JP2004533242A - 異種移植のための改変された器官および細胞 - Google Patents
異種移植のための改変された器官および細胞 Download PDFInfo
- Publication number
- JP2004533242A JP2004533242A JP2002585632A JP2002585632A JP2004533242A JP 2004533242 A JP2004533242 A JP 2004533242A JP 2002585632 A JP2002585632 A JP 2002585632A JP 2002585632 A JP2002585632 A JP 2002585632A JP 2004533242 A JP2004533242 A JP 2004533242A
- Authority
- JP
- Japan
- Prior art keywords
- cells
- human
- gal
- epitope
- prbc
- 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.)
- Pending
Links
- 210000000056 organ Anatomy 0.000 title claims abstract description 37
- 238000002689 xenotransplantation Methods 0.000 title abstract description 24
- 210000004027 cell Anatomy 0.000 claims abstract description 100
- 241001465754 Metazoa Species 0.000 claims abstract description 48
- FDJKUWYYUZCUJX-KVNVFURPSA-N N-glycolylneuraminic acid Chemical group OC[C@H](O)[C@H](O)[C@@H]1O[C@](O)(C(O)=O)C[C@H](O)[C@H]1NC(=O)CO FDJKUWYYUZCUJX-KVNVFURPSA-N 0.000 claims abstract description 42
- 238000002054 transplantation Methods 0.000 claims abstract description 33
- 241000282887 Suidae Species 0.000 claims abstract description 32
- 210000001519 tissue Anatomy 0.000 claims abstract description 26
- 238000011282 treatment Methods 0.000 claims abstract description 17
- 238000000034 method Methods 0.000 claims description 59
- 108090000623 proteins and genes Proteins 0.000 claims description 59
- 102000004169 proteins and genes Human genes 0.000 claims description 25
- 210000003743 erythrocyte Anatomy 0.000 claims description 22
- 230000000295 complement effect Effects 0.000 claims description 19
- 230000014509 gene expression Effects 0.000 claims description 19
- 108010013423 CMPacetylneuraminate monooxygenase Proteins 0.000 claims description 14
- 102000034356 gene-regulatory proteins Human genes 0.000 claims description 9
- 108091006104 gene-regulatory proteins Proteins 0.000 claims description 9
- 238000010353 genetic engineering Methods 0.000 claims description 5
- 210000004962 mammalian cell Anatomy 0.000 claims description 5
- 238000004519 manufacturing process Methods 0.000 claims description 4
- 210000001557 animal structure Anatomy 0.000 claims description 3
- 241000283707 Capra Species 0.000 claims description 2
- 102000003839 Human Proteins Human genes 0.000 claims 1
- 108090000144 Human Proteins Proteins 0.000 claims 1
- 241000282412 Homo Species 0.000 abstract description 38
- 108091007433 antigens Proteins 0.000 abstract description 27
- 102000036639 antigens Human genes 0.000 abstract description 27
- 239000000427 antigen Substances 0.000 abstract description 24
- 210000002966 serum Anatomy 0.000 abstract description 15
- 230000028993 immune response Effects 0.000 abstract description 9
- 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 abstract description 7
- 230000002829 reductive effect Effects 0.000 abstract description 6
- 230000002255 enzymatic effect Effects 0.000 abstract description 5
- 239000002253 acid Substances 0.000 abstract description 4
- 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 abstract description 3
- -1 α-galactosyl Chemical group 0.000 abstract description 3
- 210000004102 animal cell Anatomy 0.000 abstract description 2
- 230000028709 inflammatory response Effects 0.000 abstract description 2
- 239000000126 substance Substances 0.000 abstract description 2
- 210000004369 blood Anatomy 0.000 description 28
- 239000008280 blood Substances 0.000 description 28
- 108020004414 DNA Proteins 0.000 description 27
- 102000004190 Enzymes Human genes 0.000 description 25
- 108090000790 Enzymes Proteins 0.000 description 25
- 229940088598 enzyme Drugs 0.000 description 25
- 102000005840 alpha-Galactosidase Human genes 0.000 description 23
- 108010030291 alpha-Galactosidase Proteins 0.000 description 23
- FHIVAFMUCKRCQO-UHFFFAOYSA-N diazinon Chemical compound CCOP(=S)(OCC)OC1=CC(C)=NC(C(C)C)=N1 FHIVAFMUCKRCQO-UHFFFAOYSA-N 0.000 description 20
- SQVRNKJHWKZAKO-UHFFFAOYSA-N beta-N-Acetyl-D-neuraminic acid Natural products CC(=O)NC1C(O)CC(O)(C(O)=O)OC1C(O)C(O)CO SQVRNKJHWKZAKO-UHFFFAOYSA-N 0.000 description 19
- SQVRNKJHWKZAKO-PFQGKNLYSA-N N-acetyl-beta-neuraminic acid Chemical compound CC(=O)N[C@@H]1[C@@H](O)C[C@@](O)(C(O)=O)O[C@H]1[C@H](O)[C@H](O)CO SQVRNKJHWKZAKO-PFQGKNLYSA-N 0.000 description 17
- 150000001720 carbohydrates Chemical group 0.000 description 17
- 241000282898 Sus scrofa Species 0.000 description 14
- 238000002347 injection Methods 0.000 description 13
- 239000007924 injection Substances 0.000 description 13
- 238000012546 transfer Methods 0.000 description 12
- 210000001161 mammalian embryo Anatomy 0.000 description 11
- 230000001404 mediated effect Effects 0.000 description 11
- 206010018910 Haemolysis Diseases 0.000 description 10
- 235000014633 carbohydrates Nutrition 0.000 description 10
- 230000000694 effects Effects 0.000 description 10
- 239000012634 fragment Substances 0.000 description 10
- 230000008588 hemolysis Effects 0.000 description 10
- 235000000346 sugar Nutrition 0.000 description 10
- 102000005348 Neuraminidase Human genes 0.000 description 9
- 108010006232 Neuraminidase Proteins 0.000 description 9
- 239000013598 vector Substances 0.000 description 9
- 102000001554 Hemoglobins Human genes 0.000 description 8
- 108010054147 Hemoglobins Proteins 0.000 description 8
- 102100039373 Membrane cofactor protein Human genes 0.000 description 8
- 241000288906 Primates Species 0.000 description 8
- 238000013459 approach Methods 0.000 description 8
- 238000000338 in vitro Methods 0.000 description 7
- 241000894007 species Species 0.000 description 7
- 230000001225 therapeutic effect Effects 0.000 description 7
- 238000001890 transfection Methods 0.000 description 7
- 108090000288 Glycoproteins Proteins 0.000 description 6
- 102000003886 Glycoproteins Human genes 0.000 description 6
- 241000699670 Mus sp. Species 0.000 description 6
- 108091028043 Nucleic acid sequence Proteins 0.000 description 6
- 238000010367 cloning Methods 0.000 description 6
- 239000002299 complementary DNA Substances 0.000 description 6
- 230000009089 cytolysis Effects 0.000 description 6
- 238000001727 in vivo Methods 0.000 description 6
- 239000003112 inhibitor Substances 0.000 description 6
- 229940060155 neuac Drugs 0.000 description 6
- 150000007523 nucleic acids Chemical group 0.000 description 6
- 239000000523 sample Substances 0.000 description 6
- 230000009261 transgenic effect Effects 0.000 description 6
- 241000699666 Mus <mouse, genus> Species 0.000 description 5
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 5
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 5
- 108090000141 Sialyltransferases Proteins 0.000 description 5
- 102000003838 Sialyltransferases Human genes 0.000 description 5
- 238000002105 Southern blotting Methods 0.000 description 5
- 210000000349 chromosome Anatomy 0.000 description 5
- 230000024203 complement activation Effects 0.000 description 5
- 230000006378 damage Effects 0.000 description 5
- 238000004520 electroporation Methods 0.000 description 5
- 210000002257 embryonic structure Anatomy 0.000 description 5
- 238000002474 experimental method Methods 0.000 description 5
- 238000000684 flow cytometry Methods 0.000 description 5
- 238000011534 incubation Methods 0.000 description 5
- 208000015181 infectious disease Diseases 0.000 description 5
- 238000000520 microinjection Methods 0.000 description 5
- 230000008569 process Effects 0.000 description 5
- 238000012216 screening Methods 0.000 description 5
- 239000000758 substrate Substances 0.000 description 5
- 108010009575 CD55 Antigens Proteins 0.000 description 4
- 108010034753 Complement Membrane Attack Complex Proteins 0.000 description 4
- 102100025680 Complement decay-accelerating factor Human genes 0.000 description 4
- 241001272567 Hominoidea Species 0.000 description 4
- 101000856022 Homo sapiens Complement decay-accelerating factor Proteins 0.000 description 4
- 101000961414 Homo sapiens Membrane cofactor protein Proteins 0.000 description 4
- 108010052285 Membrane Proteins Proteins 0.000 description 4
- 101710146216 Membrane cofactor protein Proteins 0.000 description 4
- 241000282577 Pan troglodytes Species 0.000 description 4
- 241000881705 Porcine endogenous retrovirus Species 0.000 description 4
- 238000003556 assay Methods 0.000 description 4
- 230000008901 benefit Effects 0.000 description 4
- 239000004074 complement inhibitor Substances 0.000 description 4
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 4
- 239000003814 drug Substances 0.000 description 4
- 229940079593 drug Drugs 0.000 description 4
- 210000001671 embryonic stem cell Anatomy 0.000 description 4
- 238000005516 engineering process Methods 0.000 description 4
- 230000006870 function Effects 0.000 description 4
- 210000002216 heart Anatomy 0.000 description 4
- 230000002401 inhibitory effect Effects 0.000 description 4
- 210000001672 ovary Anatomy 0.000 description 4
- 210000003101 oviduct Anatomy 0.000 description 4
- 230000004044 response Effects 0.000 description 4
- 241001430294 unidentified retrovirus Species 0.000 description 4
- 108091026890 Coding region Proteins 0.000 description 3
- 102100022133 Complement C3 Human genes 0.000 description 3
- 229940124073 Complement inhibitor Drugs 0.000 description 3
- 108700024394 Exon Proteins 0.000 description 3
- 101000901154 Homo sapiens Complement C3 Proteins 0.000 description 3
- 108091092195 Intron Proteins 0.000 description 3
- HESSGHHCXGBPAJ-UHFFFAOYSA-N N-acetyllactosamine Natural products CC(=O)NC(C=O)C(O)C(C(O)CO)OC1OC(CO)C(O)C(O)C1O HESSGHHCXGBPAJ-UHFFFAOYSA-N 0.000 description 3
- SUHQNCLNRUAGOO-UHFFFAOYSA-N N-glycoloyl-neuraminic acid Natural products OCC(O)C(O)C(O)C(NC(=O)CO)C(O)CC(=O)C(O)=O SUHQNCLNRUAGOO-UHFFFAOYSA-N 0.000 description 3
- FDJKUWYYUZCUJX-UHFFFAOYSA-N N-glycolyl-beta-neuraminic acid Natural products OCC(O)C(O)C1OC(O)(C(O)=O)CC(O)C1NC(=O)CO FDJKUWYYUZCUJX-UHFFFAOYSA-N 0.000 description 3
- 241000700605 Viruses Species 0.000 description 3
- 230000002776 aggregation Effects 0.000 description 3
- 238000004220 aggregation Methods 0.000 description 3
- 230000000735 allogeneic effect Effects 0.000 description 3
- 150000001413 amino acids Chemical class 0.000 description 3
- 230000015572 biosynthetic process Effects 0.000 description 3
- 210000000601 blood cell Anatomy 0.000 description 3
- 229910000389 calcium phosphate Inorganic materials 0.000 description 3
- 239000001506 calcium phosphate Substances 0.000 description 3
- 235000011010 calcium phosphates Nutrition 0.000 description 3
- 238000006243 chemical reaction Methods 0.000 description 3
- 230000002950 deficient Effects 0.000 description 3
- 238000011161 development Methods 0.000 description 3
- 230000029087 digestion Effects 0.000 description 3
- 201000010099 disease Diseases 0.000 description 3
- 230000006801 homologous recombination Effects 0.000 description 3
- 238000002744 homologous recombination Methods 0.000 description 3
- 230000001939 inductive effect Effects 0.000 description 3
- 230000002458 infectious effect Effects 0.000 description 3
- 230000007246 mechanism Effects 0.000 description 3
- 239000000203 mixture Substances 0.000 description 3
- 230000036961 partial effect Effects 0.000 description 3
- 239000002953 phosphate buffered saline Substances 0.000 description 3
- 239000013612 plasmid Substances 0.000 description 3
- 238000001556 precipitation Methods 0.000 description 3
- 229960000160 recombinant therapeutic protein Drugs 0.000 description 3
- 230000006798 recombination Effects 0.000 description 3
- 230000001105 regulatory effect Effects 0.000 description 3
- 238000010561 standard procedure Methods 0.000 description 3
- 230000004083 survival effect Effects 0.000 description 3
- 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 3
- KFEUJDWYNGMDBV-UHFFFAOYSA-N (N-Acetyl)-glucosamin-4-beta-galaktosid Natural products OC1C(NC(=O)C)C(O)OC(CO)C1OC1C(O)C(O)C(O)C(CO)O1 KFEUJDWYNGMDBV-UHFFFAOYSA-N 0.000 description 2
- FWMNVWWHGCHHJJ-SKKKGAJSSA-N 4-amino-1-[(2r)-6-amino-2-[[(2r)-2-[[(2r)-2-[[(2r)-2-amino-3-phenylpropanoyl]amino]-3-phenylpropanoyl]amino]-4-methylpentanoyl]amino]hexanoyl]piperidine-4-carboxylic acid Chemical compound C([C@H](C(=O)N[C@H](CC(C)C)C(=O)N[C@H](CCCCN)C(=O)N1CCC(N)(CC1)C(O)=O)NC(=O)[C@H](N)CC=1C=CC=CC=1)C1=CC=CC=C1 FWMNVWWHGCHHJJ-SKKKGAJSSA-N 0.000 description 2
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 2
- 239000012594 Earle’s Balanced Salt Solution Substances 0.000 description 2
- 108010019236 Fucosyltransferases Proteins 0.000 description 2
- 102000006471 Fucosyltransferases Human genes 0.000 description 2
- 108060003306 Galactosyltransferase Proteins 0.000 description 2
- 102000030902 Galactosyltransferase Human genes 0.000 description 2
- 241000287828 Gallus gallus Species 0.000 description 2
- 101000802660 Homo sapiens Histo-blood group ABO system transferase Proteins 0.000 description 2
- 241000725303 Human immunodeficiency virus Species 0.000 description 2
- 102000004157 Hydrolases Human genes 0.000 description 2
- 108090000604 Hydrolases Proteins 0.000 description 2
- 108090001090 Lectins Proteins 0.000 description 2
- 102000004856 Lectins Human genes 0.000 description 2
- 241000124008 Mammalia Species 0.000 description 2
- 102000018697 Membrane Proteins Human genes 0.000 description 2
- 206010027476 Metastases Diseases 0.000 description 2
- KFEUJDWYNGMDBV-LODBTCKLSA-N N-acetyllactosamine Chemical compound O[C@@H]1[C@@H](NC(=O)C)[C@H](O)O[C@H](CO)[C@H]1O[C@H]1[C@H](O)[C@@H](O)[C@@H](O)[C@@H](CO)O1 KFEUJDWYNGMDBV-LODBTCKLSA-N 0.000 description 2
- 229930193140 Neomycin Natural products 0.000 description 2
- 241000282579 Pan Species 0.000 description 2
- 239000002202 Polyethylene glycol Substances 0.000 description 2
- 241000700159 Rattus Species 0.000 description 2
- 206010052779 Transplant rejections Diseases 0.000 description 2
- 238000002835 absorbance Methods 0.000 description 2
- 150000007513 acids Chemical class 0.000 description 2
- 230000001154 acute effect Effects 0.000 description 2
- 238000004458 analytical method Methods 0.000 description 2
- 239000003242 anti bacterial agent Substances 0.000 description 2
- 230000009833 antibody interaction Effects 0.000 description 2
- 230000005875 antibody response Effects 0.000 description 2
- 238000003491 array Methods 0.000 description 2
- 230000003115 biocidal effect Effects 0.000 description 2
- 210000002459 blastocyst Anatomy 0.000 description 2
- 210000001185 bone marrow Anatomy 0.000 description 2
- 238000009395 breeding Methods 0.000 description 2
- 230000001488 breeding effect Effects 0.000 description 2
- 230000006037 cell lysis Effects 0.000 description 2
- 238000005119 centrifugation Methods 0.000 description 2
- 235000013330 chicken meat Nutrition 0.000 description 2
- 230000034994 death Effects 0.000 description 2
- 231100000517 death Toxicity 0.000 description 2
- 230000003111 delayed effect Effects 0.000 description 2
- 238000002283 elective surgery Methods 0.000 description 2
- 210000002889 endothelial cell Anatomy 0.000 description 2
- 210000003989 endothelium vascular Anatomy 0.000 description 2
- 210000002919 epithelial cell Anatomy 0.000 description 2
- 230000008348 humoral response Effects 0.000 description 2
- 238000010348 incorporation Methods 0.000 description 2
- 208000014674 injury Diseases 0.000 description 2
- 238000003780 insertion Methods 0.000 description 2
- 230000037431 insertion Effects 0.000 description 2
- 239000002523 lectin Substances 0.000 description 2
- 230000000670 limiting effect Effects 0.000 description 2
- 210000004185 liver Anatomy 0.000 description 2
- 210000004072 lung Anatomy 0.000 description 2
- 239000003550 marker Substances 0.000 description 2
- 230000013011 mating Effects 0.000 description 2
- 210000004379 membrane Anatomy 0.000 description 2
- 239000012528 membrane Substances 0.000 description 2
- 230000004060 metabolic process Effects 0.000 description 2
- 230000009401 metastasis Effects 0.000 description 2
- 229960004927 neomycin Drugs 0.000 description 2
- 230000005937 nuclear translocation Effects 0.000 description 2
- 210000004940 nucleus Anatomy 0.000 description 2
- 229920001542 oligosaccharide Polymers 0.000 description 2
- 150000002482 oligosaccharides Chemical class 0.000 description 2
- 238000004806 packaging method and process Methods 0.000 description 2
- 229920001223 polyethylene glycol Polymers 0.000 description 2
- 238000005215 recombination Methods 0.000 description 2
- 230000009467 reduction Effects 0.000 description 2
- 230000001177 retroviral effect Effects 0.000 description 2
- SQVRNKJHWKZAKO-OQPLDHBCSA-N sialic acid Chemical compound CC(=O)N[C@@H]1[C@@H](O)C[C@@](O)(C(O)=O)OC1[C@H](O)[C@H](O)CO SQVRNKJHWKZAKO-OQPLDHBCSA-N 0.000 description 2
- 239000000243 solution Substances 0.000 description 2
- 150000008163 sugars Chemical class 0.000 description 2
- 208000001608 teratocarcinoma Diseases 0.000 description 2
- 238000012360 testing method Methods 0.000 description 2
- 230000008733 trauma Effects 0.000 description 2
- 210000004291 uterus Anatomy 0.000 description 2
- 230000003612 virological effect Effects 0.000 description 2
- KRHRWPPVNXJWRG-LUWBGTNYSA-N (4S,5R,6R)-5-acetamido-4-hydroxy-2-phosphonooxy-6-[(1R,2R)-1,2,3-trihydroxypropyl]oxane-2-carboxylic acid Chemical compound P(=O)(O)(O)OC1(C(O)=O)C[C@H](O)[C@@H](NC(C)=O)[C@@H](O1)[C@H](O)[C@H](O)CO KRHRWPPVNXJWRG-LUWBGTNYSA-N 0.000 description 1
- UHDGCWIWMRVCDJ-UHFFFAOYSA-N 1-beta-D-Xylofuranosyl-NH-Cytosine Natural products O=C1N=C(N)C=CN1C1C(O)C(O)C(CO)O1 UHDGCWIWMRVCDJ-UHFFFAOYSA-N 0.000 description 1
- HVCOBJNICQPDBP-UHFFFAOYSA-N 3-[3-[3,5-dihydroxy-6-methyl-4-(3,4,5-trihydroxy-6-methyloxan-2-yl)oxyoxan-2-yl]oxydecanoyloxy]decanoic acid;hydrate Chemical group O.OC1C(OC(CC(=O)OC(CCCCCCC)CC(O)=O)CCCCCCC)OC(C)C(O)C1OC1C(O)C(O)C(O)C(C)O1 HVCOBJNICQPDBP-UHFFFAOYSA-N 0.000 description 1
- 210000002925 A-like Anatomy 0.000 description 1
- 241000894006 Bacteria Species 0.000 description 1
- 241000283690 Bos taurus Species 0.000 description 1
- 239000004215 Carbon black (E152) Substances 0.000 description 1
- 102000016574 Complement C3-C5 Convertases Human genes 0.000 description 1
- 108010067641 Complement C3-C5 Convertases Proteins 0.000 description 1
- 108020004635 Complementary DNA Proteins 0.000 description 1
- 208000020406 Creutzfeldt Jacob disease Diseases 0.000 description 1
- 208000003407 Creutzfeldt-Jakob Syndrome Diseases 0.000 description 1
- 208000010859 Creutzfeldt-Jakob disease Diseases 0.000 description 1
- 241000699800 Cricetinae Species 0.000 description 1
- 241000699802 Cricetulus griseus Species 0.000 description 1
- PMATZTZNYRCHOR-CGLBZJNRSA-N Cyclosporin A Chemical compound CC[C@@H]1NC(=O)[C@H]([C@H](O)[C@H](C)C\C=C\C)N(C)C(=O)[C@H](C(C)C)N(C)C(=O)[C@H](CC(C)C)N(C)C(=O)[C@H](CC(C)C)N(C)C(=O)[C@@H](C)NC(=O)[C@H](C)NC(=O)[C@H](CC(C)C)N(C)C(=O)[C@H](C(C)C)NC(=O)[C@H](CC(C)C)N(C)C(=O)CN(C)C1=O PMATZTZNYRCHOR-CGLBZJNRSA-N 0.000 description 1
- 108010036949 Cyclosporine Proteins 0.000 description 1
- UHDGCWIWMRVCDJ-PSQAKQOGSA-N Cytidine Natural products O=C1N=C(N)C=CN1[C@@H]1[C@@H](O)[C@@H](O)[C@H](CO)O1 UHDGCWIWMRVCDJ-PSQAKQOGSA-N 0.000 description 1
- 239000012591 Dulbecco’s Phosphate Buffered Saline Substances 0.000 description 1
- 239000006144 Dulbecco’s modified Eagle's medium Substances 0.000 description 1
- 101150099983 GT gene Proteins 0.000 description 1
- 206010064571 Gene mutation Diseases 0.000 description 1
- 229930186217 Glycolipid Natural products 0.000 description 1
- 102000005744 Glycoside Hydrolases Human genes 0.000 description 1
- 108010031186 Glycoside Hydrolases Proteins 0.000 description 1
- 102000006771 Gonadotropins Human genes 0.000 description 1
- 108010086677 Gonadotropins Proteins 0.000 description 1
- 241000173677 Griffinia Species 0.000 description 1
- 208000032843 Hemorrhage Diseases 0.000 description 1
- 241000711549 Hepacivirus C Species 0.000 description 1
- 101100386242 Homo sapiens CD55 gene Proteins 0.000 description 1
- 101100495234 Homo sapiens CD59 gene Proteins 0.000 description 1
- 101000897400 Homo sapiens CD59 glycoprotein Proteins 0.000 description 1
- 108010003272 Hyaluronate lyase Proteins 0.000 description 1
- 102000009066 Hyaluronoglucosaminidase Human genes 0.000 description 1
- 241000581650 Ivesia Species 0.000 description 1
- 108010074633 Mixed Function Oxygenases Proteins 0.000 description 1
- 102000008109 Mixed Function Oxygenases Human genes 0.000 description 1
- 241001529936 Murinae Species 0.000 description 1
- 206010030113 Oedema Diseases 0.000 description 1
- 108700026244 Open Reading Frames Proteins 0.000 description 1
- 238000012408 PCR amplification Methods 0.000 description 1
- 101000902206 Pan troglodytes Cytidine monophosphate-N-acetylneuraminic acid hydroxylase Proteins 0.000 description 1
- 241001494479 Pecora Species 0.000 description 1
- 102000001938 Plasminogen Activators Human genes 0.000 description 1
- 108010001014 Plasminogen Activators Proteins 0.000 description 1
- 244000170475 Saraca indica Species 0.000 description 1
- 235000016135 Saraca indica Nutrition 0.000 description 1
- 206010070834 Sensitisation Diseases 0.000 description 1
- 241000533293 Sesbania emerus Species 0.000 description 1
- 206010042573 Superovulation Diseases 0.000 description 1
- 108700019146 Transgenes Proteins 0.000 description 1
- 240000003864 Ulex europaeus Species 0.000 description 1
- 235000010730 Ulex europaeus Nutrition 0.000 description 1
- HMNZFMSWFCAGGW-XPWSMXQVSA-N [3-[hydroxy(2-hydroxyethoxy)phosphoryl]oxy-2-[(e)-octadec-9-enoyl]oxypropyl] (e)-octadec-9-enoate Chemical compound CCCCCCCC\C=C\CCCCCCCC(=O)OCC(COP(O)(=O)OCCO)OC(=O)CCCCCCC\C=C\CCCCCCCC HMNZFMSWFCAGGW-XPWSMXQVSA-N 0.000 description 1
- 238000002679 ablation Methods 0.000 description 1
- 238000009825 accumulation Methods 0.000 description 1
- 239000011543 agarose gel Substances 0.000 description 1
- 230000004520 agglutination Effects 0.000 description 1
- 125000003275 alpha amino acid group Chemical group 0.000 description 1
- GZCGUPFRVQAUEE-UHFFFAOYSA-N alpha-D-galactose Natural products OCC(O)C(O)C(O)C(O)C=O GZCGUPFRVQAUEE-UHFFFAOYSA-N 0.000 description 1
- 229940126575 aminoglycoside Drugs 0.000 description 1
- 229960000723 ampicillin Drugs 0.000 description 1
- AVKUERGKIZMTKX-NJBDSQKTSA-N ampicillin Chemical compound C1([C@@H](N)C(=O)N[C@H]2[C@H]3SC([C@@H](N3C2=O)C(O)=O)(C)C)=CC=CC=C1 AVKUERGKIZMTKX-NJBDSQKTSA-N 0.000 description 1
- 210000003484 anatomy Anatomy 0.000 description 1
- 230000008827 biological function Effects 0.000 description 1
- 239000003633 blood substitute Substances 0.000 description 1
- 230000036770 blood supply Effects 0.000 description 1
- 229940098773 bovine serum albumin Drugs 0.000 description 1
- 239000000872 buffer Substances 0.000 description 1
- 238000010370 cell cloning Methods 0.000 description 1
- 210000000038 chest Anatomy 0.000 description 1
- 229960001265 ciclosporin Drugs 0.000 description 1
- 238000011260 co-administration Methods 0.000 description 1
- 230000002860 competitive effect Effects 0.000 description 1
- 238000010276 construction Methods 0.000 description 1
- 230000001276 controlling effect Effects 0.000 description 1
- 230000009260 cross reactivity Effects 0.000 description 1
- 238000009402 cross-breeding Methods 0.000 description 1
- 238000012258 culturing Methods 0.000 description 1
- 229930182912 cyclosporin Natural products 0.000 description 1
- UHDGCWIWMRVCDJ-ZAKLUEHWSA-N cytidine Chemical group O=C1N=C(N)C=CN1[C@H]1[C@H](O)[C@@H](O)[C@H](CO)O1 UHDGCWIWMRVCDJ-ZAKLUEHWSA-N 0.000 description 1
- 231100000433 cytotoxic Toxicity 0.000 description 1
- 230000001472 cytotoxic effect Effects 0.000 description 1
- 238000012217 deletion Methods 0.000 description 1
- 230000037430 deletion Effects 0.000 description 1
- 238000010586 diagram Methods 0.000 description 1
- 150000002016 disaccharides Chemical class 0.000 description 1
- 208000035475 disorder Diseases 0.000 description 1
- 238000009826 distribution Methods 0.000 description 1
- 231100000673 dose–response relationship Toxicity 0.000 description 1
- 230000009977 dual effect Effects 0.000 description 1
- 230000002526 effect on cardiovascular system Effects 0.000 description 1
- 210000002308 embryonic cell Anatomy 0.000 description 1
- 230000003511 endothelial effect Effects 0.000 description 1
- 239000002158 endotoxin Substances 0.000 description 1
- 230000009144 enzymatic modification Effects 0.000 description 1
- 208000002854 epidermolysis bullosa simplex superficialis Diseases 0.000 description 1
- 230000010437 erythropoiesis Effects 0.000 description 1
- 210000003527 eukaryotic cell Anatomy 0.000 description 1
- 230000001747 exhibiting effect Effects 0.000 description 1
- 230000002349 favourable effect Effects 0.000 description 1
- 239000012894 fetal calf serum Substances 0.000 description 1
- 230000001605 fetal effect Effects 0.000 description 1
- 210000002950 fibroblast Anatomy 0.000 description 1
- 239000012530 fluid Substances 0.000 description 1
- 238000009472 formulation Methods 0.000 description 1
- 108010001671 galactoside 3-fucosyltransferase Proteins 0.000 description 1
- IRSCQMHQWWYFCW-UHFFFAOYSA-N ganciclovir Chemical compound O=C1NC(N)=NC2=C1N=CN2COC(CO)CO IRSCQMHQWWYFCW-UHFFFAOYSA-N 0.000 description 1
- 229960002963 ganciclovir Drugs 0.000 description 1
- 210000001156 gastric mucosa Anatomy 0.000 description 1
- 238000012239 gene modification Methods 0.000 description 1
- 230000005017 genetic modification Effects 0.000 description 1
- 235000013617 genetically modified food Nutrition 0.000 description 1
- 150000002339 glycosphingolipids Chemical class 0.000 description 1
- 108091005608 glycosylated proteins Proteins 0.000 description 1
- 102000035122 glycosylated proteins Human genes 0.000 description 1
- 230000013595 glycosylation Effects 0.000 description 1
- 238000006206 glycosylation reaction Methods 0.000 description 1
- 210000002149 gonad Anatomy 0.000 description 1
- 239000002622 gonadotropin Substances 0.000 description 1
- 230000035931 haemagglutination Effects 0.000 description 1
- 230000036541 health Effects 0.000 description 1
- 230000008821 health effect Effects 0.000 description 1
- 238000005534 hematocrit Methods 0.000 description 1
- 208000006454 hepatitis Diseases 0.000 description 1
- 231100000283 hepatitis Toxicity 0.000 description 1
- 102000056538 human ABO Human genes 0.000 description 1
- 102000051442 human CD59 Human genes 0.000 description 1
- 229960002773 hyaluronidase Drugs 0.000 description 1
- 238000009396 hybridization Methods 0.000 description 1
- 210000004408 hybridoma Anatomy 0.000 description 1
- 229930195733 hydrocarbon Natural products 0.000 description 1
- 125000002887 hydroxy group Chemical group [H]O* 0.000 description 1
- 230000001900 immune effect Effects 0.000 description 1
- 210000000987 immune system Anatomy 0.000 description 1
- 238000003119 immunoblot Methods 0.000 description 1
- 238000011532 immunohistochemical staining Methods 0.000 description 1
- 230000001506 immunosuppresive effect Effects 0.000 description 1
- 229960003444 immunosuppressant agent Drugs 0.000 description 1
- 239000003018 immunosuppressive agent Substances 0.000 description 1
- 238000002650 immunosuppressive therapy Methods 0.000 description 1
- 238000002513 implantation Methods 0.000 description 1
- 230000000415 inactivating effect Effects 0.000 description 1
- 238000001802 infusion Methods 0.000 description 1
- 230000000977 initiatory effect Effects 0.000 description 1
- 230000010354 integration Effects 0.000 description 1
- 230000003993 interaction Effects 0.000 description 1
- 230000003834 intracellular effect Effects 0.000 description 1
- 238000001990 intravenous administration Methods 0.000 description 1
- 230000002427 irreversible effect Effects 0.000 description 1
- 210000003734 kidney Anatomy 0.000 description 1
- 238000001638 lipofection Methods 0.000 description 1
- 229920006008 lipopolysaccharide Polymers 0.000 description 1
- 230000007774 longterm Effects 0.000 description 1
- 230000003211 malignant effect Effects 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 244000005700 microbiome Species 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 150000002772 monosaccharides Chemical class 0.000 description 1
- 230000035772 mutation Effects 0.000 description 1
- 208000010125 myocardial infarction Diseases 0.000 description 1
- 230000025308 nuclear transport Effects 0.000 description 1
- 239000002773 nucleotide Substances 0.000 description 1
- 125000003729 nucleotide group Chemical group 0.000 description 1
- 210000000287 oocyte Anatomy 0.000 description 1
- 230000002611 ovarian Effects 0.000 description 1
- 210000000496 pancreas Anatomy 0.000 description 1
- 244000052769 pathogen Species 0.000 description 1
- 230000037361 pathway Effects 0.000 description 1
- 238000011458 pharmacological treatment Methods 0.000 description 1
- 239000007981 phosphate-citrate buffer Substances 0.000 description 1
- 230000035479 physiological effects, processes and functions Effects 0.000 description 1
- 230000035790 physiological processes and functions Effects 0.000 description 1
- 229940127126 plasminogen activator Drugs 0.000 description 1
- 230000004481 post-translational protein modification Effects 0.000 description 1
- 230000003389 potentiating effect Effects 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 230000002265 prevention Effects 0.000 description 1
- 108020001580 protein domains Proteins 0.000 description 1
- 230000009257 reactivity Effects 0.000 description 1
- 230000000384 rearing effect Effects 0.000 description 1
- 230000003362 replicative effect Effects 0.000 description 1
- 230000002441 reversible effect Effects 0.000 description 1
- 239000006152 selective media Substances 0.000 description 1
- 230000008313 sensitization Effects 0.000 description 1
- 238000012163 sequencing technique Methods 0.000 description 1
- 230000000405 serological effect Effects 0.000 description 1
- 210000003491 skin Anatomy 0.000 description 1
- 210000000813 small intestine Anatomy 0.000 description 1
- 239000007787 solid Substances 0.000 description 1
- 238000001179 sorption measurement Methods 0.000 description 1
- 210000000130 stem cell Anatomy 0.000 description 1
- 230000000638 stimulation Effects 0.000 description 1
- 230000001629 suppression Effects 0.000 description 1
- 238000003239 susceptibility assay Methods 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- 238000002560 therapeutic procedure Methods 0.000 description 1
- 230000002792 vascular Effects 0.000 description 1
- 230000035899 viability Effects 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
Images
Classifications
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K35/00—Medicinal preparations containing materials or reaction products thereof with undetermined constitution
- A61K35/12—Materials from mammals; Compositions comprising non-specified tissues or cells; Compositions comprising non-embryonic stem cells; Genetically modified cells
- A61K35/14—Blood; Artificial blood
- A61K35/18—Erythrocytes
-
- A—HUMAN NECESSITIES
- A01—AGRICULTURE; FORESTRY; ANIMAL HUSBANDRY; HUNTING; TRAPPING; FISHING
- A01K—ANIMAL HUSBANDRY; AVICULTURE; APICULTURE; PISCICULTURE; FISHING; REARING OR BREEDING ANIMALS, NOT OTHERWISE PROVIDED FOR; NEW BREEDS OF ANIMALS
- A01K67/00—Rearing or breeding animals, not otherwise provided for; New or modified breeds of animals
- A01K67/027—New or modified breeds of vertebrates
- A01K67/0271—Chimeric vertebrates, e.g. comprising exogenous cells
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K35/00—Medicinal preparations containing materials or reaction products thereof with undetermined constitution
- A61K35/12—Materials from mammals; Compositions comprising non-specified tissues or cells; Compositions comprising non-embryonic stem cells; Genetically modified cells
-
- A—HUMAN NECESSITIES
- A01—AGRICULTURE; FORESTRY; ANIMAL HUSBANDRY; HUNTING; TRAPPING; FISHING
- A01K—ANIMAL HUSBANDRY; AVICULTURE; APICULTURE; PISCICULTURE; FISHING; REARING OR BREEDING ANIMALS, NOT OTHERWISE PROVIDED FOR; NEW BREEDS OF ANIMALS
- A01K2217/00—Genetically modified animals
- A01K2217/07—Animals genetically altered by homologous recombination
- A01K2217/075—Animals genetically altered by homologous recombination inducing loss of function, i.e. knock out
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Cell Biology (AREA)
- Animal Behavior & Ethology (AREA)
- Zoology (AREA)
- Medicinal Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Developmental Biology & Embryology (AREA)
- Immunology (AREA)
- Virology (AREA)
- Biomedical Technology (AREA)
- Chemical & Material Sciences (AREA)
- Engineering & Computer Science (AREA)
- Pharmacology & Pharmacy (AREA)
- Epidemiology (AREA)
- Environmental Sciences (AREA)
- Biotechnology (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Animal Husbandry (AREA)
- Biodiversity & Conservation Biology (AREA)
- Hematology (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Materials For Medical Uses (AREA)
- Peptides Or Proteins (AREA)
Applications Claiming Priority (4)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US28768401P | 2001-04-30 | 2001-04-30 | |
| US30060401P | 2001-06-22 | 2001-06-22 | |
| US33387601P | 2001-11-28 | 2001-11-28 | |
| PCT/US2002/013564 WO2002088351A1 (en) | 2001-04-30 | 2002-04-29 | Modified organs and cells for xenotransplantation |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JP2004533242A true JP2004533242A (ja) | 2004-11-04 |
| JP2004533242A5 JP2004533242A5 (https=) | 2006-08-24 |
Family
ID=27403740
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2002585632A Pending JP2004533242A (ja) | 2001-04-30 | 2002-04-29 | 異種移植のための改変された器官および細胞 |
Country Status (7)
| Country | Link |
|---|---|
| US (3) | US7166278B2 (https=) |
| EP (1) | EP1383889B1 (https=) |
| JP (1) | JP2004533242A (https=) |
| AU (1) | AU2002308533B2 (https=) |
| CA (1) | CA2445945A1 (https=) |
| ES (1) | ES2530872T3 (https=) |
| WO (1) | WO2002088351A1 (https=) |
Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2008526318A (ja) * | 2004-12-30 | 2008-07-24 | ダイヤモンド,ポール | 器官および組織の細胞再形成促進 |
Families Citing this family (24)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP1639083A4 (en) * | 2003-06-06 | 2008-05-28 | Univ Pittsburgh | GENE OF CMP-N-ACETYLNEURAMIC ACID HYDROXYLASE FROM PIG |
| CA2533259C (en) * | 2003-07-21 | 2014-01-28 | Lifecell Corporation | Acellular tissue matrices made from galactose .alpha.-1,3-galactose-deficient tissue |
| AU2005223617A1 (en) | 2004-03-17 | 2005-09-29 | Revivicor, Inc. | Tissue products from animals lacking functional alpha 1,3 galactosyl transferase |
| JP2006129736A (ja) * | 2004-11-02 | 2006-05-25 | Nippon Dobutsu Kogaku Kenkyusho:Kk | 異種移植用豚細胞、その選抜方法及び異種移植用豚 |
| WO2006074373A2 (en) * | 2005-01-06 | 2006-07-13 | Crosscart, Inc. | Immunochemically modified and sterilized xenografts and allografts |
| EP1893756B1 (en) * | 2005-06-08 | 2015-08-12 | The Regents of The University of California | Elimination of n-glycolylneuraminic acid from mammalian products for human use |
| FI20055398A0 (fi) | 2005-07-08 | 2005-07-08 | Suomen Punainen Risti Veripalv | Menetelmä solupopulaatioiden evaluoimiseksi |
| FI20075030A0 (fi) | 2007-01-18 | 2007-01-18 | Suomen Punainen Risti Veripalv | Menetelmä solujen modifioimiseksi |
| KR101149475B1 (ko) | 2007-11-30 | 2012-05-25 | 한국생명공학연구원 | 이종 장기 이식용 미니 복제돼지 생산을 위한 유전자 조작된 세포주 및 그의 생산방법 |
| EP2166085A1 (en) | 2008-07-16 | 2010-03-24 | Suomen Punainen Risti Veripalvelu | Divalent modified cells |
| EP2324110A4 (en) * | 2008-09-09 | 2013-01-09 | Univ California | ELIMINATION OF A CONTAMINATING NON-HUMAN SIALIC ACID BY METABOLISM COMPETITION |
| US9420770B2 (en) | 2009-12-01 | 2016-08-23 | Indiana University Research & Technology Corporation | Methods of modulating thrombocytopenia and modified transgenic pigs |
| KR101276801B1 (ko) * | 2011-01-21 | 2013-06-19 | 한화엘앤씨 주식회사 | sTNFR1-Fc 유전자를 발현하는 형질전환 돼지 및 이의 용도 |
| WO2013151649A1 (en) | 2012-04-04 | 2013-10-10 | Sialix Inc | Glycan-interacting compounds |
| US20140115728A1 (en) | 2012-10-24 | 2014-04-24 | A. Joseph Tector | Double knockout (gt/cmah-ko) pigs, organs and tissues |
| WO2015066668A1 (en) | 2013-11-04 | 2015-05-07 | Lifecell Corporation | Methods of removing alpha-galactose |
| CA2965550A1 (en) | 2014-10-22 | 2016-04-28 | Indiana University Research & Technology Corporation | Triple transgenic pigs suitable for xenograft |
| FI3218005T3 (fi) | 2014-11-12 | 2023-03-31 | Seagen Inc | Glykaanin kanssa vuorovaikutteisia yhdisteitä ja käyttömenetelmiä |
| US9879087B2 (en) | 2014-11-12 | 2018-01-30 | Siamab Therapeutics, Inc. | Glycan-interacting compounds and methods of use |
| CN116059378A (zh) | 2014-12-10 | 2023-05-05 | 明尼苏达大学董事会 | 用于治疗疾病的遗传修饰的细胞、组织和器官 |
| CA3002097A1 (en) | 2015-11-12 | 2017-05-18 | Siamab Therapeutics, Inc. | Glycan-interacting compounds and methods of use |
| WO2018094143A1 (en) | 2016-11-17 | 2018-05-24 | Siamab Therapeutics, Inc. | Glycan-interacting compounds and methods of use |
| WO2018160909A1 (en) | 2017-03-03 | 2018-09-07 | Siamab Therapeutics, Inc. | Glycan-interacting compounds and methods of use |
| KR102746223B1 (ko) | 2017-04-20 | 2024-12-27 | 이제네시스, 인크. | 유전자 변형 동물의 생성 방법 |
Family Cites Families (8)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPH03255028A (ja) | 1990-03-01 | 1991-11-13 | Imeeji Meekaa:Kk | 免疫抑制剤 |
| WO1992017189A1 (en) | 1991-03-29 | 1992-10-15 | The Regents Of The University Of California | Gangliosides with immunosuppressive activity |
| US6228631B1 (en) * | 1992-10-22 | 2001-05-08 | New York Blood Center, Inc. | Recombinant α-N-acetylgalactosaminidase enzyme and cDNA encoding said enzyme |
| US5330974A (en) * | 1993-03-01 | 1994-07-19 | Fibratek, Inc. | Therapeutic fibrinogen compositions |
| US6331658B1 (en) * | 1993-04-20 | 2001-12-18 | Integris Baptist Medical Center, Inc. | Genetically engineered mammals for use as organ donors |
| JPH09508277A (ja) | 1994-01-27 | 1997-08-26 | ブレサゲン リミテッド | ヒト異種移植における超急性拒絶の管理のための物質及び方法 |
| US6166288A (en) * | 1995-09-27 | 2000-12-26 | Nextran Inc. | Method of producing transgenic animals for xenotransplantation expressing both an enzyme masking or reducing the level of the gal epitope and a complement inhibitor |
| US6245890B1 (en) * | 1999-03-26 | 2001-06-12 | New York Blood Center, Inc. | Porcine protein and uses thereof |
-
2002
- 2002-04-29 US US10/135,919 patent/US7166278B2/en not_active Expired - Lifetime
- 2002-04-29 ES ES02766869T patent/ES2530872T3/es not_active Expired - Lifetime
- 2002-04-29 WO PCT/US2002/013564 patent/WO2002088351A1/en not_active Ceased
- 2002-04-29 EP EP02766869.8A patent/EP1383889B1/en not_active Expired - Lifetime
- 2002-04-29 CA CA002445945A patent/CA2445945A1/en not_active Abandoned
- 2002-04-29 JP JP2002585632A patent/JP2004533242A/ja active Pending
- 2002-04-29 AU AU2002308533A patent/AU2002308533B2/en not_active Ceased
-
2006
- 2006-11-20 US US11/561,470 patent/US8034330B2/en not_active Expired - Fee Related
-
2011
- 2011-08-16 US US13/211,040 patent/US20110301341A1/en not_active Abandoned
Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2008526318A (ja) * | 2004-12-30 | 2008-07-24 | ダイヤモンド,ポール | 器官および組織の細胞再形成促進 |
Also Published As
| Publication number | Publication date |
|---|---|
| EP1383889A1 (en) | 2004-01-28 |
| EP1383889A4 (en) | 2005-01-26 |
| US20070089178A1 (en) | 2007-04-19 |
| US20110301341A1 (en) | 2011-12-08 |
| CA2445945A1 (en) | 2002-11-07 |
| ES2530872T3 (es) | 2015-03-06 |
| US8034330B2 (en) | 2011-10-11 |
| AU2002308533B2 (en) | 2007-07-19 |
| WO2002088351A1 (en) | 2002-11-07 |
| US7166278B2 (en) | 2007-01-23 |
| EP1383889B1 (en) | 2014-11-19 |
| US20030165480A1 (en) | 2003-09-04 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| US20110301341A1 (en) | Modified organs and cells for xenotransplantation | |
| AU2002308533A1 (en) | Modified organs and cells for xenotransplantation | |
| US6331658B1 (en) | Genetically engineered mammals for use as organ donors | |
| Peterson et al. | Physiological basis for xenotransplantation from genetically modified pigs to humans | |
| Cooper | Xenoantigens and xenoantibodies | |
| Joziasse et al. | Xenotransplantation: the importance of the Galα1, 3Gal epitope in hyperacute vascular rejection | |
| Ezzelarab et al. | Carbohydrates in xenotransplantation | |
| JP2001517924A (ja) | 抗体媒介性拒絶反応を低減させた異種移植のためのトランスジェニック動物 | |
| Sandrin et al. | Recent advances in xenotransplantation | |
| US20060147429A1 (en) | Facilitated cellular reconstitution of organs and tissues | |
| US7485769B2 (en) | Transgenic mammals | |
| Pearse et al. | Anti-xenograft immune responses in α1, 3-galactosyltransferase knock-out mice | |
| AU6144598A (en) | Tolerance to natural antibody antigens | |
| US20240294869A1 (en) | Pig xenotransplants into humans without chronic immunosuppression | |
| Platt | Genetic modification of xenografts | |
| Bohuslavskyi et al. | Gal-a-1, 3-Gal Epitope: Role in Cell Biology and Transplantation | |
| US20020114787A1 (en) | Tolerance to natural antibody antigens | |
| Knosalla et al. | The Immunology of Xenotransplantation | |
| Diamond | Progress in xenotransplantation | |
| Braidley et al. | thoracic organ xenotransplantation | |
| Tange et al. | Galα1–3Gal Xenoepitope: Donor-Targeted Genetic Strategies | |
| Madsen | and Ruediger Hoerbelt, MD | |
| JP2002291372A (ja) | トランスジェニック哺乳動物 |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| A621 | Written request for application examination |
Free format text: JAPANESE INTERMEDIATE CODE: A621 Effective date: 20050427 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20060707 |
|
| A131 | Notification of reasons for refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A131 Effective date: 20080331 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20080630 |
|
| A02 | Decision of refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A02 Effective date: 20090603 |