AU2008295449A1 - Agents with angiogenic and wound healing activity - Google Patents
Agents with angiogenic and wound healing activity Download PDFInfo
- Publication number
- AU2008295449A1 AU2008295449A1 AU2008295449A AU2008295449A AU2008295449A1 AU 2008295449 A1 AU2008295449 A1 AU 2008295449A1 AU 2008295449 A AU2008295449 A AU 2008295449A AU 2008295449 A AU2008295449 A AU 2008295449A AU 2008295449 A1 AU2008295449 A1 AU 2008295449A1
- Authority
- AU
- Australia
- Prior art keywords
- crystallin
- protein
- wound
- lens
- eye
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Abandoned
Links
- 230000002491 angiogenic effect Effects 0.000 title claims description 50
- 230000029663 wound healing Effects 0.000 title description 60
- 230000000694 effects Effects 0.000 title description 45
- 108090000623 proteins and genes Proteins 0.000 claims description 294
- 102000004169 proteins and genes Human genes 0.000 claims description 290
- 241000283690 Bos taurus Species 0.000 claims description 107
- 238000000034 method Methods 0.000 claims description 63
- 241001465754 Metazoa Species 0.000 claims description 53
- 108010067372 Pancreatic elastase Proteins 0.000 claims description 38
- 102000016387 Pancreatic elastase Human genes 0.000 claims description 38
- 230000033115 angiogenesis Effects 0.000 claims description 37
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims description 36
- 239000002904 solvent Substances 0.000 claims description 26
- 210000002889 endothelial cell Anatomy 0.000 claims description 25
- 239000000203 mixture Substances 0.000 claims description 21
- 239000012634 fragment Substances 0.000 claims description 19
- 108091005804 Peptidases Proteins 0.000 claims description 18
- 239000004365 Protease Substances 0.000 claims description 18
- 230000001737 promoting effect Effects 0.000 claims description 18
- 238000000746 purification Methods 0.000 claims description 18
- 239000002244 precipitate Substances 0.000 claims description 15
- 238000013508 migration Methods 0.000 claims description 14
- 230000004663 cell proliferation Effects 0.000 claims description 13
- 230000012292 cell migration Effects 0.000 claims description 10
- 239000008194 pharmaceutical composition Substances 0.000 claims description 10
- 238000003776 cleavage reaction Methods 0.000 claims description 8
- 230000007017 scission Effects 0.000 claims description 8
- 239000003937 drug carrier Substances 0.000 claims description 5
- 238000003825 pressing Methods 0.000 claims description 5
- BHPQYMZQTOCNFJ-UHFFFAOYSA-N Calcium cation Chemical compound [Ca+2] BHPQYMZQTOCNFJ-UHFFFAOYSA-N 0.000 claims description 4
- 229910001424 calcium ion Inorganic materials 0.000 claims description 4
- 210000004087 cornea Anatomy 0.000 claims description 4
- 210000001747 pupil Anatomy 0.000 claims description 4
- 150000003839 salts Chemical class 0.000 claims description 4
- 210000003786 sclera Anatomy 0.000 claims description 3
- 239000003125 aqueous solvent Substances 0.000 claims description 2
- 238000013375 chromatographic separation Methods 0.000 claims description 2
- 102000038379 digestive enzymes Human genes 0.000 claims description 2
- 108091007734 digestive enzymes Proteins 0.000 claims description 2
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 claims 1
- 235000018102 proteins Nutrition 0.000 description 260
- 206010052428 Wound Diseases 0.000 description 210
- 208000027418 Wounds and injury Diseases 0.000 description 209
- 239000000284 extract Substances 0.000 description 66
- 210000001508 eye Anatomy 0.000 description 52
- 239000000499 gel Substances 0.000 description 49
- 102000014824 Crystallins Human genes 0.000 description 47
- 108010064003 Crystallins Proteins 0.000 description 47
- 210000001519 tissue Anatomy 0.000 description 43
- 238000011282 treatment Methods 0.000 description 39
- 238000004458 analytical method Methods 0.000 description 38
- 210000004027 cell Anatomy 0.000 description 36
- 239000000523 sample Substances 0.000 description 36
- 241000700159 Rattus Species 0.000 description 34
- 235000001014 amino acid Nutrition 0.000 description 28
- 238000004007 reversed phase HPLC Methods 0.000 description 27
- 150000001413 amino acids Chemical class 0.000 description 25
- 238000002360 preparation method Methods 0.000 description 23
- 210000003491 skin Anatomy 0.000 description 22
- 230000035876 healing Effects 0.000 description 21
- 108090000765 processed proteins & peptides Proteins 0.000 description 21
- 230000000302 ischemic effect Effects 0.000 description 20
- 238000012360 testing method Methods 0.000 description 20
- 102000006639 indoleamine 2,3-dioxygenase Human genes 0.000 description 19
- 108020004201 indoleamine 2,3-dioxygenase Proteins 0.000 description 19
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 18
- 238000003556 assay Methods 0.000 description 18
- 230000000638 stimulation Effects 0.000 description 18
- 102000035195 Peptidases Human genes 0.000 description 17
- QTBSBXVTEAMEQO-UHFFFAOYSA-N acetic acid Substances CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 17
- 125000003275 alpha amino acid group Chemical group 0.000 description 17
- WSFSSNUMVMOOMR-UHFFFAOYSA-N Formaldehyde Chemical compound O=C WSFSSNUMVMOOMR-UHFFFAOYSA-N 0.000 description 16
- 210000004379 membrane Anatomy 0.000 description 16
- 239000012528 membrane Substances 0.000 description 16
- 239000002953 phosphate buffered saline Substances 0.000 description 16
- 102000004196 processed proteins & peptides Human genes 0.000 description 16
- WEVYAHXRMPXWCK-UHFFFAOYSA-N Acetonitrile Chemical compound CC#N WEVYAHXRMPXWCK-UHFFFAOYSA-N 0.000 description 15
- 108010067787 Proteoglycans Proteins 0.000 description 15
- 102000016611 Proteoglycans Human genes 0.000 description 15
- 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 15
- 238000010828 elution Methods 0.000 description 15
- 239000000463 material Substances 0.000 description 15
- 238000002523 gelfiltration Methods 0.000 description 14
- 230000010595 endothelial cell migration Effects 0.000 description 13
- 210000004088 microvessel Anatomy 0.000 description 13
- 239000000243 solution Substances 0.000 description 13
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 12
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 12
- 108010007908 alpha-Crystallins Proteins 0.000 description 12
- 102000007362 alpha-Crystallins Human genes 0.000 description 12
- 210000000709 aorta Anatomy 0.000 description 12
- 239000000539 dimer Substances 0.000 description 12
- 239000012153 distilled water Substances 0.000 description 12
- 238000005194 fractionation Methods 0.000 description 12
- 230000004048 modification Effects 0.000 description 12
- 238000012986 modification Methods 0.000 description 12
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 12
- 102000005789 Vascular Endothelial Growth Factors Human genes 0.000 description 11
- 108010019530 Vascular Endothelial Growth Factors Proteins 0.000 description 11
- 230000037396 body weight Effects 0.000 description 11
- 239000003981 vehicle Substances 0.000 description 11
- 239000012506 Sephacryl® Substances 0.000 description 10
- XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 description 10
- 239000000706 filtrate Substances 0.000 description 10
- 102000013069 gamma-Crystallins Human genes 0.000 description 10
- 108010079934 gamma-Crystallins Proteins 0.000 description 10
- 239000013641 positive control Substances 0.000 description 10
- 238000000692 Student's t-test Methods 0.000 description 9
- 210000004899 c-terminal region Anatomy 0.000 description 9
- 239000004744 fabric Substances 0.000 description 9
- 210000003205 muscle Anatomy 0.000 description 9
- 230000026731 phosphorylation Effects 0.000 description 9
- 238000006366 phosphorylation reaction Methods 0.000 description 9
- 230000004481 post-translational protein modification Effects 0.000 description 9
- 230000008569 process Effects 0.000 description 9
- 239000006228 supernatant Substances 0.000 description 9
- 244000144927 Aloe barbadensis Species 0.000 description 8
- 235000002961 Aloe barbadensis Nutrition 0.000 description 8
- 239000006144 Dulbecco’s modified Eagle's medium Substances 0.000 description 8
- 108090000631 Trypsin Proteins 0.000 description 8
- 102000004142 Trypsin Human genes 0.000 description 8
- 235000011399 aloe vera Nutrition 0.000 description 8
- 230000008901 benefit Effects 0.000 description 8
- 108010070654 beta-Crystallins Proteins 0.000 description 8
- 102000005735 beta-Crystallins Human genes 0.000 description 8
- 238000001574 biopsy Methods 0.000 description 8
- 239000003795 chemical substances by application Substances 0.000 description 8
- 239000011780 sodium chloride Substances 0.000 description 8
- 230000004936 stimulating effect Effects 0.000 description 8
- 239000012588 trypsin Substances 0.000 description 8
- 102000004190 Enzymes Human genes 0.000 description 7
- 108090000790 Enzymes Proteins 0.000 description 7
- QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 description 7
- 102000005431 Molecular Chaperones Human genes 0.000 description 7
- 108010006519 Molecular Chaperones Proteins 0.000 description 7
- 230000002378 acidificating effect Effects 0.000 description 7
- 230000015572 biosynthetic process Effects 0.000 description 7
- 239000000872 buffer Substances 0.000 description 7
- 229910002091 carbon monoxide Inorganic materials 0.000 description 7
- 230000003111 delayed effect Effects 0.000 description 7
- 239000003814 drug Substances 0.000 description 7
- 229940088598 enzyme Drugs 0.000 description 7
- 238000009472 formulation Methods 0.000 description 7
- 238000001641 gel filtration chromatography Methods 0.000 description 7
- 230000005012 migration Effects 0.000 description 7
- 239000012465 retentate Substances 0.000 description 7
- 210000003625 skull Anatomy 0.000 description 7
- 238000006467 substitution reaction Methods 0.000 description 7
- 238000012353 t test Methods 0.000 description 7
- 229920002271 DEAE-Sepharose Polymers 0.000 description 6
- IAZDPXIOMUYVGZ-UHFFFAOYSA-N Dimethylsulphoxide Chemical compound CS(C)=O IAZDPXIOMUYVGZ-UHFFFAOYSA-N 0.000 description 6
- 102000016680 Dioxygenases Human genes 0.000 description 6
- 108010028143 Dioxygenases Proteins 0.000 description 6
- 229960000583 acetic acid Drugs 0.000 description 6
- 239000011575 calcium Substances 0.000 description 6
- 230000015556 catabolic process Effects 0.000 description 6
- 238000005119 centrifugation Methods 0.000 description 6
- 230000029087 digestion Effects 0.000 description 6
- 239000012909 foetal bovine serum Substances 0.000 description 6
- 230000005764 inhibitory process Effects 0.000 description 6
- 239000002609 medium Substances 0.000 description 6
- 230000036961 partial effect Effects 0.000 description 6
- 230000004044 response Effects 0.000 description 6
- QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 description 5
- OYPRJOBELJOOCE-UHFFFAOYSA-N Calcium Chemical compound [Ca] OYPRJOBELJOOCE-UHFFFAOYSA-N 0.000 description 5
- 108090000317 Chymotrypsin Proteins 0.000 description 5
- 102000008186 Collagen Human genes 0.000 description 5
- 108010035532 Collagen Proteins 0.000 description 5
- 239000012981 Hank's balanced salt solution Substances 0.000 description 5
- KDXKERNSBIXSRK-YFKPBYRVSA-N L-lysine Chemical compound NCCCC[C@H](N)C(O)=O KDXKERNSBIXSRK-YFKPBYRVSA-N 0.000 description 5
- 238000002835 absorbance Methods 0.000 description 5
- 108010051585 alpha-Crystallin B Chain Proteins 0.000 description 5
- 210000004204 blood vessel Anatomy 0.000 description 5
- 229910052791 calcium Inorganic materials 0.000 description 5
- 239000004202 carbamide Substances 0.000 description 5
- 230000001684 chronic effect Effects 0.000 description 5
- 229960002376 chymotrypsin Drugs 0.000 description 5
- 229920001436 collagen Polymers 0.000 description 5
- 238000000605 extraction Methods 0.000 description 5
- 239000011521 glass Substances 0.000 description 5
- 230000036541 health Effects 0.000 description 5
- 210000002216 heart Anatomy 0.000 description 5
- 238000000338 in vitro Methods 0.000 description 5
- 238000002955 isolation Methods 0.000 description 5
- 239000001301 oxygen Substances 0.000 description 5
- 229910052760 oxygen Inorganic materials 0.000 description 5
- 229910052698 phosphorus Inorganic materials 0.000 description 5
- 230000012846 protein folding Effects 0.000 description 5
- 210000001525 retina Anatomy 0.000 description 5
- 238000000926 separation method Methods 0.000 description 5
- 230000008961 swelling Effects 0.000 description 5
- 238000000108 ultra-filtration Methods 0.000 description 5
- NGGMYCMLYOUNGM-UHFFFAOYSA-N (-)-fumagillin Natural products O1C(CC=C(C)C)C1(C)C1C(OC)C(OC(=O)C=CC=CC=CC=CC(O)=O)CCC21CO2 NGGMYCMLYOUNGM-UHFFFAOYSA-N 0.000 description 4
- 240000000560 Citrus x paradisi Species 0.000 description 4
- 108010049003 Fibrinogen Proteins 0.000 description 4
- 102000008946 Fibrinogen Human genes 0.000 description 4
- 206010021143 Hypoxia Diseases 0.000 description 4
- 206010061218 Inflammation Diseases 0.000 description 4
- 241000699666 Mus <mouse, genus> Species 0.000 description 4
- IDIDJDIHTAOVLG-VKHMYHEASA-N S-methylcysteine Chemical compound CSC[C@H](N)C(O)=O IDIDJDIHTAOVLG-VKHMYHEASA-N 0.000 description 4
- 241000251539 Vertebrata <Metazoa> Species 0.000 description 4
- 108010055905 alpha-Crystallin A Chain Proteins 0.000 description 4
- 102000013640 alpha-Crystallin B Chain Human genes 0.000 description 4
- 238000000540 analysis of variance Methods 0.000 description 4
- QVGXLLKOCUKJST-UHFFFAOYSA-N atomic oxygen Chemical compound [O] QVGXLLKOCUKJST-UHFFFAOYSA-N 0.000 description 4
- 230000035578 autophosphorylation Effects 0.000 description 4
- 238000004587 chromatography analysis Methods 0.000 description 4
- 150000001875 compounds Chemical class 0.000 description 4
- 239000013256 coordination polymer Substances 0.000 description 4
- 238000006731 degradation reaction Methods 0.000 description 4
- 230000001419 dependent effect Effects 0.000 description 4
- 231100000673 dose–response relationship Toxicity 0.000 description 4
- 229940012952 fibrinogen Drugs 0.000 description 4
- NGGMYCMLYOUNGM-CSDLUJIJSA-N fumagillin Chemical compound C([C@H]([C@H]([C@@H]1[C@]2(C)[C@H](O2)CC=C(C)C)OC)OC(=O)\C=C\C=C\C=C\C=C\C(O)=O)C[C@@]21CO2 NGGMYCMLYOUNGM-CSDLUJIJSA-N 0.000 description 4
- 229960000936 fumagillin Drugs 0.000 description 4
- 102000037865 fusion proteins Human genes 0.000 description 4
- 108020001507 fusion proteins Proteins 0.000 description 4
- 238000010438 heat treatment Methods 0.000 description 4
- 230000002757 inflammatory effect Effects 0.000 description 4
- 230000004054 inflammatory process Effects 0.000 description 4
- 230000002401 inhibitory effect Effects 0.000 description 4
- 210000000440 neutrophil Anatomy 0.000 description 4
- 150000007523 nucleic acids Chemical group 0.000 description 4
- 239000012188 paraffin wax Substances 0.000 description 4
- 239000008188 pellet Substances 0.000 description 4
- 229920000729 poly(L-lysine) polymer Polymers 0.000 description 4
- 239000000843 powder Substances 0.000 description 4
- 239000000047 product Substances 0.000 description 4
- 230000035755 proliferation Effects 0.000 description 4
- 238000011160 research Methods 0.000 description 4
- 239000012266 salt solution Substances 0.000 description 4
- 239000000126 substance Substances 0.000 description 4
- 229940124597 therapeutic agent Drugs 0.000 description 4
- 230000001225 therapeutic effect Effects 0.000 description 4
- 238000001262 western blot Methods 0.000 description 4
- WZUVPPKBWHMQCE-XJKSGUPXSA-N (+)-haematoxylin Chemical compound C12=CC(O)=C(O)C=C2C[C@]2(O)[C@H]1C1=CC=C(O)C(O)=C1OC2 WZUVPPKBWHMQCE-XJKSGUPXSA-N 0.000 description 3
- 241000282326 Felis catus Species 0.000 description 3
- WZUVPPKBWHMQCE-UHFFFAOYSA-N Haematoxylin Natural products C12=CC(O)=C(O)C=C2CC2(O)C1C1=CC=C(O)C(O)=C1OC2 WZUVPPKBWHMQCE-UHFFFAOYSA-N 0.000 description 3
- 241000124008 Mammalia Species 0.000 description 3
- 241000283984 Rodentia Species 0.000 description 3
- 238000012300 Sequence Analysis Methods 0.000 description 3
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 3
- 102000008063 Small Heat-Shock Proteins Human genes 0.000 description 3
- 108010088928 Small Heat-Shock Proteins Proteins 0.000 description 3
- 230000021736 acetylation Effects 0.000 description 3
- 238000006640 acetylation reaction Methods 0.000 description 3
- 230000001154 acute effect Effects 0.000 description 3
- 125000000539 amino acid group Chemical group 0.000 description 3
- 239000012298 atmosphere Substances 0.000 description 3
- 230000001580 bacterial effect Effects 0.000 description 3
- 230000004071 biological effect Effects 0.000 description 3
- 230000000903 blocking effect Effects 0.000 description 3
- 210000004556 brain Anatomy 0.000 description 3
- RMRJXGBAOAMLHD-IHFGGWKQSA-N buprenorphine Chemical compound C([C@]12[C@H]3OC=4C(O)=CC=C(C2=4)C[C@@H]2[C@]11CC[C@]3([C@H](C1)[C@](C)(O)C(C)(C)C)OC)CN2CC1CC1 RMRJXGBAOAMLHD-IHFGGWKQSA-N 0.000 description 3
- BQRGNLJZBFXNCZ-UHFFFAOYSA-N calcein am Chemical compound O1C(=O)C2=CC=CC=C2C21C1=CC(CN(CC(=O)OCOC(C)=O)CC(=O)OCOC(C)=O)=C(OC(C)=O)C=C1OC1=C2C=C(CN(CC(=O)OCOC(C)=O)CC(=O)OCOC(=O)C)C(OC(C)=O)=C1 BQRGNLJZBFXNCZ-UHFFFAOYSA-N 0.000 description 3
- 159000000007 calcium salts Chemical class 0.000 description 3
- 230000001413 cellular effect Effects 0.000 description 3
- 239000007979 citrate buffer Substances 0.000 description 3
- 230000003247 decreasing effect Effects 0.000 description 3
- 238000012217 deletion Methods 0.000 description 3
- 230000037430 deletion Effects 0.000 description 3
- 206010012601 diabetes mellitus Diseases 0.000 description 3
- 230000004069 differentiation Effects 0.000 description 3
- 238000006073 displacement reaction Methods 0.000 description 3
- 102000013035 dynein heavy chain Human genes 0.000 description 3
- 108060002430 dynein heavy chain Proteins 0.000 description 3
- 230000002708 enhancing effect Effects 0.000 description 3
- YQGOJNYOYNNSMM-UHFFFAOYSA-N eosin Chemical compound [Na+].OC(=O)C1=CC=CC=C1C1=C2C=C(Br)C(=O)C(Br)=C2OC2=C(Br)C(O)=C(Br)C=C21 YQGOJNYOYNNSMM-UHFFFAOYSA-N 0.000 description 3
- 210000003195 fascia Anatomy 0.000 description 3
- 239000012530 fluid Substances 0.000 description 3
- -1 glycosylation Chemical compound 0.000 description 3
- 230000013595 glycosylation Effects 0.000 description 3
- 238000006206 glycosylation reaction Methods 0.000 description 3
- 230000003370 grooming effect Effects 0.000 description 3
- 238000003505 heat denaturation Methods 0.000 description 3
- 238000004128 high performance liquid chromatography Methods 0.000 description 3
- 230000007062 hydrolysis Effects 0.000 description 3
- 238000006460 hydrolysis reaction Methods 0.000 description 3
- 230000001146 hypoxic effect Effects 0.000 description 3
- 238000001727 in vivo Methods 0.000 description 3
- 230000001965 increasing effect Effects 0.000 description 3
- 208000015181 infectious disease Diseases 0.000 description 3
- 210000004969 inflammatory cell Anatomy 0.000 description 3
- 238000004255 ion exchange chromatography Methods 0.000 description 3
- 238000011694 lewis rat Methods 0.000 description 3
- 238000005259 measurement Methods 0.000 description 3
- 238000002156 mixing Methods 0.000 description 3
- 239000003068 molecular probe Substances 0.000 description 3
- 238000012544 monitoring process Methods 0.000 description 3
- 108020004707 nucleic acids Proteins 0.000 description 3
- 102000039446 nucleic acids Human genes 0.000 description 3
- 239000002773 nucleotide Substances 0.000 description 3
- 125000003729 nucleotide group Chemical group 0.000 description 3
- 230000003647 oxidation Effects 0.000 description 3
- 238000007254 oxidation reaction Methods 0.000 description 3
- 230000003239 periodontal effect Effects 0.000 description 3
- 239000008363 phosphate buffer Substances 0.000 description 3
- 230000001323 posttranslational effect Effects 0.000 description 3
- 238000012545 processing Methods 0.000 description 3
- 230000002062 proliferating effect Effects 0.000 description 3
- 230000001681 protective effect Effects 0.000 description 3
- 239000012460 protein solution Substances 0.000 description 3
- 230000009467 reduction Effects 0.000 description 3
- 230000035939 shock Effects 0.000 description 3
- 238000007619 statistical method Methods 0.000 description 3
- 238000010254 subcutaneous injection Methods 0.000 description 3
- 239000007929 subcutaneous injection Substances 0.000 description 3
- 239000000758 substrate Substances 0.000 description 3
- 229960004072 thrombin Drugs 0.000 description 3
- 230000000699 topical effect Effects 0.000 description 3
- 230000007704 transition Effects 0.000 description 3
- 230000000007 visual effect Effects 0.000 description 3
- 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 2
- 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 2
- 102000002260 Alkaline Phosphatase Human genes 0.000 description 2
- 108020004774 Alkaline Phosphatase Proteins 0.000 description 2
- 239000004475 Arginine Substances 0.000 description 2
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 2
- 102100029388 Beta-crystallin B2 Human genes 0.000 description 2
- 208000019300 CLIPPERS Diseases 0.000 description 2
- 102000005701 Calcium-Binding Proteins Human genes 0.000 description 2
- 108010045403 Calcium-Binding Proteins Proteins 0.000 description 2
- GHXZTYHSJHQHIJ-UHFFFAOYSA-N Chlorhexidine Chemical compound C=1C=C(Cl)C=CC=1NC(N)=NC(N)=NCCCCCCN=C(N)N=C(N)NC1=CC=C(Cl)C=C1 GHXZTYHSJHQHIJ-UHFFFAOYSA-N 0.000 description 2
- 229920000742 Cotton Polymers 0.000 description 2
- YCAGGFXSFQFVQL-UHFFFAOYSA-N Endothion Chemical compound COC1=COC(CSP(=O)(OC)OC)=CC1=O YCAGGFXSFQFVQL-UHFFFAOYSA-N 0.000 description 2
- 241000283073 Equus caballus Species 0.000 description 2
- 102000009123 Fibrin Human genes 0.000 description 2
- 108010073385 Fibrin Proteins 0.000 description 2
- BWGVNKXGVNDBDI-UHFFFAOYSA-N Fibrin monomer Chemical compound CNC(=O)CNC(=O)CN BWGVNKXGVNDBDI-UHFFFAOYSA-N 0.000 description 2
- 102000003972 Fibroblast growth factor 7 Human genes 0.000 description 2
- 108090000385 Fibroblast growth factor 7 Proteins 0.000 description 2
- 208000003790 Foot Ulcer Diseases 0.000 description 2
- 102100039326 Gamma-crystallin S Human genes 0.000 description 2
- 101710092831 Gamma-crystallin S Proteins 0.000 description 2
- 239000007995 HEPES buffer Substances 0.000 description 2
- VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 description 2
- MHAJPDPJQMAIIY-UHFFFAOYSA-N Hydrogen peroxide Chemical compound OO MHAJPDPJQMAIIY-UHFFFAOYSA-N 0.000 description 2
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 2
- 238000001295 Levene's test Methods 0.000 description 2
- 239000004472 Lysine Substances 0.000 description 2
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 2
- 239000012901 Milli-Q water Substances 0.000 description 2
- DTERQYGMUDWYAZ-ZETCQYMHSA-N N(6)-acetyl-L-lysine Chemical compound CC(=O)NCCCC[C@H]([NH3+])C([O-])=O DTERQYGMUDWYAZ-ZETCQYMHSA-N 0.000 description 2
- KTHDTJVBEPMMGL-VKHMYHEASA-N N-acetyl-L-alanine Chemical compound OC(=O)[C@H](C)NC(C)=O KTHDTJVBEPMMGL-VKHMYHEASA-N 0.000 description 2
- 108091034117 Oligonucleotide Proteins 0.000 description 2
- 102000003992 Peroxidases Human genes 0.000 description 2
- 108091000080 Phosphotransferase Proteins 0.000 description 2
- 102000010780 Platelet-Derived Growth Factor Human genes 0.000 description 2
- 108010038512 Platelet-Derived Growth Factor Proteins 0.000 description 2
- 241000288906 Primates Species 0.000 description 2
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 2
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 2
- IDIDJDIHTAOVLG-UHFFFAOYSA-N S-methyl-L-cysteine Natural products CSCC(N)C(O)=O IDIDJDIHTAOVLG-UHFFFAOYSA-N 0.000 description 2
- VYPSYNLAJGMNEJ-UHFFFAOYSA-N Silicium dioxide Chemical compound O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 description 2
- 206010072170 Skin wound Diseases 0.000 description 2
- 101710172711 Structural protein Proteins 0.000 description 2
- 108090000190 Thrombin Proteins 0.000 description 2
- 241000656145 Thyrsites atun Species 0.000 description 2
- 239000002253 acid Substances 0.000 description 2
- 210000000577 adipose tissue Anatomy 0.000 description 2
- 230000002411 adverse Effects 0.000 description 2
- 238000002399 angioplasty Methods 0.000 description 2
- 239000003242 anti bacterial agent Substances 0.000 description 2
- 229940088710 antibiotic agent Drugs 0.000 description 2
- 238000013459 approach Methods 0.000 description 2
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 2
- 108010087889 beta-crystallin B2 Proteins 0.000 description 2
- 102000039493 beta/gamma-crystallin family Human genes 0.000 description 2
- 108091067237 beta/gamma-crystallin family Proteins 0.000 description 2
- 230000000740 bleeding effect Effects 0.000 description 2
- 238000009835 boiling Methods 0.000 description 2
- 235000010410 calcium alginate Nutrition 0.000 description 2
- 239000000648 calcium alginate Substances 0.000 description 2
- 229960002681 calcium alginate Drugs 0.000 description 2
- AXCZMVOFGPJBDE-UHFFFAOYSA-L calcium dihydroxide Chemical compound [OH-].[OH-].[Ca+2] AXCZMVOFGPJBDE-UHFFFAOYSA-L 0.000 description 2
- 239000000920 calcium hydroxide Substances 0.000 description 2
- 229910001861 calcium hydroxide Inorganic materials 0.000 description 2
- OKHHGHGGPDJQHR-YMOPUZKJSA-L calcium;(2s,3s,4s,5s,6r)-6-[(2r,3s,4r,5s,6r)-2-carboxy-6-[(2r,3s,4r,5s,6r)-2-carboxylato-4,5,6-trihydroxyoxan-3-yl]oxy-4,5-dihydroxyoxan-3-yl]oxy-3,4,5-trihydroxyoxane-2-carboxylate Chemical compound [Ca+2].O[C@@H]1[C@H](O)[C@H](O)O[C@@H](C([O-])=O)[C@H]1O[C@H]1[C@@H](O)[C@@H](O)[C@H](O[C@H]2[C@H]([C@@H](O)[C@H](O)[C@H](O2)C([O-])=O)O)[C@H](C(O)=O)O1 OKHHGHGGPDJQHR-YMOPUZKJSA-L 0.000 description 2
- 238000001516 cell proliferation assay Methods 0.000 description 2
- 239000006285 cell suspension Substances 0.000 description 2
- 238000006243 chemical reaction Methods 0.000 description 2
- 210000004978 chinese hamster ovary cell Anatomy 0.000 description 2
- 229960003260 chlorhexidine Drugs 0.000 description 2
- OSASVXMJTNOKOY-UHFFFAOYSA-N chlorobutanol Chemical compound CC(C)(O)C(Cl)(Cl)Cl OSASVXMJTNOKOY-UHFFFAOYSA-N 0.000 description 2
- 208000021930 chronic lymphocytic inflammation with pontine perivascular enhancement responsive to steroids Diseases 0.000 description 2
- 239000011248 coating agent Substances 0.000 description 2
- 238000000576 coating method Methods 0.000 description 2
- 239000000512 collagen gel Substances 0.000 description 2
- 210000002808 connective tissue Anatomy 0.000 description 2
- 239000000470 constituent Substances 0.000 description 2
- 238000010790 dilution Methods 0.000 description 2
- 239000012895 dilution Substances 0.000 description 2
- 201000010099 disease Diseases 0.000 description 2
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 2
- 238000004090 dissolution Methods 0.000 description 2
- 229940079593 drug Drugs 0.000 description 2
- 238000002474 experimental method Methods 0.000 description 2
- 229950003499 fibrin Drugs 0.000 description 2
- 239000012362 glacial acetic acid Substances 0.000 description 2
- RWSXRVCMGQZWBV-WDSKDSINSA-N glutathione Chemical compound OC(=O)[C@@H](N)CCC(=O)N[C@@H](CS)C(=O)NCC(O)=O RWSXRVCMGQZWBV-WDSKDSINSA-N 0.000 description 2
- 239000003102 growth factor Substances 0.000 description 2
- BCQZXOMGPXTTIC-UHFFFAOYSA-N halothane Chemical compound FC(F)(F)C(Cl)Br BCQZXOMGPXTTIC-UHFFFAOYSA-N 0.000 description 2
- 229960003132 halothane Drugs 0.000 description 2
- 210000005003 heart tissue Anatomy 0.000 description 2
- 230000023597 hemostasis Effects 0.000 description 2
- 210000004394 hip joint Anatomy 0.000 description 2
- 125000000487 histidyl group Chemical group [H]N([H])C(C(=O)O*)C([H])([H])C1=C([H])N([H])C([H])=N1 0.000 description 2
- 238000010562 histological examination Methods 0.000 description 2
- 238000012744 immunostaining Methods 0.000 description 2
- 230000001976 improved effect Effects 0.000 description 2
- 238000011534 incubation Methods 0.000 description 2
- 230000028709 inflammatory response Effects 0.000 description 2
- 238000002347 injection Methods 0.000 description 2
- 239000007924 injection Substances 0.000 description 2
- 208000014674 injury Diseases 0.000 description 2
- NOESYZHRGYRDHS-UHFFFAOYSA-N insulin Chemical compound N1C(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(NC(=O)CN)C(C)CC)CSSCC(C(NC(CO)C(=O)NC(CC(C)C)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CCC(N)=O)C(=O)NC(CC(C)C)C(=O)NC(CCC(O)=O)C(=O)NC(CC(N)=O)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CSSCC(NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2C=CC(O)=CC=2)NC(=O)C(CC(C)C)NC(=O)C(C)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2NC=NC=2)NC(=O)C(CO)NC(=O)CNC2=O)C(=O)NCC(=O)NC(CCC(O)=O)C(=O)NC(CCCNC(N)=N)C(=O)NCC(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC(O)=CC=3)C(=O)NC(C(C)O)C(=O)N3C(CCC3)C(=O)NC(CCCCN)C(=O)NC(C)C(O)=O)C(=O)NC(CC(N)=O)C(O)=O)=O)NC(=O)C(C(C)CC)NC(=O)C(CO)NC(=O)C(C(C)O)NC(=O)C1CSSCC2NC(=O)C(CC(C)C)NC(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CC(N)=O)NC(=O)C(NC(=O)C(N)CC=1C=CC=CC=1)C(C)C)CC1=CN=CN1 NOESYZHRGYRDHS-UHFFFAOYSA-N 0.000 description 2
- 208000028867 ischemia Diseases 0.000 description 2
- 210000003734 kidney Anatomy 0.000 description 2
- 230000000670 limiting effect Effects 0.000 description 2
- 239000007788 liquid Substances 0.000 description 2
- 238000011068 loading method Methods 0.000 description 2
- 230000033001 locomotion Effects 0.000 description 2
- 210000003141 lower extremity Anatomy 0.000 description 2
- 239000011777 magnesium Substances 0.000 description 2
- HQKMJHAJHXVSDF-UHFFFAOYSA-L magnesium stearate Chemical compound [Mg+2].CCCCCCCCCCCCCCCCCC([O-])=O.CCCCCCCCCCCCCCCCCC([O-])=O HQKMJHAJHXVSDF-UHFFFAOYSA-L 0.000 description 2
- 230000014759 maintenance of location Effects 0.000 description 2
- 239000011159 matrix material Substances 0.000 description 2
- 235000013372 meat Nutrition 0.000 description 2
- 108020004999 messenger RNA Proteins 0.000 description 2
- 230000002503 metabolic effect Effects 0.000 description 2
- 230000011987 methylation Effects 0.000 description 2
- 238000007069 methylation reaction Methods 0.000 description 2
- 238000010232 migration assay Methods 0.000 description 2
- 230000001617 migratory effect Effects 0.000 description 2
- 239000000178 monomer Substances 0.000 description 2
- 239000013642 negative control Substances 0.000 description 2
- 230000037311 normal skin Effects 0.000 description 2
- 108040007629 peroxidase activity proteins Proteins 0.000 description 2
- 102000020233 phosphotransferase Human genes 0.000 description 2
- 230000026341 positive regulation of angiogenesis Effects 0.000 description 2
- 238000002953 preparative HPLC Methods 0.000 description 2
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 2
- 238000011084 recovery Methods 0.000 description 2
- 230000002829 reductive effect Effects 0.000 description 2
- 230000011514 reflex Effects 0.000 description 2
- 230000008929 regeneration Effects 0.000 description 2
- 238000011069 regeneration method Methods 0.000 description 2
- 239000011347 resin Substances 0.000 description 2
- 229920005989 resin Polymers 0.000 description 2
- 238000012552 review Methods 0.000 description 2
- 238000002864 sequence alignment Methods 0.000 description 2
- 125000003607 serino group Chemical group [H]N([H])[C@]([H])(C(=O)[*])C(O[H])([H])[H] 0.000 description 2
- 210000002966 serum Anatomy 0.000 description 2
- 241000894007 species Species 0.000 description 2
- 239000011550 stock solution Substances 0.000 description 2
- 239000000725 suspension Substances 0.000 description 2
- 238000004885 tandem mass spectrometry Methods 0.000 description 2
- 210000001550 testis Anatomy 0.000 description 2
- 238000002560 therapeutic procedure Methods 0.000 description 2
- 238000004809 thin layer chromatography Methods 0.000 description 2
- 230000008733 trauma Effects 0.000 description 2
- 125000000430 tryptophan group Chemical group [H]N([H])C(C(=O)O*)C([H])([H])C1=C([H])N([H])C2=C([H])C([H])=C([H])C([H])=C12 0.000 description 2
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 2
- 238000005199 ultracentrifugation Methods 0.000 description 2
- 230000037314 wound repair Effects 0.000 description 2
- NWUYHJFMYQTDRP-UHFFFAOYSA-N 1,2-bis(ethenyl)benzene;1-ethenyl-2-ethylbenzene;styrene Chemical compound C=CC1=CC=CC=C1.CCC1=CC=CC=C1C=C.C=CC1=CC=CC=C1C=C NWUYHJFMYQTDRP-UHFFFAOYSA-N 0.000 description 1
- PZBPKYOVPCNPJY-UHFFFAOYSA-N 1-[2-(allyloxy)-2-(2,4-dichlorophenyl)ethyl]imidazole Chemical compound ClC1=CC(Cl)=CC=C1C(OCC=C)CN1C=NC=C1 PZBPKYOVPCNPJY-UHFFFAOYSA-N 0.000 description 1
- OSCJHTSDLYVCQC-UHFFFAOYSA-N 2-ethylhexyl 4-[[4-[4-(tert-butylcarbamoyl)anilino]-6-[4-(2-ethylhexoxycarbonyl)anilino]-1,3,5-triazin-2-yl]amino]benzoate Chemical compound C1=CC(C(=O)OCC(CC)CCCC)=CC=C1NC1=NC(NC=2C=CC(=CC=2)C(=O)NC(C)(C)C)=NC(NC=2C=CC(=CC=2)C(=O)OCC(CC)CCCC)=N1 OSCJHTSDLYVCQC-UHFFFAOYSA-N 0.000 description 1
- 101710088758 23kDa protein Proteins 0.000 description 1
- 238000004679 31P NMR spectroscopy Methods 0.000 description 1
- UPXRTVAIJMUAQR-UHFFFAOYSA-N 4-(9h-fluoren-9-ylmethoxycarbonylamino)-1-[(2-methylpropan-2-yl)oxycarbonyl]pyrrolidine-2-carboxylic acid Chemical compound C1C(C(O)=O)N(C(=O)OC(C)(C)C)CC1NC(=O)OCC1C2=CC=CC=C2C2=CC=CC=C21 UPXRTVAIJMUAQR-UHFFFAOYSA-N 0.000 description 1
- HIQIXEFWDLTDED-UHFFFAOYSA-N 4-hydroxy-1-piperidin-4-ylpyrrolidin-2-one Chemical compound O=C1CC(O)CN1C1CCNCC1 HIQIXEFWDLTDED-UHFFFAOYSA-N 0.000 description 1
- RZVAJINKPMORJF-UHFFFAOYSA-N Acetaminophen Chemical compound CC(=O)NC1=CC=C(O)C=C1 RZVAJINKPMORJF-UHFFFAOYSA-N 0.000 description 1
- 102100032197 Alpha-crystallin A chain Human genes 0.000 description 1
- 102100040743 Alpha-crystallin B chain Human genes 0.000 description 1
- 241000238426 Anostraca Species 0.000 description 1
- 108020005544 Antisense RNA Proteins 0.000 description 1
- 241000271566 Aves Species 0.000 description 1
- 108090001008 Avidin Proteins 0.000 description 1
- 241000193830 Bacillus <bacterium> Species 0.000 description 1
- 235000014469 Bacillus subtilis Nutrition 0.000 description 1
- 241000894006 Bacteria Species 0.000 description 1
- 102100027984 Beta-crystallin B3 Human genes 0.000 description 1
- 101710189730 Beta-crystallin B3 Proteins 0.000 description 1
- BTBUEUYNUDRHOZ-UHFFFAOYSA-N Borate Chemical compound [O-]B([O-])[O-] BTBUEUYNUDRHOZ-UHFFFAOYSA-N 0.000 description 1
- UXVMQQNJUSDDNG-UHFFFAOYSA-L Calcium chloride Chemical compound [Cl-].[Cl-].[Ca+2] UXVMQQNJUSDDNG-UHFFFAOYSA-L 0.000 description 1
- 241000282465 Canis Species 0.000 description 1
- 241000700199 Cavia porcellus Species 0.000 description 1
- 101800004419 Cleaved form Proteins 0.000 description 1
- 241000499469 Collimonas pratensis Species 0.000 description 1
- 241000699800 Cricetinae Species 0.000 description 1
- 150000008574 D-amino acids Chemical class 0.000 description 1
- 108020004414 DNA Proteins 0.000 description 1
- 206010011985 Decubitus ulcer Diseases 0.000 description 1
- 208000008960 Diabetic foot Diseases 0.000 description 1
- 241000196324 Embryophyta Species 0.000 description 1
- 102000005593 Endopeptidases Human genes 0.000 description 1
- 108010059378 Endopeptidases Proteins 0.000 description 1
- 241000588724 Escherichia coli Species 0.000 description 1
- IAYPIBMASNFSPL-UHFFFAOYSA-N Ethylene oxide Chemical compound C1CO1 IAYPIBMASNFSPL-UHFFFAOYSA-N 0.000 description 1
- 206010063560 Excessive granulation tissue Diseases 0.000 description 1
- 238000004252 FT/ICR mass spectrometry Methods 0.000 description 1
- 241000282324 Felis Species 0.000 description 1
- 102000003971 Fibroblast Growth Factor 1 Human genes 0.000 description 1
- 108090000386 Fibroblast Growth Factor 1 Proteins 0.000 description 1
- 108010010803 Gelatin Proteins 0.000 description 1
- 108010024636 Glutathione Proteins 0.000 description 1
- 108010015899 Glycopeptides Proteins 0.000 description 1
- 102000002068 Glycopeptides Human genes 0.000 description 1
- 102000003886 Glycoproteins Human genes 0.000 description 1
- 108090000288 Glycoproteins Proteins 0.000 description 1
- 102100039170 Heat shock protein beta-6 Human genes 0.000 description 1
- 101710100489 Heat shock protein beta-6 Proteins 0.000 description 1
- 102000002812 Heat-Shock Proteins Human genes 0.000 description 1
- 108010004889 Heat-Shock Proteins Proteins 0.000 description 1
- 241000238631 Hexapoda Species 0.000 description 1
- 101000920937 Homo sapiens Alpha-crystallin A chain Proteins 0.000 description 1
- 101000851058 Homo sapiens Neutrophil elastase Proteins 0.000 description 1
- PMMYEEVYMWASQN-DMTCNVIQSA-N Hydroxyproline Chemical compound O[C@H]1CN[C@H](C(O)=O)C1 PMMYEEVYMWASQN-DMTCNVIQSA-N 0.000 description 1
- 102000004877 Insulin Human genes 0.000 description 1
- 108090001061 Insulin Proteins 0.000 description 1
- YQEZLKZALYSWHR-UHFFFAOYSA-N Ketamine Chemical compound C=1C=CC=C(Cl)C=1C1(NC)CCCCC1=O YQEZLKZALYSWHR-UHFFFAOYSA-N 0.000 description 1
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 1
- 150000008575 L-amino acids Chemical class 0.000 description 1
- ODKSFYDXXFIFQN-BYPYZUCNSA-P L-argininium(2+) Chemical compound NC(=[NH2+])NCCC[C@H]([NH3+])C(O)=O ODKSFYDXXFIFQN-BYPYZUCNSA-P 0.000 description 1
- FYYHWMGAXLPEAU-UHFFFAOYSA-N Magnesium Chemical compound [Mg] FYYHWMGAXLPEAU-UHFFFAOYSA-N 0.000 description 1
- YJPIGAIKUZMOQA-UHFFFAOYSA-N Melatonin Natural products COC1=CC=C2N(C(C)=O)C=C(CCN)C2=C1 YJPIGAIKUZMOQA-UHFFFAOYSA-N 0.000 description 1
- 102000008109 Mixed Function Oxygenases Human genes 0.000 description 1
- 108010074633 Mixed Function Oxygenases Proteins 0.000 description 1
- BYHJHXPTQMMKCA-QMMMGPOBSA-N N-formyl-L-kynurenine Chemical compound [O-]C(=O)[C@@H]([NH3+])CC(=O)C1=CC=CC=C1NC=O BYHJHXPTQMMKCA-QMMMGPOBSA-N 0.000 description 1
- 238000005481 NMR spectroscopy Methods 0.000 description 1
- 108091028043 Nucleic acid sequence Proteins 0.000 description 1
- 101710141454 Nucleoprotein Proteins 0.000 description 1
- CTQNGGLPUBDAKN-UHFFFAOYSA-N O-Xylene Chemical compound CC1=CC=CC=C1C CTQNGGLPUBDAKN-UHFFFAOYSA-N 0.000 description 1
- 241000283973 Oryctolagus cuniculus Species 0.000 description 1
- 229910019142 PO4 Inorganic materials 0.000 description 1
- 241000526754 Pannonibacter phragmitetus Species 0.000 description 1
- 102000007982 Phosphoproteins Human genes 0.000 description 1
- 108010089430 Phosphoproteins Proteins 0.000 description 1
- 241000235648 Pichia Species 0.000 description 1
- 208000004210 Pressure Ulcer Diseases 0.000 description 1
- 108010059712 Pronase Proteins 0.000 description 1
- 241000589516 Pseudomonas Species 0.000 description 1
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 1
- 241000607142 Salmonella Species 0.000 description 1
- 229920002684 Sepharose Polymers 0.000 description 1
- BLRPTPMANUNPDV-UHFFFAOYSA-N Silane Chemical compound [SiH4] BLRPTPMANUNPDV-UHFFFAOYSA-N 0.000 description 1
- BQCADISMDOOEFD-UHFFFAOYSA-N Silver Chemical compound [Ag] BQCADISMDOOEFD-UHFFFAOYSA-N 0.000 description 1
- 206010040943 Skin Ulcer Diseases 0.000 description 1
- 229920002472 Starch Polymers 0.000 description 1
- 241000187747 Streptomyces Species 0.000 description 1
- 229930006000 Sucrose Natural products 0.000 description 1
- CZMRCDWAGMRECN-UGDNZRGBSA-N Sucrose Chemical compound O[C@H]1[C@H](O)[C@@H](CO)O[C@@]1(CO)O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 CZMRCDWAGMRECN-UGDNZRGBSA-N 0.000 description 1
- OUUQCZGPVNCOIJ-UHFFFAOYSA-M Superoxide Chemical compound [O-][O] OUUQCZGPVNCOIJ-UHFFFAOYSA-M 0.000 description 1
- 208000002847 Surgical Wound Diseases 0.000 description 1
- 244000269722 Thea sinensis Species 0.000 description 1
- 239000007983 Tris buffer Substances 0.000 description 1
- 238000012793 UV/ Vis spectrometry Methods 0.000 description 1
- 208000025865 Ulcer Diseases 0.000 description 1
- 101710100170 Unknown protein Proteins 0.000 description 1
- 208000000558 Varicose Ulcer Diseases 0.000 description 1
- 102000013127 Vimentin Human genes 0.000 description 1
- 108010065472 Vimentin Proteins 0.000 description 1
- 235000010724 Wisteria floribunda Nutrition 0.000 description 1
- 206010048038 Wound infection Diseases 0.000 description 1
- 240000008042 Zea mays Species 0.000 description 1
- 235000005824 Zea mays ssp. parviglumis Nutrition 0.000 description 1
- 235000002017 Zea mays subsp mays Nutrition 0.000 description 1
- HCHKCACWOHOZIP-UHFFFAOYSA-N Zinc Chemical compound [Zn] HCHKCACWOHOZIP-UHFFFAOYSA-N 0.000 description 1
- 230000001133 acceleration Effects 0.000 description 1
- 238000009825 accumulation Methods 0.000 description 1
- 125000000218 acetic acid group Chemical group C(C)(=O)* 0.000 description 1
- 239000003929 acidic solution Substances 0.000 description 1
- 150000007513 acids Chemical class 0.000 description 1
- 230000009471 action Effects 0.000 description 1
- 239000013543 active substance Substances 0.000 description 1
- 230000032683 aging Effects 0.000 description 1
- 238000013019 agitation Methods 0.000 description 1
- 235000004279 alanine Nutrition 0.000 description 1
- 150000001298 alcohols Chemical class 0.000 description 1
- 230000029936 alkylation Effects 0.000 description 1
- 238000005804 alkylation reaction Methods 0.000 description 1
- BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 description 1
- 229910052921 ammonium sulfate Inorganic materials 0.000 description 1
- 235000011130 ammonium sulphate Nutrition 0.000 description 1
- 238000010171 animal model Methods 0.000 description 1
- 230000003042 antagnostic effect Effects 0.000 description 1
- 239000002260 anti-inflammatory agent Substances 0.000 description 1
- 229940121363 anti-inflammatory agent Drugs 0.000 description 1
- 230000003110 anti-inflammatory effect Effects 0.000 description 1
- 239000000427 antigen Substances 0.000 description 1
- 102000036639 antigens Human genes 0.000 description 1
- 108091007433 antigens Proteins 0.000 description 1
- 239000004599 antimicrobial Substances 0.000 description 1
- 210000002565 arteriole Anatomy 0.000 description 1
- 210000001188 articular cartilage Anatomy 0.000 description 1
- 235000021053 average weight gain Nutrition 0.000 description 1
- 210000002469 basement membrane Anatomy 0.000 description 1
- 239000011230 binding agent Substances 0.000 description 1
- 229960002685 biotin Drugs 0.000 description 1
- 235000020958 biotin Nutrition 0.000 description 1
- 239000011616 biotin Substances 0.000 description 1
- 210000004369 blood Anatomy 0.000 description 1
- 239000008280 blood Substances 0.000 description 1
- 230000017531 blood circulation Effects 0.000 description 1
- 210000000988 bone and bone Anatomy 0.000 description 1
- 238000009395 breeding Methods 0.000 description 1
- 230000001488 breeding effect Effects 0.000 description 1
- 239000007853 buffer solution Substances 0.000 description 1
- 239000007975 buffered saline Substances 0.000 description 1
- 239000001110 calcium chloride Substances 0.000 description 1
- 229910001628 calcium chloride Inorganic materials 0.000 description 1
- 125000000837 carbohydrate group Chemical group 0.000 description 1
- ADRVNXBAWSRFAJ-UHFFFAOYSA-N catechin Natural products OC1Cc2cc(O)cc(O)c2OC1c3ccc(O)c(O)c3 ADRVNXBAWSRFAJ-UHFFFAOYSA-N 0.000 description 1
- 150000001765 catechin Chemical class 0.000 description 1
- 235000005487 catechin Nutrition 0.000 description 1
- 238000005341 cation exchange Methods 0.000 description 1
- 239000006143 cell culture medium Substances 0.000 description 1
- 230000005779 cell damage Effects 0.000 description 1
- 238000002737 cell proliferation kit Methods 0.000 description 1
- 230000008859 change Effects 0.000 description 1
- 238000012512 characterization method Methods 0.000 description 1
- PBAYDYUZOSNJGU-UHFFFAOYSA-N chelidonic acid Natural products OC(=O)C1=CC(=O)C=C(C(O)=O)O1 PBAYDYUZOSNJGU-UHFFFAOYSA-N 0.000 description 1
- 229960004926 chlorobutanol Drugs 0.000 description 1
- 230000004087 circulation Effects 0.000 description 1
- 230000000052 comparative effect Effects 0.000 description 1
- 230000000295 complement effect Effects 0.000 description 1
- 239000002299 complementary DNA Substances 0.000 description 1
- 239000003184 complementary RNA Substances 0.000 description 1
- 239000002131 composite material Substances 0.000 description 1
- 229940125898 compound 5 Drugs 0.000 description 1
- 230000001010 compromised effect Effects 0.000 description 1
- 235000005822 corn Nutrition 0.000 description 1
- 230000001054 cortical effect Effects 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
- 239000006071 cream Substances 0.000 description 1
- 239000000287 crude extract Substances 0.000 description 1
- 238000012258 culturing Methods 0.000 description 1
- 238000005520 cutting process Methods 0.000 description 1
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 description 1
- 230000002380 cytological effect Effects 0.000 description 1
- 230000006378 damage Effects 0.000 description 1
- 239000007857 degradation product Substances 0.000 description 1
- 239000008367 deionised water Substances 0.000 description 1
- 229910021641 deionized water Inorganic materials 0.000 description 1
- 230000001934 delay Effects 0.000 description 1
- 238000004925 denaturation Methods 0.000 description 1
- 230000036425 denaturation Effects 0.000 description 1
- 238000001514 detection method Methods 0.000 description 1
- 235000005911 diet Nutrition 0.000 description 1
- 230000037213 diet Effects 0.000 description 1
- 239000002612 dispersion medium Substances 0.000 description 1
- 238000010494 dissociation reaction Methods 0.000 description 1
- 230000005593 dissociations Effects 0.000 description 1
- PMMYEEVYMWASQN-UHFFFAOYSA-N dl-hydroxyproline Natural products OC1C[NH2+]C(C([O-])=O)C1 PMMYEEVYMWASQN-UHFFFAOYSA-N 0.000 description 1
- 230000000437 effect on angiogenesis Effects 0.000 description 1
- 230000002849 elastaseinhibitory effect Effects 0.000 description 1
- 238000001493 electron microscopy Methods 0.000 description 1
- 230000009881 electrostatic interaction Effects 0.000 description 1
- 239000003995 emulsifying agent Substances 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 230000006862 enzymatic digestion Effects 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- 210000003979 eosinophil Anatomy 0.000 description 1
- 230000010393 epithelial cell migration Effects 0.000 description 1
- 238000011067 equilibration Methods 0.000 description 1
- 239000006167 equilibration buffer Substances 0.000 description 1
- BEFDCLMNVWHSGT-UHFFFAOYSA-N ethenylcyclopentane Chemical compound C=CC1CCCC1 BEFDCLMNVWHSGT-UHFFFAOYSA-N 0.000 description 1
- 125000001495 ethyl group Chemical group [H]C([H])([H])C([H])([H])* 0.000 description 1
- 238000011156 evaluation Methods 0.000 description 1
- 230000005284 excitation Effects 0.000 description 1
- 230000007717 exclusion Effects 0.000 description 1
- 230000029142 excretion Effects 0.000 description 1
- 239000013604 expression vector Substances 0.000 description 1
- 239000011536 extraction buffer Substances 0.000 description 1
- 210000000416 exudates and transudate Anatomy 0.000 description 1
- 239000000835 fiber Substances 0.000 description 1
- 230000001497 fibrovascular Effects 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- 239000012847 fine chemical Substances 0.000 description 1
- 235000012631 food intake Nutrition 0.000 description 1
- 230000002538 fungal effect Effects 0.000 description 1
- 239000007789 gas Substances 0.000 description 1
- 239000008273 gelatin Substances 0.000 description 1
- 229920000159 gelatin Polymers 0.000 description 1
- 235000019322 gelatine Nutrition 0.000 description 1
- 235000011852 gelatine desserts Nutrition 0.000 description 1
- 239000003349 gelling agent Substances 0.000 description 1
- 238000007429 general method Methods 0.000 description 1
- 230000002068 genetic effect Effects 0.000 description 1
- 102000034238 globular proteins Human genes 0.000 description 1
- 108091005896 globular proteins Proteins 0.000 description 1
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 1
- 229960003180 glutathione Drugs 0.000 description 1
- 210000001126 granulation tissue Anatomy 0.000 description 1
- 229940065115 grapefruit extract Drugs 0.000 description 1
- 235000009569 green tea Nutrition 0.000 description 1
- 210000004013 groin Anatomy 0.000 description 1
- 239000001963 growth medium Substances 0.000 description 1
- ZRALSGWEFCBTJO-UHFFFAOYSA-O guanidinium Chemical compound NC(N)=[NH2+] ZRALSGWEFCBTJO-UHFFFAOYSA-O 0.000 description 1
- 210000003128 head Anatomy 0.000 description 1
- 239000000833 heterodimer Substances 0.000 description 1
- 210000003630 histaminocyte Anatomy 0.000 description 1
- 239000000710 homodimer Substances 0.000 description 1
- 102000052502 human ELANE Human genes 0.000 description 1
- 230000036571 hydration Effects 0.000 description 1
- 238000006703 hydration reaction Methods 0.000 description 1
- 229910052739 hydrogen Inorganic materials 0.000 description 1
- 230000003301 hydrolyzing effect Effects 0.000 description 1
- 229960002591 hydroxyproline Drugs 0.000 description 1
- 230000007954 hypoxia Effects 0.000 description 1
- 238000005286 illumination Methods 0.000 description 1
- 238000003119 immunoblot Methods 0.000 description 1
- 230000002055 immunohistochemical effect Effects 0.000 description 1
- 238000003364 immunohistochemistry Methods 0.000 description 1
- 230000001771 impaired effect Effects 0.000 description 1
- 239000007943 implant Substances 0.000 description 1
- 230000006872 improvement Effects 0.000 description 1
- 238000000099 in vitro assay Methods 0.000 description 1
- 230000002779 inactivation Effects 0.000 description 1
- 125000001041 indolyl group Chemical group 0.000 description 1
- 230000001939 inductive effect Effects 0.000 description 1
- 230000006749 inflammatory damage Effects 0.000 description 1
- 239000004615 ingredient Substances 0.000 description 1
- 239000002198 insoluble material Substances 0.000 description 1
- 229940125396 insulin Drugs 0.000 description 1
- 230000003993 interaction Effects 0.000 description 1
- 230000008863 intramolecular interaction Effects 0.000 description 1
- 238000007918 intramuscular administration Methods 0.000 description 1
- 238000001990 intravenous administration Methods 0.000 description 1
- 238000011835 investigation Methods 0.000 description 1
- 239000003456 ion exchange resin Substances 0.000 description 1
- 229920003303 ion-exchange polymer Polymers 0.000 description 1
- 230000005865 ionizing radiation Effects 0.000 description 1
- 238000005304 joining Methods 0.000 description 1
- 210000002510 keratinocyte Anatomy 0.000 description 1
- 229960003299 ketamine Drugs 0.000 description 1
- 229960004184 ketamine hydrochloride Drugs 0.000 description 1
- 238000009533 lab test Methods 0.000 description 1
- 210000003041 ligament Anatomy 0.000 description 1
- 239000006210 lotion Substances 0.000 description 1
- 210000004924 lung microvascular endothelial cell Anatomy 0.000 description 1
- 210000004698 lymphocyte Anatomy 0.000 description 1
- 210000002540 macrophage Anatomy 0.000 description 1
- 229910052749 magnesium Inorganic materials 0.000 description 1
- 235000019359 magnesium stearate Nutrition 0.000 description 1
- 210000004962 mammalian cell Anatomy 0.000 description 1
- 238000004519 manufacturing process Methods 0.000 description 1
- 230000035800 maturation Effects 0.000 description 1
- 230000007246 mechanism Effects 0.000 description 1
- 230000001404 mediated effect Effects 0.000 description 1
- DRLFMBDRBRZALE-UHFFFAOYSA-N melatonin Chemical compound COC1=CC=C2NC=C(CCNC(C)=O)C2=C1 DRLFMBDRBRZALE-UHFFFAOYSA-N 0.000 description 1
- 229960003987 melatonin Drugs 0.000 description 1
- 230000007102 metabolic function Effects 0.000 description 1
- 125000002496 methyl group Chemical group [H]C([H])([H])* 0.000 description 1
- 238000010369 molecular cloning Methods 0.000 description 1
- 230000000869 mutational effect Effects 0.000 description 1
- 210000000492 nasalseptum Anatomy 0.000 description 1
- 230000031990 negative regulation of inflammatory response Effects 0.000 description 1
- 230000001537 neural effect Effects 0.000 description 1
- 210000005157 neural retina Anatomy 0.000 description 1
- 230000007935 neutral effect Effects 0.000 description 1
- 229910052757 nitrogen Inorganic materials 0.000 description 1
- 239000002674 ointment Substances 0.000 description 1
- 239000003002 pH adjusting agent Substances 0.000 description 1
- 238000010979 pH adjustment Methods 0.000 description 1
- 238000012856 packing Methods 0.000 description 1
- 244000052769 pathogen Species 0.000 description 1
- 230000006320 pegylation Effects 0.000 description 1
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 1
- 239000010452 phosphate Substances 0.000 description 1
- USRGIUJOYOXOQJ-GBXIJSLDSA-N phosphothreonine Chemical compound OP(=O)(O)O[C@H](C)[C@H](N)C(O)=O USRGIUJOYOXOQJ-GBXIJSLDSA-N 0.000 description 1
- 230000004962 physiological condition Effects 0.000 description 1
- 235000017807 phytochemicals Nutrition 0.000 description 1
- 229930000223 plant secondary metabolite Natural products 0.000 description 1
- 210000004180 plasmocyte Anatomy 0.000 description 1
- 238000007747 plating Methods 0.000 description 1
- 229920001184 polypeptide Polymers 0.000 description 1
- 230000008092 positive effect Effects 0.000 description 1
- 239000003755 preservative agent Substances 0.000 description 1
- 230000001023 pro-angiogenic effect Effects 0.000 description 1
- 230000002035 prolonged effect Effects 0.000 description 1
- 230000000069 prophylactic effect Effects 0.000 description 1
- 125000001436 propyl group Chemical group [H]C([*])([H])C([H])([H])C([H])([H])[H] 0.000 description 1
- 235000004252 protein component Nutrition 0.000 description 1
- 230000009145 protein modification Effects 0.000 description 1
- 230000006920 protein precipitation Effects 0.000 description 1
- 230000017854 proteolysis Effects 0.000 description 1
- 239000005297 pyrex Substances 0.000 description 1
- 238000012207 quantitative assay Methods 0.000 description 1
- 230000005855 radiation Effects 0.000 description 1
- 238000011552 rat model Methods 0.000 description 1
- 230000000717 retained effect Effects 0.000 description 1
- 230000004233 retinal vasculature Effects 0.000 description 1
- 238000013341 scale-up Methods 0.000 description 1
- 239000012679 serum free medium Substances 0.000 description 1
- 229910000077 silane Inorganic materials 0.000 description 1
- 229910052709 silver Inorganic materials 0.000 description 1
- 239000004332 silver Substances 0.000 description 1
- 210000000813 small intestine Anatomy 0.000 description 1
- 238000002791 soaking Methods 0.000 description 1
- 239000011343 solid material Substances 0.000 description 1
- 239000004334 sorbic acid Substances 0.000 description 1
- 229940075582 sorbic acid Drugs 0.000 description 1
- 235000010199 sorbic acid Nutrition 0.000 description 1
- 238000004611 spectroscopical analysis Methods 0.000 description 1
- 238000013222 sprague-dawley male rat Methods 0.000 description 1
- 238000012453 sprague-dawley rat model Methods 0.000 description 1
- 230000006641 stabilisation Effects 0.000 description 1
- 238000011105 stabilization Methods 0.000 description 1
- 238000010186 staining Methods 0.000 description 1
- 239000008107 starch Substances 0.000 description 1
- 235000019698 starch Nutrition 0.000 description 1
- 230000001954 sterilising effect Effects 0.000 description 1
- 238000004659 sterilization and disinfection Methods 0.000 description 1
- 238000003756 stirring Methods 0.000 description 1
- 210000002784 stomach Anatomy 0.000 description 1
- 230000035882 stress Effects 0.000 description 1
- 239000005720 sucrose Substances 0.000 description 1
- 239000004094 surface-active agent Substances 0.000 description 1
- 238000001356 surgical procedure Methods 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- 230000009885 systemic effect Effects 0.000 description 1
- 239000002562 thickening agent Substances 0.000 description 1
- 210000003813 thumb Anatomy 0.000 description 1
- 230000000451 tissue damage Effects 0.000 description 1
- 231100000827 tissue damage Toxicity 0.000 description 1
- FGMPLJWBKKVCDB-UHFFFAOYSA-N trans-L-hydroxy-proline Natural products ON1CCCC1C(O)=O FGMPLJWBKKVCDB-UHFFFAOYSA-N 0.000 description 1
- 230000001131 transforming effect Effects 0.000 description 1
- 239000013638 trimer Substances 0.000 description 1
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 1
- 239000003656 tris buffered saline Substances 0.000 description 1
- 231100000397 ulcer Toxicity 0.000 description 1
- 238000010200 validation analysis Methods 0.000 description 1
- 208000019553 vascular disease Diseases 0.000 description 1
- 210000003462 vein Anatomy 0.000 description 1
- 230000035899 viability Effects 0.000 description 1
- 210000005048 vimentin Anatomy 0.000 description 1
- 238000012800 visualization Methods 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
- 239000002699 waste material Substances 0.000 description 1
- 238000005303 weighing Methods 0.000 description 1
- 230000004580 weight loss Effects 0.000 description 1
- 239000012224 working solution Substances 0.000 description 1
- 238000011610 wound healing animal model Methods 0.000 description 1
- BPICBUSOMSTKRF-UHFFFAOYSA-N xylazine Chemical compound CC1=CC=CC(C)=C1NC1=NCCCS1 BPICBUSOMSTKRF-UHFFFAOYSA-N 0.000 description 1
- 229960001600 xylazine Drugs 0.000 description 1
- 239000008096 xylene Substances 0.000 description 1
- 238000004383 yellowing Methods 0.000 description 1
- 229910052725 zinc Inorganic materials 0.000 description 1
- 239000011701 zinc Substances 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
- C07K14/47—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P17/00—Drugs for dermatological disorders
- A61P17/02—Drugs for dermatological disorders for treating wounds, ulcers, burns, scars, keloids, or the like
-
- 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
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P9/00—Drugs for disorders of the cardiovascular system
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- General Chemical & Material Sciences (AREA)
- Pharmacology & Pharmacy (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Animal Behavior & Ethology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Engineering & Computer Science (AREA)
- Biochemistry (AREA)
- Genetics & Genomics (AREA)
- Toxicology (AREA)
- Zoology (AREA)
- Gastroenterology & Hepatology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Biophysics (AREA)
- Molecular Biology (AREA)
- Heart & Thoracic Surgery (AREA)
- Cardiology (AREA)
- Dermatology (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Peptides Or Proteins (AREA)
- Medicinal Preparation (AREA)
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| AU2008295449A AU2008295449A1 (en) | 2007-09-07 | 2008-09-05 | Agents with angiogenic and wound healing activity |
Applications Claiming Priority (4)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| AU2007904857 | 2007-09-07 | ||
| AU2007904857A AU2007904857A0 (en) | 2007-09-07 | Agents with angiogenic and wound healing activity | |
| PCT/AU2008/001319 WO2009029991A1 (en) | 2007-09-07 | 2008-09-05 | Agents with angiogenic and wound healing activity |
| AU2008295449A AU2008295449A1 (en) | 2007-09-07 | 2008-09-05 | Agents with angiogenic and wound healing activity |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| AU2008295449A1 true AU2008295449A1 (en) | 2009-03-12 |
Family
ID=40428369
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| AU2008295449A Abandoned AU2008295449A1 (en) | 2007-09-07 | 2008-09-05 | Agents with angiogenic and wound healing activity |
Country Status (6)
| Country | Link |
|---|---|
| US (1) | US8404644B2 (cg-RX-API-DMAC7.html) |
| EP (2) | EP2190455A4 (cg-RX-API-DMAC7.html) |
| JP (1) | JP5685773B2 (cg-RX-API-DMAC7.html) |
| AU (1) | AU2008295449A1 (cg-RX-API-DMAC7.html) |
| NZ (1) | NZ583803A (cg-RX-API-DMAC7.html) |
| WO (1) | WO2009029991A1 (cg-RX-API-DMAC7.html) |
Families Citing this family (9)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| AU2008295449A1 (en) * | 2007-09-07 | 2009-03-12 | Industrial Research Limited | Agents with angiogenic and wound healing activity |
| EP2512492A1 (en) * | 2009-12-14 | 2012-10-24 | University of Massachusetts | Methods of inhibiting cataracts and presbyopia |
| EP2668956A4 (en) * | 2011-01-26 | 2015-11-11 | Megmilk Snow Brand Co Ltd | MEANS FOR IMPROVED SENSUAL ASSESSMENT |
| WO2013073968A2 (en) * | 2011-09-12 | 2013-05-23 | Industrial Research Limited | Agents for modulation of cell signalling |
| JP2014005254A (ja) * | 2012-06-26 | 2014-01-16 | Bfsr:Kk | 熱傷由来全身性炎症反応症候群の予防外用薬 |
| ES2727293T3 (es) | 2013-03-14 | 2019-10-15 | Univ Massachusetts | Métodos de inhibición de cataratas y presbicia |
| KR20170040648A (ko) * | 2015-10-05 | 2017-04-13 | 차의과학대학교 산학협력단 | 당뇨병성 족부궤양의 예방 또는 치료용 약학 조성물 |
| CN108348494A (zh) | 2015-11-13 | 2018-07-31 | 马萨诸塞大学 | 用于抑制白内障和老花眼的含peg的双官能分子 |
| JP2022522247A (ja) * | 2019-02-08 | 2022-04-14 | オークランド ユニサービシズ リミテッド | 生体材料およびそれに関連する方法 |
Family Cites Families (19)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CA2187482A1 (en) * | 1995-10-13 | 1997-04-14 | Eri Inoue | Pharmaceutical composition |
| WO1999051634A1 (en) | 1998-04-03 | 1999-10-14 | Hunan Medical University | Human gap junction protein beta-3 |
| WO1999051738A1 (en) | 1998-04-03 | 1999-10-14 | Hunan Medical University | Human gap junction protein beta-4 |
| JP2002527544A (ja) | 1998-10-15 | 2002-08-27 | イー・アイ・デュポン・ドウ・ヌムール・アンド・カンパニー | フルオロシクロブチル環を含むポリマー及びその製造 |
| JP3783200B2 (ja) * | 2000-08-24 | 2006-06-07 | 株式会社加美乃素本舗 | 血管新生剤 |
| US7263214B2 (en) | 2002-05-15 | 2007-08-28 | Ge Medical Systems Global Technology Company Llc | Computer aided diagnosis from multiple energy images |
| AU2003234613A1 (en) | 2002-05-15 | 2003-12-02 | Seul, Kyung, Hwan | Method of modulating angiogenesis |
| AU2003281325A1 (en) * | 2002-07-02 | 2004-01-23 | The Johns Hopkins University | Secreted and cytoplasmic tumor endothelial markers |
| JPWO2004096277A1 (ja) * | 2003-05-01 | 2006-07-13 | 国立大学法人京都大学 | 眼内血管新生疾患の予防又は治療剤 |
| EP1624886A2 (en) * | 2003-05-12 | 2006-02-15 | Expressive Constructs, Inc. | Methods for increasing cell and tissue viability |
| US7456151B2 (en) * | 2004-07-14 | 2008-11-25 | University Of Utah Research Foundation | Promoting angiogenesis with netrin1 polypeptides |
| JP5964538B2 (ja) | 2005-02-03 | 2016-08-03 | コーダ セラピューティクス， インコーポレイテッド | 抗コネキシン化合物およびそれらの使用 |
| WO2006091930A2 (en) | 2005-02-24 | 2006-08-31 | Massachusetts Eye & Ear Infirmary | Methods and compounds for promoting vessel regression |
| EP1978988A4 (en) | 2006-01-13 | 2009-11-04 | Univ New York State Res Found | PEPTIDE-BASED REGULATION OF GAP-JUNCTIONS |
| US20100004168A1 (en) * | 2006-06-30 | 2010-01-07 | The Johns Hopkins University | Use of Crystallin For The Modulation of Angiogenesis |
| US8247384B2 (en) * | 2006-11-15 | 2012-08-21 | Coda Therapeutics, Inc. | Methods and compositions for wound healing |
| WO2008073466A2 (en) | 2006-12-11 | 2008-06-19 | The Board Of Trustees Of The Leland Stanford Junior University | Alpha b-crystallin as a therapy for inflammation |
| WO2009012224A2 (en) | 2007-07-13 | 2009-01-22 | The Research Foundation Of State University Of New York | Peptide-based regulation of gap junctions |
| AU2008295449A1 (en) * | 2007-09-07 | 2009-03-12 | Industrial Research Limited | Agents with angiogenic and wound healing activity |
-
2008
- 2008-09-05 AU AU2008295449A patent/AU2008295449A1/en not_active Abandoned
- 2008-09-05 EP EP08783056A patent/EP2190455A4/en not_active Withdrawn
- 2008-09-05 WO PCT/AU2008/001319 patent/WO2009029991A1/en not_active Ceased
- 2008-09-05 NZ NZ583803A patent/NZ583803A/xx not_active IP Right Cessation
- 2008-09-05 US US12/676,295 patent/US8404644B2/en not_active Expired - Fee Related
- 2008-09-05 EP EP11164650A patent/EP2407175A1/en not_active Ceased
- 2008-09-05 JP JP2010523239A patent/JP5685773B2/ja not_active Expired - Fee Related
Also Published As
| Publication number | Publication date |
|---|---|
| EP2190455A1 (en) | 2010-06-02 |
| EP2407175A9 (en) | 2012-02-29 |
| WO2009029991A1 (en) | 2009-03-12 |
| NZ583803A (en) | 2012-12-21 |
| US20100210531A1 (en) | 2010-08-19 |
| JP2010538020A (ja) | 2010-12-09 |
| US8404644B2 (en) | 2013-03-26 |
| EP2407175A1 (en) | 2012-01-18 |
| JP5685773B2 (ja) | 2015-03-18 |
| EP2190455A4 (en) | 2010-11-24 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| US8404644B2 (en) | Agents with angiogenic and wound healing activity | |
| Meng et al. | The effect of alkaline pretreatment on the biochemical characteristics and fibril-forming abilities of types I and II collagen extracted from bester sturgeon by-products | |
| JP4616642B2 (ja) | コラーゲンおよびコラーゲンを製造する方法 | |
| JP5774999B2 (ja) | 水生動物からのコラーゲン抽出物 | |
| CA2032059C (en) | Wound treatment employing biologically active peptides | |
| RU2683649C1 (ru) | Композиция для лечения и профилактики доброкачественной гиперплазии простаты | |
| EP2737910B1 (en) | Composite collagen sponge and preparation method thereof | |
| JPH07502490A (ja) | 殺菌性／透過性増大タンパク質および脂質担体を含有する組成物、その製造方法、およびそれらの使用 | |
| DK2244724T3 (en) | Use of peptides for promoting wound healing | |
| KR20160136342A (ko) | 모발 성장의 억제를 위한 오스테오폰틴 유도체를 포함하는 조성물 | |
| CA2371794C (en) | Human antibiotic proteins | |
| EP1080111B1 (en) | The induction of antiobiotic peptides by lait (scd14) protein | |
| KR20230088787A (ko) | 신규 생물활성 펩티드 조합 및 이의 용도 | |
| WO2013073968A2 (en) | Agents for modulation of cell signalling | |
| CN110772632B (zh) | 神经导向因子semaphorin 3a在制备治疗骨关节炎药物中的用途 | |
| JP4811885B2 (ja) | ルシリア・セリカータの幼虫から得られるキモトリプシン及び創傷の治療のためのその使用 | |
| TWI863205B (zh) | 具傷口癒合功效之鱸魚胜肽及其組成物 | |
| WO2007142381A1 (en) | Human short helical peptide-1 which has antimicrobial, antitumor, and immune stimulating activity and uses thereof | |
| WO2001089450A2 (en) | Treating musculoskeletal disorders using lp85 and analogs thereof | |
| KR101106706B1 (ko) | 실고기 유래 콜라겐 및 그 제조 방법 | |
| Guo et al. | Sema3A ameliorates the pathological progression of osteoarthritis by modulating mitochondrial damage in chondrocytes | |
| Assis et al. | Peptides from frog skin for wound repair: a systematic review | |
| CN116568703A (zh) | 治疗纤维化和伤口愈合的方法 | |
| WO2019168697A1 (en) | Overexpression of foxc1 to treat corneal vascularization | |
| KR20150001370A (ko) | 피부 주름 예방 및 개선용 조성물 |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| MK4 | Application lapsed section 142(2)(d) - no continuation fee paid for the application |