteins Nutrition 0.000 description 36
- 102100035360 Cerebellar degeneration-related antigen 1 Human genes 0.000 description 31
- 208000035475 disorder Diseases 0.000 description 30
- 201000010099 disease Diseases 0.000 description 29
- 230000014509 gene expression Effects 0.000 description 26
- 230000001225 therapeutic effect Effects 0.000 description 24
- 108010047041 Complementarity Determining Regions Proteins 0.000 description 22
- 239000013598 vector Substances 0.000 description 22
- 241001529936 Murinae Species 0.000 description 21
- 239000000872 buffer Substances 0.000 description 21
- 108020004414 DNA Proteins 0.000 description 20
- 239000013604 expression vector Substances 0.000 description 20
- 108060003951 Immunoglobulin Proteins 0.000 description 17
- 230000002163 immunogen Effects 0.000 description 17
- 102000018358 immunoglobulin Human genes 0.000 description 17
- 210000004602 germ cell Anatomy 0.000 description 16
- 238000001727 in vivo Methods 0.000 description 16
- 150000007523 nucleic acids Chemical class 0.000 description 15
- 230000004071 biological effect Effects 0.000 description 14
- 239000000203 mixture Substances 0.000 description 13
- 238000003259 recombinant expression Methods 0.000 description 13
- 238000006467 substitution reaction Methods 0.000 description 13
- 238000004519 manufacturing process Methods 0.000 description 12
- 241000699670 Mus sp. Species 0.000 description 11
- 102000004887 Transforming Growth Factor beta Human genes 0.000 description 11
- 108090001012 Transforming Growth Factor beta Proteins 0.000 description 11
- 238000002965 ELISA Methods 0.000 description 10
- 241000282412 Homo Species 0.000 description 10
- 230000000890 antigenic effect Effects 0.000 description 10
- 230000008901 benefit Effects 0.000 description 10
- 230000006870 function Effects 0.000 description 10
- 102000039446 nucleic acids Human genes 0.000 description 10
- 108020004707 nucleic acids Proteins 0.000 description 10
- 230000002829 reductive effect Effects 0.000 description 10
- 239000000243 solution Substances 0.000 description 10
- 238000012360 testing method Methods 0.000 description 10
- 238000005516 engineering process Methods 0.000 description 9
- 230000001105 regulatory effect Effects 0.000 description 9
- ZRKFYGHZFMAOKI-QMGMOQQFSA-N tgfbeta Chemical compound C([C@H](NC(=O)[C@H](C(C)C)NC(=O)CNC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H]([C@@H](C)O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H]([C@@H](C)O)NC(=O)[C@H](CC(C)C)NC(=O)CNC(=O)[C@H](C)NC(=O)[C@H](CO)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@@H](NC(=O)[C@H](C)NC(=O)[C@H](C)NC(=O)[C@@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](N)CCSC)C(C)C)[C@@H](C)CC)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](C)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](C)C(=O)N[C@@H](CC(C)C)C(=O)N1[C@@H](CCC1)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(C)C)C(O)=O)C1=CC=C(O)C=C1 ZRKFYGHZFMAOKI-QMGMOQQFSA-N 0.000 description 9
- 210000001519 tissue Anatomy 0.000 description 9
- 239000011534 wash buffer Substances 0.000 description 9
- 241000699666 Mus <mouse, genus> Species 0.000 description 8
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 8
- 238000007792 addition Methods 0.000 description 8
- 125000000539 amino acid group Chemical group 0.000 description 8
- 238000001990 intravenous administration Methods 0.000 description 8
- 239000000463 material Substances 0.000 description 8
- 239000002953 phosphate buffered saline Substances 0.000 description 8
- 230000000069 prophylactic effect Effects 0.000 description 8
- 241000271566 Aves Species 0.000 description 7
- 102000004190 Enzymes Human genes 0.000 description 7
- 108090000790 Enzymes Proteins 0.000 description 7
- 101000893545 Homo sapiens Growth/differentiation factor 11 Proteins 0.000 description 7
- 108091028043 Nucleic acid sequence Proteins 0.000 description 7
- 230000000903 blocking effect Effects 0.000 description 7
- 230000007423 decrease Effects 0.000 description 7
- 238000012217 deletion Methods 0.000 description 7
- 229940088598 enzyme Drugs 0.000 description 7
- 230000013595 glycosylation Effects 0.000 description 7
- 238000006206 glycosylation reaction Methods 0.000 description 7
- 239000001963 growth medium Substances 0.000 description 7
- 210000004408 hybridoma Anatomy 0.000 description 7
- 239000007924 injection Substances 0.000 description 7
- 238000002347 injection Methods 0.000 description 7
- 238000007912 intraperitoneal administration Methods 0.000 description 7
- 239000003550 marker Substances 0.000 description 7
- 239000002609 medium Substances 0.000 description 7
- 230000004044 response Effects 0.000 description 7
- 238000010561 standard procedure Methods 0.000 description 7
- NFGXHKASABOEEW-UHFFFAOYSA-N 1-methylethyl 11-methoxy-3,7,11-trimethyl-2,4-dodecadienoate Chemical compound COC(C)(C)CCCC(C)CC=CC(C)=CC(=O)OC(C)C NFGXHKASABOEEW-UHFFFAOYSA-N 0.000 description 6
- 241000287828 Gallus gallus Species 0.000 description 6
- 108010076504 Protein Sorting Signals Proteins 0.000 description 6
- 239000003153 chemical reaction reagent Substances 0.000 description 6
- 235000013330 chicken meat Nutrition 0.000 description 6
- 230000003247 decreasing effect Effects 0.000 description 6
- 230000037430 deletion Effects 0.000 description 6
- 238000005259 measurement Methods 0.000 description 6
- 108020003175 receptors Proteins 0.000 description 6
- 102000005962 receptors Human genes 0.000 description 6
- 238000011084 recovery Methods 0.000 description 6
- 239000000758 substrate Substances 0.000 description 6
- 239000003981 vehicle Substances 0.000 description 6
- 241000283690 Bos taurus Species 0.000 description 5
- 241000283707 Capra Species 0.000 description 5
- BVKZGUZCCUSVTD-UHFFFAOYSA-L Carbonate Chemical compound [O-]C([O-])=O BVKZGUZCCUSVTD-UHFFFAOYSA-L 0.000 description 5
- 108060001084 Luciferase Proteins 0.000 description 5
- 208000008589 Obesity Diseases 0.000 description 5
- 108020004511 Recombinant DNA Proteins 0.000 description 5
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 5
- 238000002835 absorbance Methods 0.000 description 5
- 230000003321 amplification Effects 0.000 description 5
- 239000011324 bead Substances 0.000 description 5
- 150000001875 compounds Chemical class 0.000 description 5
- 238000011161 development Methods 0.000 description 5
- 230000018109 developmental process Effects 0.000 description 5
- 239000003623 enhancer Substances 0.000 description 5
- 230000001900 immune effect Effects 0.000 description 5
- 230000002401 inhibitory effect Effects 0.000 description 5
- 230000005764 inhibitory process Effects 0.000 description 5
- 238000003199 nucleic acid amplification method Methods 0.000 description 5
- 235000020824 obesity Nutrition 0.000 description 5
- 238000002823 phage display Methods 0.000 description 5
- 108091033319 polynucleotide Proteins 0.000 description 5
- 102000040430 polynucleotide Human genes 0.000 description 5
- 239000002157 polynucleotide Substances 0.000 description 5
- 210000002027 skeletal muscle Anatomy 0.000 description 5
- YBJHBAHKTGYVGT-ZKWXMUAHSA-N (+)-Biotin Chemical compound N1C(=O)N[C@@H]2[C@H](CCCCC(=O)O)SC[C@@H]21 YBJHBAHKTGYVGT-ZKWXMUAHSA-N 0.000 description 4
- MTCFGRXMJLQNBG-REOHCLBHSA-N (2S)-2-Amino-3-hydroxypropansäure Chemical compound OC[C@H](N)C(O)=O MTCFGRXMJLQNBG-REOHCLBHSA-N 0.000 description 4
- 241000282465 Canis Species 0.000 description 4
- 108091035707 Consensus sequence Proteins 0.000 description 4
- 241000701022 Cytomegalovirus Species 0.000 description 4
- 241000283086 Equidae Species 0.000 description 4
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 4
- 241000700159 Rattus Species 0.000 description 4
- 238000011579 SCID mouse model Methods 0.000 description 4
- UIIMBOGNXHQVGW-UHFFFAOYSA-M Sodium bicarbonate Chemical compound [Na+].OC([O-])=O UIIMBOGNXHQVGW-UHFFFAOYSA-M 0.000 description 4
- 210000000577 adipose tissue Anatomy 0.000 description 4
- 208000020538 atrophic muscular disease Diseases 0.000 description 4
- 210000000988 bone and bone Anatomy 0.000 description 4
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 4
- 230000002860 competitive effect Effects 0.000 description 4
- 238000004590 computer program Methods 0.000 description 4
- 239000003085 diluting agent Substances 0.000 description 4
- 238000010494 dissociation reaction Methods 0.000 description 4
- 230000005593 dissociations Effects 0.000 description 4
- 239000012636 effector Substances 0.000 description 4
- GNBHRKFJIUUOQI-UHFFFAOYSA-N fluorescein Chemical compound O1C(=O)C2=CC=CC=C2C21C1=CC=C(O)C=C1OC1=CC(O)=CC=C21 GNBHRKFJIUUOQI-UHFFFAOYSA-N 0.000 description 4
- 230000036541 health Effects 0.000 description 4
- 208000019622 heart disease Diseases 0.000 description 4
- 239000000710 homodimer Substances 0.000 description 4
- 238000011813 knockout mouse model Methods 0.000 description 4
- 239000003446 ligand Substances 0.000 description 4
- 238000002703 mutagenesis Methods 0.000 description 4
- 231100000350 mutagenesis Toxicity 0.000 description 4
- 238000006386 neutralization reaction Methods 0.000 description 4
- 239000005022 packaging material Substances 0.000 description 4
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 4
- 239000012146 running buffer Substances 0.000 description 4
- 230000028327 secretion Effects 0.000 description 4
- 210000002966 serum Anatomy 0.000 description 4
- 239000011780 sodium chloride Substances 0.000 description 4
- 208000024891 symptom Diseases 0.000 description 4
- 208000011580 syndromic disease Diseases 0.000 description 4
- 238000011830 transgenic mouse model Methods 0.000 description 4
- -1 xylose sugars Chemical class 0.000 description 4
- JKMHFZQWWAIEOD-UHFFFAOYSA-N 2-[4-(2-hydroxyethyl)piperazin-1-yl]ethanesulfonic acid Chemical compound OCC[NH+]1CCN(CCS([O-])(=O)=O)CC1 JKMHFZQWWAIEOD-UHFFFAOYSA-N 0.000 description 3
- 102000053602 DNA Human genes 0.000 description 3
- 241000282324 Felis Species 0.000 description 3
- 206010019663 Hepatic failure Diseases 0.000 description 3
- 102000008394 Immunoglobulin Fragments Human genes 0.000 description 3
- 108010021625 Immunoglobulin Fragments Proteins 0.000 description 3
- 108700005091 Immunoglobulin Genes Proteins 0.000 description 3
- FBOZXECLQNJBKD-ZDUSSCGKSA-N L-methotrexate Chemical compound C=1N=C2N=C(N)N=C(N)C2=NC=1CN(C)C1=CC=C(C(=O)N[C@@H](CCC(O)=O)C(O)=O)C=C1 FBOZXECLQNJBKD-ZDUSSCGKSA-N 0.000 description 3
- 241000829100 Macaca mulatta polyomavirus 1 Species 0.000 description 3
- 239000012124 Opti-MEM Substances 0.000 description 3
- 241001494479 Pecora Species 0.000 description 3
- 241000286209 Phasianidae Species 0.000 description 3
- 229920001213 Polysorbate 20 Polymers 0.000 description 3
- 241000288906 Primates Species 0.000 description 3
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 3
- 206010040047 Sepsis Diseases 0.000 description 3
- 208000006011 Stroke Diseases 0.000 description 3
- 241000282887 Suidae Species 0.000 description 3
- 241000269370 Xenopus <genus> Species 0.000 description 3
- 238000009825 accumulation Methods 0.000 description 3
- 230000004075 alteration Effects 0.000 description 3
- 230000001580 bacterial effect Effects 0.000 description 3
- 230000009286 beneficial effect Effects 0.000 description 3
- 108010005774 beta-Galactosidase Proteins 0.000 description 3
- 230000037396 body weight Effects 0.000 description 3
- 210000004899 c-terminal region Anatomy 0.000 description 3
- 150000001720 carbohydrates Chemical group 0.000 description 3
- 210000004978 chinese hamster ovary cell Anatomy 0.000 description 3
- 230000001684 chronic effect Effects 0.000 description 3
- 238000003776 cleavage reaction Methods 0.000 description 3
- 230000009260 cross reactivity Effects 0.000 description 3
- 235000018417 cysteine Nutrition 0.000 description 3
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 3
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 description 3
- 238000001514 detection method Methods 0.000 description 3
- 230000004069 differentiation Effects 0.000 description 3
- 238000010790 dilution Methods 0.000 description 3
- 239000012895 dilution Substances 0.000 description 3
- 239000000539 dimer Substances 0.000 description 3
- 229940079593 drug Drugs 0.000 description 3
- 230000004927 fusion Effects 0.000 description 3
- 230000012010 growth Effects 0.000 description 3
- 239000003102 growth factor Substances 0.000 description 3
- 238000002649 immunization Methods 0.000 description 3
- 230000003053 immunization Effects 0.000 description 3
- 229940072221 immunoglobulins Drugs 0.000 description 3
- 230000003993 interaction Effects 0.000 description 3
- 238000012482 interaction analysis Methods 0.000 description 3
- 208000007903 liver failure Diseases 0.000 description 3
- 210000004962 mammalian cell Anatomy 0.000 description 3
- 229960000485 methotrexate Drugs 0.000 description 3
- 230000035772 mutation Effects 0.000 description 3
- 201000008482 osteoarthritis Diseases 0.000 description 3
- 230000001575 pathological effect Effects 0.000 description 3
- 239000000546 pharmaceutical excipient Substances 0.000 description 3
- 239000000256 polyoxyethylene sorbitan monolaurate Substances 0.000 description 3
- 235000010486 polyoxyethylene sorbitan monolaurate Nutrition 0.000 description 3
- 238000012545 processing Methods 0.000 description 3
- 238000003127 radioimmunoassay Methods 0.000 description 3
- 230000008439 repair process Effects 0.000 description 3
- 230000010076 replication Effects 0.000 description 3
- 208000001076 sarcopenia Diseases 0.000 description 3
- 230000007017 scission Effects 0.000 description 3
- 125000003607 serino group Chemical group [H]N([H])[C@]([H])(C(=O)[*])C(O[H])([H])[H] 0.000 description 3
- 230000009870 specific binding Effects 0.000 description 3
- 239000000126 substance Substances 0.000 description 3
- 230000001629 suppression Effects 0.000 description 3
- 238000013518 transcription Methods 0.000 description 3
- 230000035897 transcription Effects 0.000 description 3
- 238000001890 transfection Methods 0.000 description 3
- 241000701161 unidentified adenovirus Species 0.000 description 3
- 102000002260 Alkaline Phosphatase Human genes 0.000 description 2
- 108020004774 Alkaline Phosphatase Proteins 0.000 description 2
- 101100227726 Arabidopsis thaliana FRL3 gene Proteins 0.000 description 2
- 101100120609 Caenorhabditis elegans frh-1 gene Proteins 0.000 description 2
- 229920002307 Dextran Polymers 0.000 description 2
- 240000006497 Dianthus caryophyllus Species 0.000 description 2
- 235000009355 Dianthus caryophyllus Nutrition 0.000 description 2
- 102100024746 Dihydrofolate reductase Human genes 0.000 description 2
- 241000196324 Embryophyta Species 0.000 description 2
- 101150023991 FMNL1 gene Proteins 0.000 description 2
- 101150005226 FRL1 gene Proteins 0.000 description 2
- 101150065691 FRL2 gene Proteins 0.000 description 2
- 102100028930 Formin-like protein 1 Human genes 0.000 description 2
- 102100032789 Formin-like protein 3 Human genes 0.000 description 2
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Chemical compound OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 2
- 239000004471 Glycine Substances 0.000 description 2
- 108010041881 Growth Differentiation Factor 10 Proteins 0.000 description 2
- 102100040895 Growth/differentiation factor 10 Human genes 0.000 description 2
- 239000007995 HEPES buffer Substances 0.000 description 2
- 101000898034 Homo sapiens Hepatocyte growth factor Proteins 0.000 description 2
- 101000869690 Homo sapiens Protein S100-A8 Proteins 0.000 description 2
- 108010001336 Horseradish Peroxidase Proteins 0.000 description 2
- 239000005089 Luciferase Substances 0.000 description 2
- CSNNHWWHGAXBCP-UHFFFAOYSA-L Magnesium sulfate Chemical compound [Mg+2].[O-][S+2]([O-])([O-])[O-] CSNNHWWHGAXBCP-UHFFFAOYSA-L 0.000 description 2
- 208000029549 Muscle injury Diseases 0.000 description 2
- 206010028980 Neoplasm Diseases 0.000 description 2
- 108091005461 Nucleic proteins Proteins 0.000 description 2
- 230000004989 O-glycosylation Effects 0.000 description 2
- 206010035226 Plasma cell myeloma Diseases 0.000 description 2
- 102100032442 Protein S100-A8 Human genes 0.000 description 2
- 241000282898 Sus scrofa Species 0.000 description 2
- 102000007453 TGF-beta Superfamily Proteins Human genes 0.000 description 2
- 108010085004 TGF-beta Superfamily Proteins Proteins 0.000 description 2
- 239000004473 Threonine Substances 0.000 description 2
- 108010022394 Threonine synthase Proteins 0.000 description 2
- 239000013543 active substance Substances 0.000 description 2
- 210000001789 adipocyte Anatomy 0.000 description 2
- 238000004458 analytical method Methods 0.000 description 2
- 230000003042 antagnostic effect Effects 0.000 description 2
- 239000005557 antagonist Substances 0.000 description 2
- 230000005875 antibody response Effects 0.000 description 2
- 102000005936 beta-Galactosidase Human genes 0.000 description 2
- 238000001574 biopsy Methods 0.000 description 2
- 229960002685 biotin Drugs 0.000 description 2
- 235000020958 biotin Nutrition 0.000 description 2
- 239000011616 biotin Substances 0.000 description 2
- 239000001506 calcium phosphate Substances 0.000 description 2
- 229910000389 calcium phosphate Inorganic materials 0.000 description 2
- 235000011010 calcium phosphates Nutrition 0.000 description 2
- 201000011510 cancer Diseases 0.000 description 2
- 238000004113 cell culture Methods 0.000 description 2
- 238000006243 chemical reaction Methods 0.000 description 2
- 238000007796 conventional method Methods 0.000 description 2
- 238000012258 culturing Methods 0.000 description 2
- UQLDLKMNUJERMK-UHFFFAOYSA-L di(octadecanoyloxy)lead Chemical compound [Pb+2].CCCCCCCCCCCCCCCCCC([O-])=O.CCCCCCCCCCCCCCCCCC([O-])=O UQLDLKMNUJERMK-UHFFFAOYSA-L 0.000 description 2
- 238000003745 diagnosis Methods 0.000 description 2
- 102000004419 dihydrofolate reductase Human genes 0.000 description 2
- 108020001096 dihydrofolate reductase Proteins 0.000 description 2
- 238000009826 distribution Methods 0.000 description 2
- 210000002257 embryonic structure Anatomy 0.000 description 2
- 230000002255 enzymatic effect Effects 0.000 description 2
- 239000012530 fluid Substances 0.000 description 2
- 101150029401 fmnl3 gene Proteins 0.000 description 2
- 238000009472 formulation Methods 0.000 description 2
- 108020001507 fusion proteins Proteins 0.000 description 2
- 102000037865 fusion proteins Human genes 0.000 description 2
- 238000010353 genetic engineering Methods 0.000 description 2
- 238000001631 haemodialysis Methods 0.000 description 2
- 230000000322 hemodialysis Effects 0.000 description 2
- 230000002209 hydrophobic effect Effects 0.000 description 2
- 206010020718 hyperplasia Diseases 0.000 description 2
- 230000028993 immune response Effects 0.000 description 2
- 238000001802 infusion Methods 0.000 description 2
- 238000003780 insertion Methods 0.000 description 2
- 230000037431 insertion Effects 0.000 description 2
- 238000007918 intramuscular administration Methods 0.000 description 2
- 238000002955 isolation Methods 0.000 description 2
- 150000002540 isothiocyanates Chemical class 0.000 description 2
- 210000003041 ligament Anatomy 0.000 description 2
- 230000000670 limiting effect Effects 0.000 description 2
- 231100000835 liver failure Toxicity 0.000 description 2
- 230000001404 mediated effect Effects 0.000 description 2
- 230000005486 microgravity Effects 0.000 description 2
- 235000013336 milk Nutrition 0.000 description 2
- 239000008267 milk Substances 0.000 description 2
- 210000004080 milk Anatomy 0.000 description 2
- 230000004048 modification Effects 0.000 description 2
- 238000012986 modification Methods 0.000 description 2
- 238000012544 monitoring process Methods 0.000 description 2
- 239000000178 monomer Substances 0.000 description 2
- 201000000050 myeloid neoplasm Diseases 0.000 description 2
- 239000013642 negative control Substances 0.000 description 2
- 210000000056 organ Anatomy 0.000 description 2
- 230000036961 partial effect Effects 0.000 description 2
- 239000002245 particle Substances 0.000 description 2
- 239000013612 plasmid Substances 0.000 description 2
- 238000003752 polymerase chain reaction Methods 0.000 description 2
- 229920000136 polysorbate Polymers 0.000 description 2
- 244000144977 poultry Species 0.000 description 2
- 235000013594 poultry meat Nutrition 0.000 description 2
- 239000002243 precursor Substances 0.000 description 2
- 230000008569 process Effects 0.000 description 2
- 230000002035 prolonged effect Effects 0.000 description 2
- 238000000159 protein binding assay Methods 0.000 description 2
- 239000012857 radioactive material Substances 0.000 description 2
- 238000011160 research Methods 0.000 description 2
- 230000002441 reversible effect Effects 0.000 description 2
- PYWVYCXTNDRMGF-UHFFFAOYSA-N rhodamine B Chemical compound [Cl-].C=12C=CC(=[N+](CC)CC)C=C2OC2=CC(N(CC)CC)=CC=C2C=1C1=CC=CC=C1C(O)=O PYWVYCXTNDRMGF-UHFFFAOYSA-N 0.000 description 2
- 230000000276 sedentary effect Effects 0.000 description 2
- 230000011664 signaling Effects 0.000 description 2
- 235000017557 sodium bicarbonate Nutrition 0.000 description 2
- 229910000030 sodium bicarbonate Inorganic materials 0.000 description 2
- 239000007787 solid Substances 0.000 description 2
- 210000000952 spleen Anatomy 0.000 description 2
- 239000003381 stabilizer Substances 0.000 description 2
- 238000012409 standard PCR amplification Methods 0.000 description 2
- 238000003860 storage Methods 0.000 description 2
- 238000007920 subcutaneous administration Methods 0.000 description 2
- 239000004094 surface-active agent Substances 0.000 description 2
- 230000009885 systemic effect Effects 0.000 description 2
- 238000002560 therapeutic procedure Methods 0.000 description 2
- 238000010361 transduction Methods 0.000 description 2
- 230000026683 transduction Effects 0.000 description 2
- 230000009261 transgenic effect Effects 0.000 description 2
- 238000013519 translation Methods 0.000 description 2
- 238000002054 transplantation Methods 0.000 description 2
- QORWJWZARLRLPR-UHFFFAOYSA-H tricalcium bis(phosphate) Chemical compound [Ca+2].[Ca+2].[Ca+2].[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O QORWJWZARLRLPR-UHFFFAOYSA-H 0.000 description 2
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 2
- 238000011144 upstream manufacturing Methods 0.000 description 2
- KYBXNPIASYUWLN-WUCPZUCCSA-N (2s)-5-hydroxypyrrolidine-2-carboxylic acid Chemical compound OC1CC[C@@H](C(O)=O)N1 KYBXNPIASYUWLN-WUCPZUCCSA-N 0.000 description 1
- LMDZBCPBFSXMTL-UHFFFAOYSA-N 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide Chemical compound CCN=C=NCCCN(C)C LMDZBCPBFSXMTL-UHFFFAOYSA-N 0.000 description 1
- 125000000979 2-amino-2-oxoethyl group Chemical group [H]C([*])([H])C(=O)N([H])[H] 0.000 description 1
- PMUNIMVZCACZBB-UHFFFAOYSA-N 2-hydroxyethylazanium;chloride Chemical compound Cl.NCCO PMUNIMVZCACZBB-UHFFFAOYSA-N 0.000 description 1
- 108010022752 Acetylcholinesterase Proteins 0.000 description 1
- 102000012440 Acetylcholinesterase Human genes 0.000 description 1
- 241000272517 Anseriformes Species 0.000 description 1
- 206010003694 Atrophy Diseases 0.000 description 1
- 108090001008 Avidin Proteins 0.000 description 1
- 108010049931 Bone Morphogenetic Protein 2 Proteins 0.000 description 1
- 108010049951 Bone Morphogenetic Protein 3 Proteins 0.000 description 1
- 108010049955 Bone Morphogenetic Protein 4 Proteins 0.000 description 1
- 108010049976 Bone Morphogenetic Protein 5 Proteins 0.000 description 1
- 108010049870 Bone Morphogenetic Protein 7 Proteins 0.000 description 1
- 102100024506 Bone morphogenetic protein 2 Human genes 0.000 description 1
- 102100024504 Bone morphogenetic protein 3 Human genes 0.000 description 1
- 102100024505 Bone morphogenetic protein 4 Human genes 0.000 description 1
- 102100022526 Bone morphogenetic protein 5 Human genes 0.000 description 1
- 102100022544 Bone morphogenetic protein 7 Human genes 0.000 description 1
- 102100022545 Bone morphogenetic protein 8B Human genes 0.000 description 1
- 101710117970 Bone morphogenetic protein 8B Proteins 0.000 description 1
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 1
- 241000282472 Canis lupus familiaris Species 0.000 description 1
- 102000014914 Carrier Proteins Human genes 0.000 description 1
- 108010078791 Carrier Proteins Proteins 0.000 description 1
- 108091026890 Coding region Proteins 0.000 description 1
- 108020004705 Codon Proteins 0.000 description 1
- 102000004420 Creatine Kinase Human genes 0.000 description 1
- 108010042126 Creatine kinase Proteins 0.000 description 1
- 241000699800 Cricetinae Species 0.000 description 1
- 241000699802 Cricetulus griseus Species 0.000 description 1
- 102000004127 Cytokines Human genes 0.000 description 1
- 108090000695 Cytokines Proteins 0.000 description 1
- 101150074155 DHFR gene Proteins 0.000 description 1
- XPDXVDYUQZHFPV-UHFFFAOYSA-N Dansyl Chloride Chemical compound C1=CC=C2C(N(C)C)=CC=CC2=C1S(Cl)(=O)=O XPDXVDYUQZHFPV-UHFFFAOYSA-N 0.000 description 1
- BWGNESOTFCXPMA-UHFFFAOYSA-N Dihydrogen disulfide Chemical compound SS BWGNESOTFCXPMA-UHFFFAOYSA-N 0.000 description 1
- 239000006144 Dulbecco’s modified Eagle's medium Substances 0.000 description 1
- KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 1
- YQYJSBFKSSDGFO-UHFFFAOYSA-N Epihygromycin Natural products OC1C(O)C(C(=O)C)OC1OC(C(=C1)O)=CC=C1C=C(C)C(=O)NC1C(O)C(O)C2OCOC2C1O YQYJSBFKSSDGFO-UHFFFAOYSA-N 0.000 description 1
- 241000283073 Equus caballus Species 0.000 description 1
- 108010054218 Factor VIII Proteins 0.000 description 1
- 102000001690 Factor VIII Human genes 0.000 description 1
- 102000009109 Fc receptors Human genes 0.000 description 1
- 108010087819 Fc receptors Proteins 0.000 description 1
- 241000724791 Filamentous phage Species 0.000 description 1
- 208000036119 Frailty Diseases 0.000 description 1
- 108010090293 Growth Differentiation Factor 3 Proteins 0.000 description 1
- 102100035364 Growth/differentiation factor 3 Human genes 0.000 description 1
- 239000012981 Hank's balanced salt solution Substances 0.000 description 1
- 241001272567 Hominoidea Species 0.000 description 1
- 108090000144 Human Proteins Proteins 0.000 description 1
- 102000003839 Human Proteins Human genes 0.000 description 1
- 206010020880 Hypertrophy Diseases 0.000 description 1
- DGAQECJNVWCQMB-PUAWFVPOSA-M Ilexoside XXIX Chemical compound C[C@@H]1CC[C@@]2(CC[C@@]3(C(=CC[C@H]4[C@]3(CC[C@@H]5[C@@]4(CC[C@@H](C5(C)C)OS(=O)(=O)[O-])C)C)[C@@H]2[C@]1(C)O)C)C(=O)O[C@H]6[C@@H]([C@H]([C@@H]([C@H](O6)CO)O)O)O.[Na+] DGAQECJNVWCQMB-PUAWFVPOSA-M 0.000 description 1
- 102000009786 Immunoglobulin Constant Regions Human genes 0.000 description 1
- 108010009817 Immunoglobulin Constant Regions Proteins 0.000 description 1
- 102000012745 Immunoglobulin Subunits Human genes 0.000 description 1
- 108010079585 Immunoglobulin Subunits Proteins 0.000 description 1
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical group SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 description 1
- ZDXPYRJPNDTMRX-VKHMYHEASA-N L-glutamine Chemical compound OC(=O)[C@@H](N)CCC(N)=O ZDXPYRJPNDTMRX-VKHMYHEASA-N 0.000 description 1
- 229930182816 L-glutamine Natural products 0.000 description 1
- AYFVYJQAPQTCCC-GBXIJSLDSA-N L-threonine Chemical compound C[C@@H](O)[C@H](N)C(O)=O AYFVYJQAPQTCCC-GBXIJSLDSA-N 0.000 description 1
- 101800001155 Latency-associated peptide Proteins 0.000 description 1
- 102400000401 Latency-associated peptide Human genes 0.000 description 1
- 208000019693 Lung disease Diseases 0.000 description 1
- 208000002693 Multiple Abnormalities Diseases 0.000 description 1
- 241000699660 Mus musculus Species 0.000 description 1
- 101001075141 Mus musculus Growth/differentiation factor 8 Proteins 0.000 description 1
- 101100448224 Mus musculus Mstn gene Proteins 0.000 description 1
- 206010028311 Muscle hypertrophy Diseases 0.000 description 1
- OVRNDRQMDRJTHS-CBQIKETKSA-N N-Acetyl-D-Galactosamine Chemical compound CC(=O)N[C@H]1[C@@H](O)O[C@H](CO)[C@H](O)[C@@H]1O OVRNDRQMDRJTHS-CBQIKETKSA-N 0.000 description 1
- NQTADLQHYWFPDB-UHFFFAOYSA-N N-Hydroxysuccinimide Chemical compound ON1C(=O)CCC1=O NQTADLQHYWFPDB-UHFFFAOYSA-N 0.000 description 1
- MBLBDJOUHNCFQT-UHFFFAOYSA-N N-acetyl-D-galactosamine Natural products CC(=O)NC(C=O)C(O)C(O)C(O)CO MBLBDJOUHNCFQT-UHFFFAOYSA-N 0.000 description 1
- 230000004988 N-glycosylation Effects 0.000 description 1
- 241001045988 Neogene Species 0.000 description 1
- 108700026244 Open Reading Frames Proteins 0.000 description 1
- 241000283973 Oryctolagus cuniculus Species 0.000 description 1
- 108010058846 Ovalbumin Proteins 0.000 description 1
- 108090000526 Papain Proteins 0.000 description 1
- 102000057297 Pepsin A Human genes 0.000 description 1
- 108090000284 Pepsin A Proteins 0.000 description 1
- 102000003992 Peroxidases Human genes 0.000 description 1
- 108010004729 Phycoerythrin Proteins 0.000 description 1
- 108010022233 Plasminogen Activator Inhibitor 1 Proteins 0.000 description 1
- 102100039418 Plasminogen activator inhibitor 1 Human genes 0.000 description 1
- 241000276498 Pollachius virens Species 0.000 description 1
- 239000002202 Polyethylene glycol Substances 0.000 description 1
- 108010039918 Polylysine Proteins 0.000 description 1
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 1
- 239000004365 Protease Substances 0.000 description 1
- 108700008625 Reporter Genes Proteins 0.000 description 1
- 241000283984 Rodentia Species 0.000 description 1
- 238000006811 Samuelson reaction Methods 0.000 description 1
- 206010039491 Sarcoma Diseases 0.000 description 1
- 229920002684 Sepharose Polymers 0.000 description 1
- 108010090804 Streptavidin Proteins 0.000 description 1
- 102000043168 TGF-beta family Human genes 0.000 description 1
- 108091085018 TGF-beta family Proteins 0.000 description 1
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 1
- 102000011117 Transforming Growth Factor beta2 Human genes 0.000 description 1
- 101800004564 Transforming growth factor alpha Proteins 0.000 description 1
- 102400001320 Transforming growth factor alpha Human genes 0.000 description 1
- 101800000304 Transforming growth factor beta-2 Proteins 0.000 description 1
- 241000700605 Viruses Species 0.000 description 1
- 208000027418 Wounds and injury Diseases 0.000 description 1
- SRBFZHDQGSBBOR-IOVATXLUSA-N Xylose Natural products O[C@@H]1COC(O)[C@H](O)[C@H]1O SRBFZHDQGSBBOR-IOVATXLUSA-N 0.000 description 1
- 230000001594 aberrant effect Effects 0.000 description 1
- 229940022698 acetylcholinesterase Drugs 0.000 description 1
- 230000003213 activating effect Effects 0.000 description 1
- 239000004480 active ingredient Substances 0.000 description 1
- 108010023082 activin A Proteins 0.000 description 1
- 108010023079 activin B Proteins 0.000 description 1
- 239000000654 additive Substances 0.000 description 1
- 230000011759 adipose tissue development Effects 0.000 description 1
- 230000002411 adverse Effects 0.000 description 1
- 230000009824 affinity maturation Effects 0.000 description 1
- 230000032683 aging Effects 0.000 description 1
- 238000012867 alanine scanning Methods 0.000 description 1
- 230000001476 alcoholic effect Effects 0.000 description 1
- WQZGKKKJIJFFOK-PHYPRBDBSA-N alpha-D-galactose Chemical compound OC[C@H]1O[C@H](O)[C@H](O)[C@@H](O)[C@H]1O WQZGKKKJIJFFOK-PHYPRBDBSA-N 0.000 description 1
- 150000001412 amines Chemical class 0.000 description 1
- 229940124277 aminobutyric acid Drugs 0.000 description 1
- 238000012870 ammonium sulfate precipitation Methods 0.000 description 1
- 230000008485 antagonism Effects 0.000 description 1
- 230000010056 antibody-dependent cellular cytotoxicity Effects 0.000 description 1
- 210000000628 antibody-producing cell Anatomy 0.000 description 1
- PYMYPHUHKUWMLA-UHFFFAOYSA-N arabinose Natural products OCC(O)C(O)C(O)C=O PYMYPHUHKUWMLA-UHFFFAOYSA-N 0.000 description 1
- 125000000613 asparagine group Chemical group N[C@@H](CC(N)=O)C(=O)* 0.000 description 1
- 206010003549 asthenia Diseases 0.000 description 1
- 230000037444 atrophy Effects 0.000 description 1
- SRBFZHDQGSBBOR-UHFFFAOYSA-N beta-D-Pyranose-Lyxose Natural products OC1COC(O)C(O)C1O SRBFZHDQGSBBOR-UHFFFAOYSA-N 0.000 description 1
- WQZGKKKJIJFFOK-FPRJBGLDSA-N beta-D-galactose Chemical compound OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@H]1O WQZGKKKJIJFFOK-FPRJBGLDSA-N 0.000 description 1
- 230000001588 bifunctional effect Effects 0.000 description 1
- 239000011230 binding agent Substances 0.000 description 1
- 230000000975 bioactive effect Effects 0.000 description 1
- 230000008827 biological function Effects 0.000 description 1
- 230000033228 biological regulation Effects 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- 210000001124 body fluid Anatomy 0.000 description 1
- 239000010839 body fluid Substances 0.000 description 1
- 229940098773 bovine serum albumin Drugs 0.000 description 1
- 210000004556 brain Anatomy 0.000 description 1
- 230000010261 cell growth Effects 0.000 description 1
- 239000013592 cell lysate Substances 0.000 description 1
- 230000036755 cellular response Effects 0.000 description 1
- 230000008859 change Effects 0.000 description 1
- 238000012512 characterization method Methods 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 238000004587 chromatography analysis Methods 0.000 description 1
- 239000003593 chromogenic compound Substances 0.000 description 1
- 210000000349 chromosome Anatomy 0.000 description 1
- 238000010367 cloning Methods 0.000 description 1
- 230000006957 competitive inhibition Effects 0.000 description 1
- 230000000295 complement effect Effects 0.000 description 1
- 230000004540 complement-dependent cytotoxicity Effects 0.000 description 1
- 239000000356 contaminant Substances 0.000 description 1
- 230000008878 coupling Effects 0.000 description 1
- 238000010168 coupling process Methods 0.000 description 1
- 238000005859 coupling reaction Methods 0.000 description 1
- 238000004132 cross linking Methods 0.000 description 1
- 239000013078 crystal Substances 0.000 description 1
- 230000006378 damage Effects 0.000 description 1
- 238000013480 data collection Methods 0.000 description 1
- 230000006240 deamidation Effects 0.000 description 1
- 230000007547 defect Effects 0.000 description 1
- 230000002950 deficient Effects 0.000 description 1
- 210000003074 dental pulp Anatomy 0.000 description 1
- 238000013461 design Methods 0.000 description 1
- 230000006866 deterioration Effects 0.000 description 1
- 230000001627 detrimental effect Effects 0.000 description 1
- 206010012601 diabetes mellitus Diseases 0.000 description 1
- LOKCTEFSRHRXRJ-UHFFFAOYSA-I dipotassium trisodium dihydrogen phosphate hydrogen phosphate dichloride Chemical compound P(=O)(O)(O)[O-].[K+].P(=O)(O)([O-])[O-].[Na+].[Na+].[Cl-].[K+].[Cl-].[Na+] LOKCTEFSRHRXRJ-UHFFFAOYSA-I 0.000 description 1
- 239000002270 dispersing agent Substances 0.000 description 1
- 238000002224 dissection Methods 0.000 description 1
- 238000004090 dissolution Methods 0.000 description 1
- 125000002228 disulfide group Chemical group 0.000 description 1
- 150000002019 disulfides Chemical class 0.000 description 1
- 238000004520 electroporation Methods 0.000 description 1
- 230000013020 embryo development Effects 0.000 description 1
- 210000003527 eukaryotic cell Anatomy 0.000 description 1
- 238000011156 evaluation Methods 0.000 description 1
- 230000000763 evoking effect Effects 0.000 description 1
- 230000001747 exhibiting effect Effects 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 230000002349 favourable effect Effects 0.000 description 1
- 238000001943 fluorescence-activated cell sorting Methods 0.000 description 1
- 238000004108 freeze drying Methods 0.000 description 1
- 229930182830 galactose Natural products 0.000 description 1
- BTCSSZJGUNDROE-UHFFFAOYSA-N gamma-aminobutyric acid Chemical compound NCCCC(O)=O BTCSSZJGUNDROE-UHFFFAOYSA-N 0.000 description 1
- 238000001502 gel electrophoresis Methods 0.000 description 1
- 239000011521 glass Substances 0.000 description 1
- 230000014101 glucose homeostasis Effects 0.000 description 1
- 150000002337 glycosamines Chemical group 0.000 description 1
- 210000002216 heart Anatomy 0.000 description 1
- 210000005003 heart tissue Anatomy 0.000 description 1
- 230000013632 homeostatic process Effects 0.000 description 1
- 102000057308 human HGF Human genes 0.000 description 1
- 210000005260 human cell Anatomy 0.000 description 1
- 125000002349 hydroxyamino group Chemical group [H]ON([H])[*] 0.000 description 1
- 238000010191 image analysis Methods 0.000 description 1
- 230000008105 immune reaction Effects 0.000 description 1
- 210000000987 immune system Anatomy 0.000 description 1
- 238000003018 immunoassay Methods 0.000 description 1
- 230000002998 immunogenetic effect Effects 0.000 description 1
- 230000016784 immunoglobulin production Effects 0.000 description 1
- 238000003364 immunohistochemistry Methods 0.000 description 1
- 238000001114 immunoprecipitation Methods 0.000 description 1
- 230000001771 impaired effect Effects 0.000 description 1
- 208000015181 infectious disease Diseases 0.000 description 1
- 239000003112 inhibitor Substances 0.000 description 1
- 208000014674 injury Diseases 0.000 description 1
- 239000007928 intraperitoneal injection Substances 0.000 description 1
- 150000002500 ions Chemical class 0.000 description 1
- 238000005304 joining Methods 0.000 description 1
- 210000003734 kidney Anatomy 0.000 description 1
- 238000002372 labelling Methods 0.000 description 1
- 238000004020 luminiscence type Methods 0.000 description 1
- HWYHZTIRURJOHG-UHFFFAOYSA-N luminol Chemical compound O=C1NNC(=O)C2=C1C(N)=CC=C2 HWYHZTIRURJOHG-UHFFFAOYSA-N 0.000 description 1
- 210000004072 lung Anatomy 0.000 description 1
- 210000001165 lymph node Anatomy 0.000 description 1
- 239000008176 lyophilized powder Substances 0.000 description 1
- 239000012139 lysis buffer Substances 0.000 description 1
- 229910052943 magnesium sulfate Inorganic materials 0.000 description 1
- 235000019341 magnesium sulphate Nutrition 0.000 description 1
- 210000001161 mammalian embryo Anatomy 0.000 description 1
- 239000011159 matrix material Substances 0.000 description 1
- 238000000691 measurement method Methods 0.000 description 1
- 210000003716 mesoderm Anatomy 0.000 description 1
- 108020004999 messenger RNA Proteins 0.000 description 1
- MYWUZJCMWCOHBA-VIFPVBQESA-N methamphetamine Chemical compound CN[C@@H](C)CC1=CC=CC=C1 MYWUZJCMWCOHBA-VIFPVBQESA-N 0.000 description 1
- 229920012128 methyl methacrylate acrylonitrile butadiene styrene Polymers 0.000 description 1
- 238000001823 molecular biology technique Methods 0.000 description 1
- 238000010369 molecular cloning Methods 0.000 description 1
- 230000000921 morphogenic effect Effects 0.000 description 1
- 229940126619 mouse monoclonal antibody Drugs 0.000 description 1
- 230000015604 muscle hyperplasia Effects 0.000 description 1
- 230000012042 muscle hypertrophy Effects 0.000 description 1
- 239000003471 mutagenic agent Substances 0.000 description 1
- 231100000707 mutagenic chemical Toxicity 0.000 description 1
- 210000003098 myoblast Anatomy 0.000 description 1
- ZTLGJPIZUOVDMT-UHFFFAOYSA-N n,n-dichlorotriazin-4-amine Chemical compound ClN(Cl)C1=CC=NN=N1 ZTLGJPIZUOVDMT-UHFFFAOYSA-N 0.000 description 1
- 101150091879 neo gene Proteins 0.000 description 1
- 230000001537 neural effect Effects 0.000 description 1
- 238000011275 oncology therapy Methods 0.000 description 1
- 230000003287 optical effect Effects 0.000 description 1
- 230000000399 orthopedic effect Effects 0.000 description 1
- 229940092253 ovalbumin Drugs 0.000 description 1
- 210000001672 ovary Anatomy 0.000 description 1
- 230000002018 overexpression Effects 0.000 description 1
- 230000001590 oxidative effect Effects 0.000 description 1
- 238000004806 packaging method and process Methods 0.000 description 1
- 210000000496 pancreas Anatomy 0.000 description 1
- 229940055729 papain Drugs 0.000 description 1
- 235000019834 papain Nutrition 0.000 description 1
- 238000007911 parenteral administration Methods 0.000 description 1
- 229940111202 pepsin Drugs 0.000 description 1
- 230000000737 periodic effect Effects 0.000 description 1
- 230000002093 peripheral effect Effects 0.000 description 1
- 108040007629 peroxidase activity proteins Proteins 0.000 description 1
- 230000000144 pharmacologic effect Effects 0.000 description 1
- 230000001766 physiological effect Effects 0.000 description 1
- 230000035790 physiological processes and functions Effects 0.000 description 1
- 239000002504 physiological saline solution Substances 0.000 description 1
- 239000004033 plastic Substances 0.000 description 1
- 229920003023 plastic Polymers 0.000 description 1
- 230000008488 polyadenylation Effects 0.000 description 1
- 229920001223 polyethylene glycol Polymers 0.000 description 1
- 229920000656 polylysine Polymers 0.000 description 1
- 230000004481 post-translational protein modification Effects 0.000 description 1
- 210000000229 preadipocyte Anatomy 0.000 description 1
- 238000001556 precipitation Methods 0.000 description 1
- 239000003755 preservative agent Substances 0.000 description 1
- 238000007639 printing Methods 0.000 description 1
- 210000001236 prokaryotic cell Anatomy 0.000 description 1
- 230000035755 proliferation Effects 0.000 description 1
- 238000011321 prophylaxis Methods 0.000 description 1
- 230000002797 proteolythic effect Effects 0.000 description 1
- 230000006337 proteolytic cleavage Effects 0.000 description 1
- 230000002685 pulmonary effect Effects 0.000 description 1
- 238000000746 purification Methods 0.000 description 1
- 210000003314 quadriceps muscle Anatomy 0.000 description 1
- 238000011002 quantification Methods 0.000 description 1
- 238000002708 random mutagenesis Methods 0.000 description 1
- 239000000376 reactant Substances 0.000 description 1
- 230000008707 rearrangement Effects 0.000 description 1
- 238000010188 recombinant method Methods 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 230000008929 regeneration Effects 0.000 description 1
- 238000011069 regeneration method Methods 0.000 description 1
- 230000022532 regulation of transcription, DNA-dependent Effects 0.000 description 1
- 230000000717 retained effect Effects 0.000 description 1
- 238000012552 review Methods 0.000 description 1
- 238000002702 ribosome display Methods 0.000 description 1
- 230000003248 secreting effect Effects 0.000 description 1
- 230000035945 sensitivity Effects 0.000 description 1
- 238000002864 sequence alignment Methods 0.000 description 1
- 238000013207 serial dilution Methods 0.000 description 1
- 208000002491 severe combined immunodeficiency Diseases 0.000 description 1
- 230000007781 signaling event Effects 0.000 description 1
- 230000025175 skeletal muscle hypertrophy Effects 0.000 description 1
- 230000004096 skeletal muscle tissue growth Effects 0.000 description 1
- 239000011734 sodium Substances 0.000 description 1
- 229910052708 sodium Inorganic materials 0.000 description 1
- 239000002904 solvent Substances 0.000 description 1
- 230000000392 somatic effect Effects 0.000 description 1
- 210000000278 spinal cord Anatomy 0.000 description 1
- 208000020431 spinal cord injury Diseases 0.000 description 1
- 230000006641 stabilisation Effects 0.000 description 1
- 238000011105 stabilization Methods 0.000 description 1
- 230000000638 stimulation Effects 0.000 description 1
- 210000002784 stomach Anatomy 0.000 description 1
- 238000010254 subcutaneous injection Methods 0.000 description 1
- 239000007929 subcutaneous injection Substances 0.000 description 1
- 235000000346 sugar Nutrition 0.000 description 1
- 239000000829 suppository Substances 0.000 description 1
- 238000002198 surface plasmon resonance spectroscopy Methods 0.000 description 1
- 238000001356 surgical procedure Methods 0.000 description 1
- 238000010408 sweeping Methods 0.000 description 1
- 230000002194 synthesizing effect Effects 0.000 description 1
- 230000002123 temporal effect Effects 0.000 description 1
- 229940124597 therapeutic agent Drugs 0.000 description 1
- 238000011287 therapeutic dose Methods 0.000 description 1
- 125000000341 threoninyl group Chemical group [H]OC([H])(C([H])([H])[H])C([H])(N([H])[H])C(*)=O 0.000 description 1
- 238000004448 titration Methods 0.000 description 1
- 230000000699 topical effect Effects 0.000 description 1
- 231100000331 toxic Toxicity 0.000 description 1
- 231100000816 toxic dose Toxicity 0.000 description 1
- 230000002588 toxic effect Effects 0.000 description 1
- 238000012546 transfer Methods 0.000 description 1
- 241000701447 unidentified baculovirus Species 0.000 description 1
- 210000002700 urine Anatomy 0.000 description 1
- 239000013603 viral vector Substances 0.000 description 1
- 230000003612 virological effect Effects 0.000 description 1
- 239000002699 waste material Substances 0.000 description 1
- 230000003442 weekly effect Effects 0.000 description 1
- 238000002424 x-ray crystallography Methods 0.000 description 1
- 210000005253 yeast cell Anatomy 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
- C07K16/22—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against growth factors ; against growth regulators
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K39/395—Antibodies; Immunoglobulins; Immune serum, e.g. antilymphocytic serum
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P1/00—Drugs for disorders of the alimentary tract or the digestive system
- A61P1/16—Drugs for disorders of the alimentary tract or the digestive system for liver or gallbladder disorders, e.g. hepatoprotective agents, cholagogues, litholytics
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P11/00—Drugs for disorders of the respiratory system
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P13/00—Drugs for disorders of the urinary system
- A61P13/12—Drugs for disorders of the urinary system of the kidneys
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P19/00—Drugs for skeletal disorders
- A61P19/08—Drugs for skeletal disorders for bone diseases, e.g. rachitism, Paget's disease
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P19/00—Drugs for skeletal disorders
- A61P19/08—Drugs for skeletal disorders for bone diseases, e.g. rachitism, Paget's disease
- A61P19/10—Drugs for skeletal disorders for bone diseases, e.g. rachitism, Paget's disease for osteoporosis
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P21/00—Drugs for disorders of the muscular or neuromuscular system
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P21/00—Drugs for disorders of the muscular or neuromuscular system
- A61P21/04—Drugs for disorders of the muscular or neuromuscular system for myasthenia gravis
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P3/00—Drugs for disorders of the metabolism
- A61P3/08—Drugs for disorders of the metabolism for glucose homeostasis
- A61P3/10—Drugs for disorders of the metabolism for glucose homeostasis for hyperglycaemia, e.g. antidiabetics
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P35/00—Antineoplastic agents
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P43/00—Drugs for specific purposes, not provided for in groups A61P1/00-A61P41/00
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K2039/505—Medicinal preparations containing antigens or antibodies comprising antibodies
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/20—Immunoglobulins specific features characterized by taxonomic origin
- C07K2317/24—Immunoglobulins specific features characterized by taxonomic origin containing regions, domains or residues from different species, e.g. chimeric, humanized or veneered
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
- C07K2317/55—Fab or Fab'
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/70—Immunoglobulins specific features characterized by effect upon binding to a cell or to an antigen
- C07K2317/76—Antagonist effect on antigen, e.g. neutralization or inhibition of binding
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/90—Immunoglobulins specific features characterized by (pharmaco)kinetic aspects or by stability of the immunoglobulin
- C07K2317/92—Affinity (KD), association rate (Ka), dissociation rate (Kd) or EC50 value
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y02—TECHNOLOGIES OR APPLICATIONS FOR MITIGATION OR ADAPTATION AGAINST CLIMATE CHANGE
- Y02P—CLIMATE CHANGE MITIGATION TECHNOLOGIES IN THE PRODUCTION OR PROCESSING OF GOODS
- Y02P20/00—Technologies relating to chemical industry
- Y02P20/50—Improvements relating to the production of bulk chemicals
- Y02P20/582—Recycling of unreacted starting or intermediate materials
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Medicinal Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- General Health & Medical Sciences (AREA)
- Veterinary Medicine (AREA)
- Public Health (AREA)
- Animal Behavior & Ethology (AREA)
- Pharmacology & Pharmacy (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Engineering & Computer Science (AREA)
- Physical Education & Sports Medicine (AREA)
- Orthopedic Medicine & Surgery (AREA)
- Immunology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Diabetes (AREA)
- Molecular Biology (AREA)
- Genetics & Genomics (AREA)
- Rheumatology (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- Neurology (AREA)
- Emergency Medicine (AREA)
- Endocrinology (AREA)
- Hematology (AREA)
- Obesity (AREA)
- Urology & Nephrology (AREA)
- Gastroenterology & Hepatology (AREA)
- Pulmonology (AREA)
- Microbiology (AREA)
- Mycology (AREA)
- Epidemiology (AREA)
- Peptides Or Proteins (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
Applications Claiming Priority (7)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US72467005P | 2005-10-06 | 2005-10-06 | |
| US60/724,670 | 2005-10-06 | ||
| US72523505P | 2005-10-11 | 2005-10-11 | |
| US60/725,235 | 2005-10-11 | ||
| US72606205P | 2005-10-12 | 2005-10-12 | |
| US60/726,062 | 2005-10-12 | ||
| PCT/US2006/038818 WO2007044411A2 (en) | 2005-10-06 | 2006-10-05 | Anti-myostatin antibodies |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| BRPI0616923A2 true BRPI0616923A2 (pt) | 2011-07-05 |
Family
ID=37943347
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| BRPI0616923-6A BRPI0616923A2 (pt) | 2005-10-06 | 2006-10-05 | anticorpos monoclonais, seus usos e composição farmacêutica |
Country Status (13)
| Country | Link |
|---|---|
| US (2) | US7635760B2 (enExample) |
| EP (1) | EP1951756B1 (enExample) |
| JP (1) | JP5052517B2 (enExample) |
| KR (1) | KR101135220B1 (enExample) |
| CN (1) | CN101277976B (enExample) |
| AU (1) | AU2006302494B2 (enExample) |
| BR (1) | BRPI0616923A2 (enExample) |
| CA (1) | CA2624976A1 (enExample) |
| EA (1) | EA015589B1 (enExample) |
| ES (1) | ES2533464T3 (enExample) |
| IL (1) | IL189579A0 (enExample) |
| NO (1) | NO20082073L (enExample) |
| WO (1) | WO2007044411A2 (enExample) |
Families Citing this family (44)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| ES2533464T3 (es) | 2005-10-06 | 2015-04-10 | Eli Lilly And Company | Anticuerpos anti-miostatina |
| UA92504C2 (en) | 2005-10-12 | 2010-11-10 | Эли Лилли Энд Компани | Anti-myostatin monoclonal antibody |
| CA2647846C (en) | 2006-03-31 | 2016-06-21 | Chugai Seiyaku Kabushiki Kaisha | Methods for controlling blood pharmacokinetics of antibodies |
| KR101123531B1 (ko) * | 2006-09-05 | 2012-04-20 | 일라이 릴리 앤드 캄파니 | 항-마이오스타틴 항체 |
| EP2478905B1 (en) | 2007-06-01 | 2014-05-14 | Wyeth LLC | Treatment of imatinib resistant leukemia using 4-aminoquinoline-3-carbonitriles |
| CN106519025B (zh) | 2007-09-26 | 2021-04-23 | 中外制药株式会社 | 利用cdr的氨基酸取代来改变抗体等电点的方法 |
| KR100857861B1 (ko) * | 2007-10-15 | 2008-09-11 | 주식회사 바이오리더스 | Ｍｙｏ－２ 펩타이드 중합체와 마이오스타틴의 융합단백질표면발현용 벡터 및 상기 벡터로 형질전환된 미생물 |
| PE20091163A1 (es) * | 2007-11-01 | 2009-08-09 | Wyeth Corp | Anticuerpos para gdf8 |
| CA2721052C (en) | 2008-04-11 | 2023-02-21 | Chugai Seiyaku Kabushiki Kaisha | Antigen-binding molecule capable of binding to two or more antigen molecules repeatedly |
| WO2010027797A1 (en) * | 2008-08-26 | 2010-03-11 | Macrogenics Inc. | T-cell receptor antibodies and methods of use thereof |
| TW201029662A (en) | 2008-12-19 | 2010-08-16 | Glaxo Group Ltd | Novel antigen binding proteins |
| JO3340B1 (ar) * | 2010-05-26 | 2019-03-13 | Regeneron Pharma | مضادات حيوية لـعامل تمايز النمو 8 البشري |
| TW201210612A (en) | 2010-06-03 | 2012-03-16 | Glaxo Group Ltd | Humanised antigen binding proteins |
| KR20140005864A (ko) | 2010-08-16 | 2014-01-15 | 암젠 인코퍼레이티드 | 미오스타틴에 결합하는 항체, 조성물 및 방법 |
| AR082641A1 (es) | 2010-09-07 | 2012-12-19 | Imclone Llc | Composiciones de anticuerpo anti-vegfr-3 |
| BR112013013354A2 (pt) | 2010-11-30 | 2020-10-06 | Chugai Seiyaku Kabushiki Kaisha | molécula de ligação ao antígeno capaz de se ligar a uma pluralidade de moléculas de antígeno repetidamente |
| CN102212545B (zh) * | 2011-04-07 | 2013-05-08 | 北京济福霖生物技术有限公司 | 利用锌指核酸酶敲除牛β-乳球蛋白基因的方法 |
| CN102260711B (zh) * | 2011-06-24 | 2013-09-18 | 北京济福霖生物技术有限公司 | 利用锌指核酸酶敲除牛肌肉抑制素基因的方法 |
| SI2780368T1 (en) | 2011-11-14 | 2018-04-30 | Regeneron Pharmaceuticals, Inc. | INGREDIENTS AND PROCEDURES FOR INCREASING PURE MASS AND MICROWAVE WITH SPECIFIC ANTAGONISING OF GDF8 AND / OR ACTIVITY A |
| CN102660577B (zh) * | 2012-04-18 | 2013-12-25 | 山东省农业科学院奶牛研究中心 | 利用锌指核酸酶敲除牛整合素β6亚基基因的方法 |
| JP6501521B2 (ja) | 2012-08-24 | 2019-04-17 | 中外製薬株式会社 | ＦｃγＲＩＩｂ特異的Ｆｃ領域改変体 |
| JP6774164B2 (ja) | 2012-08-24 | 2020-10-21 | 中外製薬株式会社 | マウスＦｃγＲＩＩ特異的Ｆｃ抗体 |
| PL3835310T3 (pl) | 2012-09-13 | 2024-06-03 | Bristol-Myers Squibb Company | Białka domeny rusztowania oparte na fibronektynie wiążące się z miostatyną |
| JPWO2014119634A1 (ja) * | 2013-01-30 | 2017-01-26 | 国立研究開発法人国立精神・神経医療研究センター | 筋増加剤及びそれを含む医薬組成物 |
| CA2908350C (en) | 2013-04-02 | 2023-08-08 | Futa Mimoto | Fc region variant |
| AU2014262843B2 (en) | 2013-05-06 | 2017-06-22 | Scholar Rock, Inc. | Compositions and methods for growth factor modulation |
| TWI655207B (zh) | 2013-07-30 | 2019-04-01 | 再生元醫藥公司 | 抗活化素ａ之抗體及其用途 |
| CN107073088A (zh) * | 2014-03-19 | 2017-08-18 | 台湾基督长老教会马偕医疗财团法人马偕纪念医院 | 免疫原性糖肽、包含所述糖肽的组合物及其用途 |
| EP2960653A1 (en) * | 2014-06-24 | 2015-12-30 | Stichting Kwaliteitsgarantie Vleeskalversector | Diagnostic kit and method for the identification of the manipulation of muscle mass in a domestic animal |
| HK1243940A1 (zh) | 2014-11-06 | 2018-07-27 | Scholar Rock, Inc. | 抗原肌肉生长抑制素/潜在肌肉生长抑制素的抗体及其用途 |
| MY181199A (en) | 2014-12-19 | 2020-12-21 | Chugai Pharmaceutical Co Ltd | Anti-myostatin antibodies, polypeptides containing variant fc regions, and methods of use |
| CN107108729A (zh) | 2015-02-05 | 2017-08-29 | 中外制药株式会社 | 包含离子浓度依赖性的抗原结合结构域的抗体，fc区变体，il‑8‑结合抗体，及其应用 |
| IL255010B2 (en) | 2015-04-15 | 2024-01-01 | Regeneron Pharma | Methods of increasing strength and functionality with gdf8 inhibitors |
| SMT202500263T1 (it) | 2015-09-15 | 2025-09-12 | Scholar Rock Inc | Anticorpi anti-pro-miostatina/miostatina latente e loro usi |
| WO2017110981A1 (en) * | 2015-12-25 | 2017-06-29 | Chugai Seiyaku Kabushiki Kaisha | Anti-myostatin antibodies and methods of use |
| KR20180094110A (ko) | 2016-01-08 | 2018-08-22 | 스칼러 락, 인크. | 항-프로/잠재성 미오스타틴 항체 및 그의 사용 방법 |
| JP6527643B2 (ja) | 2016-08-05 | 2019-06-05 | 中外製薬株式会社 | Ｉｌ−８関連疾患の治療用又は予防用組成物 |
| DK3565592T5 (da) | 2017-01-06 | 2024-09-02 | Scholar Rock Inc | Behandling af stofskiftesygdomme ved inhibering af myostatinaktivering |
| WO2018162931A1 (en) * | 2017-03-10 | 2018-09-13 | Ucl Business Plc | Method relating to myostatin pathway inhibition |
| AU2019226551B2 (en) | 2018-03-01 | 2025-02-06 | Regeneron Pharmaceuticals, Inc. | Methods for altering body composition |
| CA3094400A1 (en) | 2018-04-06 | 2019-10-10 | Regeneron Pharmaceuticals, Inc. | A leptin receptor agonist antibody for use in treating a metabolic dysfunction or hypoleptinemia |
| MX2021007394A (es) | 2018-12-18 | 2021-07-15 | Regeneron Pharma | Composiciones y metodos para aumentar el peso corporal y la masa muscular magra mediante el uso de antagonistas contra el receptor de leptina, gdf8 y activina a. |
| EP4590698A1 (en) | 2022-09-21 | 2025-07-30 | Regeneron Pharmaceuticals, Inc. | Methods of treating obesity, diabetes, and liver dysfunction |
| TW202430247A (zh) | 2022-12-22 | 2024-08-01 | 美商供石公司 | 肌肉生長抑制素活化之選擇性及強效抑制劑 |
Family Cites Families (35)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US7393682B1 (en) | 1993-03-19 | 2008-07-01 | The Johns Hopkins University School Of Medicine | Polynucleotides encoding promyostatin polypeptides |
| ES2201076T3 (es) * | 1993-03-19 | 2004-03-16 | The Johns Hopkins University School Of Medicine | Factor-8 de diferenciacion del crecimiento. |
| US5994618A (en) * | 1997-02-05 | 1999-11-30 | Johns Hopkins University School Of Medicine | Growth differentiation factor-8 transgenic mice |
| EP0698094B1 (en) * | 1993-05-12 | 2004-02-04 | Genetics Institute, LLC | Bmp-11 compositions |
| DK0776337T3 (da) | 1994-07-08 | 2005-12-12 | Univ Johns Hopkins Med | Vækstdifferentieringsfaktor-11 |
| US6008434A (en) * | 1994-07-08 | 1999-12-28 | Johns Hopkins University School Of Medicine | Growth differentiation factor-11 transgenic mice |
| US6696260B1 (en) * | 1997-08-01 | 2004-02-24 | The Johns Hopkins University School Of Medicine | Methods to identify growth differentiation factor (GDF) binding proteins |
| US6656475B1 (en) * | 1997-08-01 | 2003-12-02 | The Johns Hopkins University School Of Medicine | Growth differentiation factor receptors, agonists and antagonists thereof, and methods of using same |
| WO1999006559A1 (en) | 1997-08-01 | 1999-02-11 | The Johns Hopkins University School Of Medicine | Methods to identify growth differentiation factor (gdf) receptors |
| AU1276399A (en) | 1997-11-07 | 1999-05-31 | Genetics Institute Inc. | Neuronal uses of bmp-11 |
| GB2333706A (en) | 1998-02-02 | 1999-08-04 | Merck & Co Inc | Method for increasing muscle mass in animals |
| WO1999040181A1 (en) | 1998-02-05 | 1999-08-12 | The Johns Hopkins University School Of Medicine | Growth differentiation factor-8 |
| US6368597B1 (en) * | 1998-05-06 | 2002-04-09 | Matamorphix, Inc. | Methods of treating diabetes |
| US7504490B1 (en) * | 1998-10-16 | 2009-03-17 | Oscient Pharmaceuticals Corporation | Nucleic acid and amino acid sequences relating to Apergillus fumigatus for diagnostics and therapeutics |
| ATE322681T1 (de) | 1999-01-21 | 2006-04-15 | Metamorphix Inc | Inhibitoren für wachstumdifferenzierungsfaktor und ihre anwendungen |
| US7320789B2 (en) | 2001-09-26 | 2008-01-22 | Wyeth | Antibody inhibitors of GDF-8 and uses thereof |
| BR0314270A (pt) * | 2002-09-16 | 2005-08-02 | Univ Johns Hopkins | Ativação de miostatina com metaloprotease e processos de modulação da atividade da miostatina |
| US7261893B2 (en) * | 2002-10-22 | 2007-08-28 | Wyeth | Neutralizing antibodies against GDF-8 and uses therefor |
| EA009056B1 (ru) * | 2002-12-20 | 2007-10-26 | Амген, Инк. | Связывающие агенты, ингибирующие миостатин |
| JP5110877B2 (ja) * | 2003-06-02 | 2012-12-26 | ワイス・エルエルシー | 神経筋障害を処置するための、コルチコステロイドと組み合わせたミオスタチン（ｇｄｆ８）インヒビターの使用 |
| NZ529860A (en) * | 2003-11-28 | 2006-10-27 | Ovita Ltd | Muscle growth regulator mighty and use in promoting muscle mass and treating muscle wasting diseases |
| AU2004312411B8 (en) * | 2003-12-31 | 2011-11-24 | Schering-Plough Pty. Limited | Neutralizing epitope-based growth enhancing vaccine |
| JP4695133B2 (ja) * | 2004-03-23 | 2011-06-08 | イーライ リリー アンド カンパニー | 抗ミオスタチン抗体 |
| US20060034831A1 (en) * | 2004-08-12 | 2006-02-16 | Wyeth | Combination therapy for diabetes, obesity and cardiovascular diseases using GDF-8 inhibitors |
| NZ538097A (en) * | 2005-02-07 | 2006-07-28 | Ovita Ltd | Method and compositions for improving wound healing |
| AU2006226878A1 (en) * | 2005-03-23 | 2006-09-28 | Wyeth | Detection of GDF-8 modulating agents |
| AU2006239860B2 (en) * | 2005-04-25 | 2012-01-19 | Amgen Fremont Inc. | Antibodies to myostatin |
| US20090215671A1 (en) * | 2005-05-27 | 2009-08-27 | The Regents Of The University Of California | Compositions And Methods For Treatment of Neural Disorders Using Transforming Growth Factor-Beta Superfamily Proteins And Their Antagonists |
| EP3327033A1 (en) * | 2005-08-19 | 2018-05-30 | Wyeth LLC | Antagonist antibodies against gdf-8 and uses in treatment of als and other gdf-8-associated disorders |
| ES2533464T3 (es) * | 2005-10-06 | 2015-04-10 | Eli Lilly And Company | Anticuerpos anti-miostatina |
| UA92504C2 (en) * | 2005-10-12 | 2010-11-10 | Эли Лилли Энд Компани | Anti-myostatin monoclonal antibody |
| AU2006321906C1 (en) * | 2005-12-06 | 2014-01-16 | Amgen Inc. | Uses of myostatin antagonists |
| US20070190056A1 (en) * | 2006-02-07 | 2007-08-16 | Ravi Kambadur | Muscle regeneration compositions and uses therefor |
| KR101123531B1 (ko) | 2006-09-05 | 2012-04-20 | 일라이 릴리 앤드 캄파니 | 항-마이오스타틴 항체 |
| TW201718635A (zh) | 2007-03-06 | 2017-06-01 | 安美基公司 | 變異之活動素受體多肽及其用途 |
-
2006
- 2006-10-05 ES ES06816226.2T patent/ES2533464T3/es active Active
- 2006-10-05 EP EP06816226.2A patent/EP1951756B1/en active Active
- 2006-10-05 JP JP2008534657A patent/JP5052517B2/ja not_active Expired - Fee Related
- 2006-10-05 EA EA200801027A patent/EA015589B1/ru not_active IP Right Cessation
- 2006-10-05 AU AU2006302494A patent/AU2006302494B2/en not_active Ceased
- 2006-10-05 CN CN2006800368248A patent/CN101277976B/zh not_active Expired - Fee Related
- 2006-10-05 KR KR1020087008254A patent/KR101135220B1/ko not_active Expired - Fee Related
- 2006-10-05 CA CA002624976A patent/CA2624976A1/en not_active Abandoned
- 2006-10-05 US US12/066,664 patent/US7635760B2/en not_active Expired - Fee Related
- 2006-10-05 BR BRPI0616923-6A patent/BRPI0616923A2/pt not_active IP Right Cessation
- 2006-10-05 WO PCT/US2006/038818 patent/WO2007044411A2/en not_active Ceased
-
2008
- 2008-02-18 IL IL189579A patent/IL189579A0/en unknown
- 2008-05-02 NO NO20082073A patent/NO20082073L/no not_active Application Discontinuation
-
2009
- 2009-11-04 US US12/612,060 patent/US7745583B2/en not_active Expired - Fee Related
Also Published As
| Publication number | Publication date |
|---|---|
| KR20080045733A (ko) | 2008-05-23 |
| WO2007044411A3 (en) | 2007-08-16 |
| JP2009511480A (ja) | 2009-03-19 |
| US20100087631A1 (en) | 2010-04-08 |
| EP1951756B1 (en) | 2015-01-07 |
| NO20082073L (no) | 2008-06-17 |
| US7745583B2 (en) | 2010-06-29 |
| EP1951756A2 (en) | 2008-08-06 |
| WO2007044411A2 (en) | 2007-04-19 |
| ES2533464T3 (es) | 2015-04-10 |
| CA2624976A1 (en) | 2007-04-19 |
| CN101277976B (zh) | 2012-04-11 |
| CN101277976A (zh) | 2008-10-01 |
| EA015589B1 (ru) | 2011-10-31 |
| EA200801027A1 (ru) | 2008-10-30 |
| AU2006302494A1 (en) | 2007-04-19 |
| AU2006302494B2 (en) | 2011-01-06 |
| US20080299126A1 (en) | 2008-12-04 |
| JP5052517B2 (ja) | 2012-10-17 |
| KR101135220B1 (ko) | 2012-04-24 |
| US7635760B2 (en) | 2009-12-22 |
| IL189579A0 (en) | 2008-08-07 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| US7745583B2 (en) | Anti-myostatin antibodies | |
| US8066995B2 (en) | Anti-myostatin antibodies | |
| CN101326195B (zh) | 抗il-17抗体 | |
| JP2009519348A5 (enExample) | ||
| HK1118564B (en) | Anti-myostatin antibodies |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| B06F | Objections, documents and/or translations needed after an examination request according [chapter 6.6 patent gazette] | ||
| B06H | Technical and formal requirements: requirement cancelled [chapter 6.8 patent gazette] |
Free format text: REF. A RPI NO 2154 DE 17/04/2012. ANULACAO DA EXIGENCIA 6.6 POR TER SIDO INDEVIDA. REQUERENTE NAO APRESENTOU RESPOSTA A EXIGENCIA CONFORME DISPOE A RESOLUCAO 207 DE 24/04/2009, ENTRETANTO, A RESPOSTA CONSTA NO FORMULARIO DE DEPOSITO. |
|
| B07D | Technical examination (opinion) related to article 229 of industrial property law [chapter 7.4 patent gazette] | ||
| B08F | Application dismissed because of non-payment of annual fees [chapter 8.6 patent gazette] |
Free format text: REFERENTE AS 8A E 9A ANUIDADES. |
|
| B08K | Patent lapsed as no evidence of payment of the annual fee has been furnished to inpi [chapter 8.11 patent gazette] |
Free format text: EM VIRTUDE DO ARQUIVAMENTO PUBLICADO NA RPI 2343 DE 01-12-2015 E CONSIDERANDO AUSENCIA DE MANIFESTACAO DENTRO DOS PRAZOS LEGAIS, INFORMO QUE CABE SER MANTIDO O ARQUIVAMENTO DO PEDIDO DE PATENTE, CONFORME O DISPOSTO NO ARTIGO 12, DA RESOLUCAO 113/2013. |