JPH06506205A - 創傷治療 - Google Patents
創傷治療Info
- Publication number
- JPH06506205A JPH06506205A JP4506944A JP50694492A JPH06506205A JP H06506205 A JPH06506205 A JP H06506205A JP 4506944 A JP4506944 A JP 4506944A JP 50694492 A JP50694492 A JP 50694492A JP H06506205 A JPH06506205 A JP H06506205A
- Authority
- JP
- Japan
- Prior art keywords
- composition
- growth factor
- wound
- composition according
- neutralizing agent
- 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.)
- Granted
Links
- 208000027418 Wounds and injury Diseases 0.000 title claims description 93
- 206010052428 Wound Diseases 0.000 title claims description 87
- 238000011282 treatment Methods 0.000 title claims description 46
- 239000003102 growth factor Substances 0.000 claims description 114
- 239000000203 mixture Substances 0.000 claims description 66
- 230000003472 neutralizing effect Effects 0.000 claims description 61
- 239000003795 chemical substances by application Substances 0.000 claims description 36
- 238000000034 method Methods 0.000 claims description 36
- 230000000694 effects Effects 0.000 claims description 22
- 230000015572 biosynthetic process Effects 0.000 claims description 21
- 238000002347 injection Methods 0.000 claims description 17
- 239000007924 injection Substances 0.000 claims description 17
- 231100000241 scar Toxicity 0.000 claims description 16
- 239000003112 inhibitor Substances 0.000 claims description 15
- 102000005962 receptors Human genes 0.000 claims description 14
- 108020003175 receptors Proteins 0.000 claims description 14
- 230000008569 process Effects 0.000 claims description 12
- 230000009772 tissue formation Effects 0.000 claims description 9
- 108020004999 messenger RNA Proteins 0.000 claims description 7
- 239000008194 pharmaceutical composition Substances 0.000 claims description 7
- 108090000765 processed proteins & peptides Proteins 0.000 claims description 7
- 239000006071 cream Substances 0.000 claims description 6
- 239000007788 liquid Substances 0.000 claims description 6
- 230000000699 topical effect Effects 0.000 claims description 6
- 230000002401 inhibitory effect Effects 0.000 claims description 5
- 239000000843 powder Substances 0.000 claims description 5
- 102000004127 Cytokines Human genes 0.000 claims description 4
- 108090000695 Cytokines Proteins 0.000 claims description 4
- 108090000790 Enzymes Proteins 0.000 claims description 4
- 102000004190 Enzymes Human genes 0.000 claims description 4
- 102000009465 Growth Factor Receptors Human genes 0.000 claims description 4
- 108010009202 Growth Factor Receptors Proteins 0.000 claims description 4
- 239000000443 aerosol Substances 0.000 claims description 4
- 239000002775 capsule Substances 0.000 claims description 4
- 239000003937 drug carrier Substances 0.000 claims description 4
- 230000001629 suppression Effects 0.000 claims description 4
- 238000002604 ultrasonography Methods 0.000 claims description 4
- 239000000074 antisense oligonucleotide Substances 0.000 claims description 3
- 238000012230 antisense oligonucleotides Methods 0.000 claims description 3
- 238000013270 controlled release Methods 0.000 claims description 3
- 239000007943 implant Substances 0.000 claims description 3
- 238000001727 in vivo Methods 0.000 claims description 3
- 230000002262 irrigation Effects 0.000 claims description 3
- 238000003973 irrigation Methods 0.000 claims description 3
- 229920000642 polymer Polymers 0.000 claims description 3
- 239000000243 solution Substances 0.000 claims description 3
- 102000004954 Biglycan Human genes 0.000 claims description 2
- 108090001138 Biglycan Proteins 0.000 claims description 2
- 102000004237 Decorin Human genes 0.000 claims description 2
- 108090000738 Decorin Proteins 0.000 claims description 2
- 239000002250 absorbent Substances 0.000 claims description 2
- 230000002745 absorbent Effects 0.000 claims description 2
- 239000000654 additive Substances 0.000 claims description 2
- 230000000996 additive effect Effects 0.000 claims description 2
- 230000003176 fibrotic effect Effects 0.000 claims description 2
- 238000002513 implantation Methods 0.000 claims description 2
- 230000007935 neutral effect Effects 0.000 claims description 2
- 238000002360 preparation method Methods 0.000 claims description 2
- 239000008174 sterile solution Substances 0.000 claims description 2
- 230000000638 stimulation Effects 0.000 claims description 2
- 108091034117 Oligonucleotide Proteins 0.000 claims 1
- 229920001222 biopolymer Polymers 0.000 claims 1
- 230000002779 inactivation Effects 0.000 claims 1
- 108010017843 platelet-derived growth factor A Proteins 0.000 claims 1
- 230000001568 sexual effect Effects 0.000 claims 1
- ZRKFYGHZFMAOKI-QMGMOQQFSA-N tgfbeta Chemical compound C([C@H](NC(=O)[C@H](C(C)C)NC(=O)CNC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H]([C@@H](C)O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H]([C@@H](C)O)NC(=O)[C@H](CC(C)C)NC(=O)CNC(=O)[C@H](C)NC(=O)[C@H](CO)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@@H](NC(=O)[C@H](C)NC(=O)[C@H](C)NC(=O)[C@@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](N)CCSC)C(C)C)[C@@H](C)CC)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](C)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](C)C(=O)N[C@@H](CC(C)C)C(=O)N1[C@@H](CCC1)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(C)C)C(O)=O)C1=CC=C(O)C=C1 ZRKFYGHZFMAOKI-QMGMOQQFSA-N 0.000 description 22
- 102000010780 Platelet-Derived Growth Factor Human genes 0.000 description 21
- 108010038512 Platelet-Derived Growth Factor Proteins 0.000 description 21
- 102000004887 Transforming Growth Factor beta Human genes 0.000 description 21
- 108090001012 Transforming Growth Factor beta Proteins 0.000 description 21
- 210000001519 tissue Anatomy 0.000 description 21
- 102000008186 Collagen Human genes 0.000 description 14
- 108010035532 Collagen Proteins 0.000 description 14
- 229920001436 collagen Polymers 0.000 description 14
- 102000018233 Fibroblast Growth Factor Human genes 0.000 description 13
- 108050007372 Fibroblast Growth Factor Proteins 0.000 description 13
- 239000003814 drug Substances 0.000 description 12
- 229940079593 drug Drugs 0.000 description 12
- 229940126864 fibroblast growth factor Drugs 0.000 description 10
- 230000029663 wound healing Effects 0.000 description 10
- 210000003491 skin Anatomy 0.000 description 8
- 102000010834 Extracellular Matrix Proteins Human genes 0.000 description 7
- 108010037362 Extracellular Matrix Proteins Proteins 0.000 description 7
- 241000700159 Rattus Species 0.000 description 7
- 210000004027 cell Anatomy 0.000 description 7
- 210000002744 extracellular matrix Anatomy 0.000 description 7
- 208000014674 injury Diseases 0.000 description 7
- 210000002540 macrophage Anatomy 0.000 description 7
- 108090000623 proteins and genes Proteins 0.000 description 7
- 238000001356 surgical procedure Methods 0.000 description 7
- 238000003786 synthesis reaction Methods 0.000 description 7
- 102000046299 Transforming Growth Factor beta1 Human genes 0.000 description 6
- 101800002279 Transforming growth factor beta-1 Proteins 0.000 description 6
- 230000006378 damage Effects 0.000 description 6
- 235000018102 proteins Nutrition 0.000 description 6
- 102000004169 proteins and genes Human genes 0.000 description 6
- 241000282412 Homo Species 0.000 description 5
- 241001465754 Metazoa Species 0.000 description 5
- 230000002378 acidificating effect Effects 0.000 description 5
- 235000018417 cysteine Nutrition 0.000 description 5
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 5
- 238000002474 experimental method Methods 0.000 description 5
- 238000010186 staining Methods 0.000 description 5
- 238000012360 testing method Methods 0.000 description 5
- 241000283690 Bos taurus Species 0.000 description 4
- 102000009123 Fibrin Human genes 0.000 description 4
- 108010073385 Fibrin Proteins 0.000 description 4
- BWGVNKXGVNDBDI-UHFFFAOYSA-N Fibrin monomer Chemical compound CNC(=O)CNC(=O)CN BWGVNKXGVNDBDI-UHFFFAOYSA-N 0.000 description 4
- 241000283973 Oryctolagus cuniculus Species 0.000 description 4
- 210000004556 brain Anatomy 0.000 description 4
- 239000002537 cosmetic Substances 0.000 description 4
- 229950003499 fibrin Drugs 0.000 description 4
- 239000000499 gel Substances 0.000 description 4
- 210000001616 monocyte Anatomy 0.000 description 4
- 239000002243 precursor Substances 0.000 description 4
- 241000894007 species Species 0.000 description 4
- VBEQCZHXXJYVRD-GACYYNSASA-N uroanthelone Chemical compound C([C@@H](C(=O)N[C@H](C(=O)N[C@@H](CS)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CS)C(=O)N[C@H](C(=O)N[C@@H]([C@@H](C)CC)C(=O)NCC(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CS)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(O)=O)C(C)C)[C@@H](C)O)NC(=O)[C@H](CO)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CO)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@@H](NC(=O)[C@H](CC=1NC=NC=1)NC(=O)[C@H](CCSC)NC(=O)[C@H](CS)NC(=O)[C@@H](NC(=O)CNC(=O)CNC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CS)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)CNC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CO)NC(=O)[C@H](CO)NC(=O)[C@H]1N(CCC1)C(=O)[C@H](CS)NC(=O)CNC(=O)[C@H]1N(CCC1)C(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CO)NC(=O)[C@@H](N)CC(N)=O)C(C)C)[C@@H](C)CC)C1=CC=C(O)C=C1 VBEQCZHXXJYVRD-GACYYNSASA-N 0.000 description 4
- 238000005406 washing Methods 0.000 description 4
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 3
- 208000032544 Cicatrix Diseases 0.000 description 3
- 102400001368 Epidermal growth factor Human genes 0.000 description 3
- 101800003838 Epidermal growth factor Proteins 0.000 description 3
- 206010016654 Fibrosis Diseases 0.000 description 3
- 238000004458 analytical method Methods 0.000 description 3
- 230000009286 beneficial effect Effects 0.000 description 3
- 230000005540 biological transmission Effects 0.000 description 3
- 238000005516 engineering process Methods 0.000 description 3
- 229940116977 epidermal growth factor Drugs 0.000 description 3
- 210000002950 fibroblast Anatomy 0.000 description 3
- 230000004761 fibrosis Effects 0.000 description 3
- MHMNJMPURVTYEJ-UHFFFAOYSA-N fluorescein-5-isothiocyanate Chemical compound O1C(=O)C2=CC(N=C=S)=CC=C2C21C1=CC=C(O)C=C1OC1=CC(O)=CC=C21 MHMNJMPURVTYEJ-UHFFFAOYSA-N 0.000 description 3
- 230000035876 healing Effects 0.000 description 3
- 238000012744 immunostaining Methods 0.000 description 3
- 238000004519 manufacturing process Methods 0.000 description 3
- 230000008520 organization Effects 0.000 description 3
- 239000000825 pharmaceutical preparation Substances 0.000 description 3
- 230000008439 repair process Effects 0.000 description 3
- 230000037387 scars Effects 0.000 description 3
- 239000006228 supernatant Substances 0.000 description 3
- 230000008685 targeting 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
- 108020000948 Antisense Oligonucleotides Proteins 0.000 description 2
- 241000283707 Capra Species 0.000 description 2
- HEDRZPFGACZZDS-UHFFFAOYSA-N Chloroform Chemical compound ClC(Cl)Cl HEDRZPFGACZZDS-UHFFFAOYSA-N 0.000 description 2
- KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 2
- 206010063560 Excessive granulation tissue Diseases 0.000 description 2
- 102000003971 Fibroblast Growth Factor 1 Human genes 0.000 description 2
- 108090000386 Fibroblast Growth Factor 1 Proteins 0.000 description 2
- 102000016359 Fibronectins Human genes 0.000 description 2
- 108010067306 Fibronectins Proteins 0.000 description 2
- ZRALSGWEFCBTJO-UHFFFAOYSA-N Guanidine Chemical compound NC(N)=N ZRALSGWEFCBTJO-UHFFFAOYSA-N 0.000 description 2
- WZUVPPKBWHMQCE-UHFFFAOYSA-N Haematoxylin Chemical compound C12=CC(O)=C(O)C=C2CC2(O)C1C1=CC=C(O)C(O)=C1OC2 WZUVPPKBWHMQCE-UHFFFAOYSA-N 0.000 description 2
- 101000599951 Homo sapiens Insulin-like growth factor I Proteins 0.000 description 2
- 102100037852 Insulin-like growth factor I Human genes 0.000 description 2
- 241000124008 Mammalia Species 0.000 description 2
- GQPLMRYTRLFLPF-UHFFFAOYSA-N Nitrous Oxide Chemical compound [O-][N+]#N GQPLMRYTRLFLPF-UHFFFAOYSA-N 0.000 description 2
- 206010072170 Skin wound Diseases 0.000 description 2
- 102000009618 Transforming Growth Factors Human genes 0.000 description 2
- 108010009583 Transforming Growth Factors Proteins 0.000 description 2
- 241000251539 Vertebrata <Metazoa> Species 0.000 description 2
- 239000002253 acid Substances 0.000 description 2
- 150000001413 amino acids Chemical group 0.000 description 2
- 230000008901 benefit Effects 0.000 description 2
- 238000012742 biochemical analysis Methods 0.000 description 2
- 210000004204 blood vessel Anatomy 0.000 description 2
- 230000004663 cell proliferation Effects 0.000 description 2
- 230000001413 cellular effect Effects 0.000 description 2
- 238000006243 chemical reaction Methods 0.000 description 2
- 239000003153 chemical reaction reagent Substances 0.000 description 2
- 210000002808 connective tissue Anatomy 0.000 description 2
- 230000008021 deposition Effects 0.000 description 2
- 238000013461 design Methods 0.000 description 2
- 238000011161 development Methods 0.000 description 2
- 229940088598 enzyme Drugs 0.000 description 2
- 238000009472 formulation Methods 0.000 description 2
- 239000012634 fragment Substances 0.000 description 2
- 238000005469 granulation Methods 0.000 description 2
- 230000003179 granulation Effects 0.000 description 2
- 210000001126 granulation tissue Anatomy 0.000 description 2
- 230000012010 growth Effects 0.000 description 2
- 230000000977 initiatory effect Effects 0.000 description 2
- 239000000463 material Substances 0.000 description 2
- 239000011159 matrix material Substances 0.000 description 2
- 238000013508 migration Methods 0.000 description 2
- 238000012986 modification Methods 0.000 description 2
- 230000004048 modification Effects 0.000 description 2
- 238000006386 neutralization reaction Methods 0.000 description 2
- 230000037311 normal skin Effects 0.000 description 2
- 238000007911 parenteral administration Methods 0.000 description 2
- 102000004196 processed proteins & peptides Human genes 0.000 description 2
- 230000001737 promoting effect Effects 0.000 description 2
- 230000002797 proteolythic effect Effects 0.000 description 2
- 230000004044 response Effects 0.000 description 2
- 230000036573 scar formation Effects 0.000 description 2
- 230000037390 scarring Effects 0.000 description 2
- 239000000021 stimulant Substances 0.000 description 2
- 239000003826 tablet Substances 0.000 description 2
- 238000011200 topical administration Methods 0.000 description 2
- 238000013519 translation Methods 0.000 description 2
- 230000037314 wound repair Effects 0.000 description 2
- KIUKXJAPPMFGSW-DNGZLQJQSA-N (2S,3S,4S,5R,6R)-6-[(2S,3R,4R,5S,6R)-3-Acetamido-2-[(2S,3S,4R,5R,6R)-6-[(2R,3R,4R,5S,6R)-3-acetamido-2,5-dihydroxy-6-(hydroxymethyl)oxan-4-yl]oxy-2-carboxy-4,5-dihydroxyoxan-3-yl]oxy-5-hydroxy-6-(hydroxymethyl)oxan-4-yl]oxy-3,4,5-trihydroxyoxane-2-carboxylic acid Chemical compound CC(=O)N[C@H]1[C@H](O)O[C@H](CO)[C@@H](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]3[C@@H]([C@@H](O)[C@H](O)[C@H](O3)C(O)=O)O)[C@H](O)[C@@H](CO)O2)NC(C)=O)[C@@H](C(O)=O)O1 KIUKXJAPPMFGSW-DNGZLQJQSA-N 0.000 description 1
- NMWKYTGJWUAZPZ-WWHBDHEGSA-N (4S)-4-[[(4R,7S,10S,16S,19S,25S,28S,31R)-31-[[(2S)-2-[[(1R,6R,9S,12S,18S,21S,24S,27S,30S,33S,36S,39S,42R,47R,53S,56S,59S,62S,65S,68S,71S,76S,79S,85S)-47-[[(2S)-2-[[(2S)-4-amino-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-amino-3-methylbutanoyl]amino]-3-methylbutanoyl]amino]-3-hydroxypropanoyl]amino]-3-(1H-imidazol-4-yl)propanoyl]amino]-3-phenylpropanoyl]amino]-4-oxobutanoyl]amino]-3-carboxypropanoyl]amino]-18-(4-aminobutyl)-27,68-bis(3-amino-3-oxopropyl)-36,71,76-tribenzyl-39-(3-carbamimidamidopropyl)-24-(2-carboxyethyl)-21,56-bis(carboxymethyl)-65,85-bis[(1R)-1-hydroxyethyl]-59-(hydroxymethyl)-62,79-bis(1H-imidazol-4-ylmethyl)-9-methyl-33-(2-methylpropyl)-8,11,17,20,23,26,29,32,35,38,41,48,54,57,60,63,66,69,72,74,77,80,83,86-tetracosaoxo-30-propan-2-yl-3,4,44,45-tetrathia-7,10,16,19,22,25,28,31,34,37,40,49,55,58,61,64,67,70,73,75,78,81,84,87-tetracosazatetracyclo[40.31.14.012,16.049,53]heptaoctacontane-6-carbonyl]amino]-3-methylbutanoyl]amino]-7-(3-carbamimidamidopropyl)-25-(hydroxymethyl)-19-[(4-hydroxyphenyl)methyl]-28-(1H-imidazol-4-ylmethyl)-10-methyl-6,9,12,15,18,21,24,27,30-nonaoxo-16-propan-2-yl-1,2-dithia-5,8,11,14,17,20,23,26,29-nonazacyclodotriacontane-4-carbonyl]amino]-5-[[(2S)-1-[[(2S)-1-[[(2S)-3-carboxy-1-[[(2S)-1-[[(2S)-1-[[(1S)-1-carboxyethyl]amino]-4-methyl-1-oxopentan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]amino]-1-oxopropan-2-yl]amino]-1-oxopropan-2-yl]amino]-3-(1H-imidazol-4-yl)-1-oxopropan-2-yl]amino]-5-oxopentanoic acid Chemical compound CC(C)C[C@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](C)NC(=O)[C@H](Cc1c[nH]cn1)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@@H]1CSSC[C@H](NC(=O)[C@@H](NC(=O)[C@@H]2CSSC[C@@H]3NC(=O)[C@H](Cc4ccccc4)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@@H](NC(=O)[C@H](Cc4c[nH]cn4)NC(=O)[C@H](CO)NC(=O)[C@H](CC(O)=O)NC(=O)[C@@H]4CCCN4C(=O)[C@H](CSSC[C@H](NC(=O)[C@@H](NC(=O)CNC(=O)[C@H](Cc4c[nH]cn4)NC(=O)[C@H](Cc4ccccc4)NC3=O)[C@@H](C)O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](Cc3ccccc3)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CCCCN)C(=O)N3CCC[C@H]3C(=O)N[C@@H](C)C(=O)N2)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](Cc2ccccc2)NC(=O)[C@H](Cc2c[nH]cn2)NC(=O)[C@H](CO)NC(=O)[C@@H](NC(=O)[C@@H](N)C(C)C)C(C)C)[C@@H](C)O)C(C)C)C(=O)N[C@@H](Cc2c[nH]cn2)C(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H](Cc2ccc(O)cc2)C(=O)N[C@@H](C(C)C)C(=O)NCC(=O)N[C@@H](C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N1)C(=O)N[C@@H](C)C(O)=O NMWKYTGJWUAZPZ-WWHBDHEGSA-N 0.000 description 1
- 208000012260 Accidental injury Diseases 0.000 description 1
- 108020005544 Antisense RNA Proteins 0.000 description 1
- 239000004475 Arginine Substances 0.000 description 1
- 239000011547 Bouin solution Substances 0.000 description 1
- 102000012422 Collagen Type I Human genes 0.000 description 1
- 108010022452 Collagen Type I Proteins 0.000 description 1
- 238000012270 DNA recombination Methods 0.000 description 1
- MYMOFIZGZYHOMD-UHFFFAOYSA-N Dioxygen Chemical compound O=O MYMOFIZGZYHOMD-UHFFFAOYSA-N 0.000 description 1
- 241000257465 Echinoidea Species 0.000 description 1
- 102000003974 Fibroblast growth factor 2 Human genes 0.000 description 1
- 108090000379 Fibroblast growth factor 2 Proteins 0.000 description 1
- 101000851176 Homo sapiens Pro-epidermal growth factor 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
- 108700012441 IGF2 Proteins 0.000 description 1
- 206010061218 Inflammation Diseases 0.000 description 1
- 102000005755 Intercellular Signaling Peptides and Proteins Human genes 0.000 description 1
- 108010070716 Intercellular Signaling Peptides and Proteins Proteins 0.000 description 1
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 1
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 1
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 1
- 241000699666 Mus <mouse, genus> Species 0.000 description 1
- 241000699670 Mus sp. Species 0.000 description 1
- CHJJGSNFBQVOTG-UHFFFAOYSA-N N-methyl-guanidine Natural products CNC(N)=N CHJJGSNFBQVOTG-UHFFFAOYSA-N 0.000 description 1
- 206010028980 Neoplasm Diseases 0.000 description 1
- 206010029164 Nephrotic syndrome Diseases 0.000 description 1
- 229910019142 PO4 Inorganic materials 0.000 description 1
- 108090000526 Papain Proteins 0.000 description 1
- 208000031481 Pathologic Constriction Diseases 0.000 description 1
- 241001494479 Pecora Species 0.000 description 1
- 102000057297 Pepsin A Human genes 0.000 description 1
- 108090000284 Pepsin A Proteins 0.000 description 1
- 239000004365 Protease Substances 0.000 description 1
- 101100058509 Rattus norvegicus Bloc1s5 gene Proteins 0.000 description 1
- 108020004511 Recombinant DNA Proteins 0.000 description 1
- VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 0.000 description 1
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 1
- 208000002847 Surgical Wound Diseases 0.000 description 1
- 102000006747 Transforming Growth Factor alpha Human genes 0.000 description 1
- 102000011117 Transforming Growth Factor beta2 Human genes 0.000 description 1
- 101800004564 Transforming growth factor alpha Proteins 0.000 description 1
- 101800000304 Transforming growth factor beta-2 Proteins 0.000 description 1
- 230000002159 abnormal effect Effects 0.000 description 1
- 238000009825 accumulation Methods 0.000 description 1
- 239000004480 active ingredient Substances 0.000 description 1
- 230000002411 adverse Effects 0.000 description 1
- 238000001042 affinity chromatography Methods 0.000 description 1
- 235000001014 amino acid Nutrition 0.000 description 1
- 239000003708 ampul Substances 0.000 description 1
- 230000033115 angiogenesis Effects 0.000 description 1
- 238000010171 animal model Methods 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
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 1
- 238000003556 assay Methods 0.000 description 1
- 210000002469 basement membrane Anatomy 0.000 description 1
- ZYXYTGQFPZEUFX-UHFFFAOYSA-N benzpyrimoxan Chemical compound O1C(OCCC1)C=1C(=NC=NC=1)OCC1=CC=C(C=C1)C(F)(F)F ZYXYTGQFPZEUFX-UHFFFAOYSA-N 0.000 description 1
- 238000002306 biochemical method Methods 0.000 description 1
- 229920002988 biodegradable polymer Polymers 0.000 description 1
- 239000004621 biodegradable polymer 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
- 238000004061 bleaching Methods 0.000 description 1
- 230000000903 blocking effect Effects 0.000 description 1
- 239000000872 buffer Substances 0.000 description 1
- 239000007975 buffered saline Substances 0.000 description 1
- 206010061592 cardiac fibrillation Diseases 0.000 description 1
- 239000000969 carrier Substances 0.000 description 1
- 230000012292 cell migration Effects 0.000 description 1
- 230000008859 change Effects 0.000 description 1
- 238000001311 chemical methods and process Methods 0.000 description 1
- 239000002975 chemoattractant Substances 0.000 description 1
- 238000004140 cleaning Methods 0.000 description 1
- 238000002316 cosmetic surgery Methods 0.000 description 1
- 230000034994 death Effects 0.000 description 1
- 230000007547 defect Effects 0.000 description 1
- 230000006735 deficit Effects 0.000 description 1
- 210000004207 dermis Anatomy 0.000 description 1
- 238000001514 detection method Methods 0.000 description 1
- 230000006866 deterioration Effects 0.000 description 1
- 239000003085 diluting agent Substances 0.000 description 1
- SWSQBOPZIKWTGO-UHFFFAOYSA-N dimethylaminoamidine Natural products CN(C)C(N)=N SWSQBOPZIKWTGO-UHFFFAOYSA-N 0.000 description 1
- 238000002224 dissection Methods 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
- 239000002552 dosage form Substances 0.000 description 1
- 235000013399 edible fruits Nutrition 0.000 description 1
- 230000002500 effect on skin Effects 0.000 description 1
- 238000005538 encapsulation Methods 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- 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 1
- 210000000981 epithelium Anatomy 0.000 description 1
- 239000004744 fabric Substances 0.000 description 1
- 230000001605 fetal effect Effects 0.000 description 1
- 210000003754 fetus Anatomy 0.000 description 1
- 239000000835 fiber Substances 0.000 description 1
- 230000002600 fibrillogenic effect Effects 0.000 description 1
- 230000009760 functional impairment Effects 0.000 description 1
- 230000014509 gene expression Effects 0.000 description 1
- 238000010353 genetic engineering Methods 0.000 description 1
- 230000037313 granulation tissue formation Effects 0.000 description 1
- 208000037824 growth disorder Diseases 0.000 description 1
- 210000004209 hair Anatomy 0.000 description 1
- 210000003780 hair follicle Anatomy 0.000 description 1
- 238000010562 histological examination Methods 0.000 description 1
- 229920002674 hyaluronan Polymers 0.000 description 1
- 229960003160 hyaluronic acid Drugs 0.000 description 1
- 229960002591 hydroxyproline Drugs 0.000 description 1
- 230000028993 immune response Effects 0.000 description 1
- 238000003018 immunoassay Methods 0.000 description 1
- 238000012760 immunocytochemical staining Methods 0.000 description 1
- 238000010166 immunofluorescence Methods 0.000 description 1
- 230000002163 immunogen Effects 0.000 description 1
- 238000002991 immunohistochemical analysis Methods 0.000 description 1
- 230000000415 inactivating effect Effects 0.000 description 1
- 238000011534 incubation Methods 0.000 description 1
- 230000006698 induction Effects 0.000 description 1
- 208000015181 infectious disease Diseases 0.000 description 1
- 230000008595 infiltration Effects 0.000 description 1
- 238000001764 infiltration Methods 0.000 description 1
- 230000004054 inflammatory process Effects 0.000 description 1
- 230000035992 intercellular communication Effects 0.000 description 1
- 150000002500 ions Chemical class 0.000 description 1
- 210000003734 kidney Anatomy 0.000 description 1
- 238000009533 lab test Methods 0.000 description 1
- 238000002372 labelling Methods 0.000 description 1
- 230000011268 leukocyte chemotaxis Effects 0.000 description 1
- 239000003446 ligand Substances 0.000 description 1
- 210000005228 liver tissue Anatomy 0.000 description 1
- 230000033001 locomotion Effects 0.000 description 1
- 230000005923 long-lasting effect Effects 0.000 description 1
- 238000005259 measurement Methods 0.000 description 1
- 230000008384 membrane barrier Effects 0.000 description 1
- 230000005012 migration Effects 0.000 description 1
- 208000009928 nephrosis Diseases 0.000 description 1
- 231100001027 nephrosis Toxicity 0.000 description 1
- GVUGOAYIVIDWIO-UFWWTJHBSA-N nepidermin Chemical compound C([C@@H](C(=O)N[C@@H]([C@@H](C)CC)C(=O)NCC(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CS)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(O)=O)NC(=O)CNC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@H](CS)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CS)NC(=O)[C@H](C)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](C)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@@H](NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CCSC)NC(=O)[C@H](CS)NC(=O)[C@@H](NC(=O)CNC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC=1NC=NC=1)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CS)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)CNC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC=1NC=NC=1)NC(=O)[C@H](CO)NC(=O)[C@H](CC(C)C)NC(=O)[C@H]1N(CCC1)C(=O)[C@H](CS)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](CO)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CO)NC(=O)[C@@H](N)CC(N)=O)C(C)C)[C@@H](C)CC)C(C)C)C(C)C)C1=CC=C(O)C=C1 GVUGOAYIVIDWIO-UFWWTJHBSA-N 0.000 description 1
- 239000001272 nitrous oxide Substances 0.000 description 1
- 239000002674 ointment Substances 0.000 description 1
- 239000001301 oxygen Substances 0.000 description 1
- 229910052760 oxygen Inorganic materials 0.000 description 1
- 238000012856 packing Methods 0.000 description 1
- 206010033675 panniculitis Diseases 0.000 description 1
- 229940055729 papain Drugs 0.000 description 1
- 235000019834 papain Nutrition 0.000 description 1
- 239000008188 pellet Substances 0.000 description 1
- 229940111202 pepsin Drugs 0.000 description 1
- 230000010412 perfusion Effects 0.000 description 1
- 239000008177 pharmaceutical agent Substances 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
- 239000008363 phosphate buffer Substances 0.000 description 1
- 229920001184 polypeptide Polymers 0.000 description 1
- 239000013641 positive control Substances 0.000 description 1
- 239000002994 raw material Substances 0.000 description 1
- 239000012925 reference material Substances 0.000 description 1
- 230000001105 regulatory effect Effects 0.000 description 1
- 238000009877 rendering Methods 0.000 description 1
- 238000012552 review Methods 0.000 description 1
- 210000003079 salivary gland Anatomy 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 239000001632 sodium acetate Substances 0.000 description 1
- 235000017281 sodium acetate Nutrition 0.000 description 1
- 239000011780 sodium chloride Substances 0.000 description 1
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 1
- 208000035736 spondylodysplastic type Ehlers-Danlos syndrome Diseases 0.000 description 1
- 230000036262 stenosis Effects 0.000 description 1
- 208000037804 stenosis Diseases 0.000 description 1
- 230000004936 stimulating effect Effects 0.000 description 1
- 230000036435 stunted growth Effects 0.000 description 1
- 238000010254 subcutaneous injection Methods 0.000 description 1
- 239000007929 subcutaneous injection Substances 0.000 description 1
- 210000004304 subcutaneous tissue Anatomy 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 239000004753 textile Substances 0.000 description 1
- 229940124597 therapeutic agent Drugs 0.000 description 1
- 230000001225 therapeutic effect Effects 0.000 description 1
- 230000000287 tissue oxygenation Effects 0.000 description 1
- 230000007838 tissue remodeling Effects 0.000 description 1
- 239000012859 tissue stain Substances 0.000 description 1
- FGMPLJWBKKVCDB-UHFFFAOYSA-N trans-L-hydroxy-proline Natural products ON1CCCC1C(O)=O FGMPLJWBKKVCDB-UHFFFAOYSA-N 0.000 description 1
- 229940099456 transforming growth factor beta 1 Drugs 0.000 description 1
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
- 238000005303 weighing Methods 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
- C07K14/705—Receptors; Cell surface antigens; Cell surface determinants
- C07K14/71—Receptors; Cell surface antigens; Cell surface determinants for growth factors; for growth regulators
-
- 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
-
- 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
- A61P43/00—Drugs for specific purposes, not provided for in groups A61P1/00-A61P41/00
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
- C07K16/22—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against growth factors ; against growth regulators
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- Medicinal Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Biochemistry (AREA)
- Immunology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Molecular Biology (AREA)
- Genetics & Genomics (AREA)
- Biophysics (AREA)
- Public Health (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Veterinary Medicine (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Engineering & Computer Science (AREA)
- Animal Behavior & Ethology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Pharmacology & Pharmacy (AREA)
- General Chemical & Material Sciences (AREA)
- Toxicology (AREA)
- Cell Biology (AREA)
- Dermatology (AREA)
- Zoology (AREA)
- Gastroenterology & Hepatology (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Acyclic And Carbocyclic Compounds In Medicinal Compositions (AREA)
- Materials For Medical Uses (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Pharmaceuticals Containing Other Organic And Inorganic Compounds (AREA)
- Medicinal Preparation (AREA)
- Transceivers (AREA)
- Mobile Radio Communication Systems (AREA)
Abstract
Description
Claims (27)
- 1.創傷の治療で用いて治療中の瘢痕組織形成を抑制する組成物であって、線維 性成長因子にのみ特効のある有効活性度抑制量の1種類または複数種類の成長因 子中和剤を、製薬上許容なキャリヤと共に包含することを特徴とする組成物。
- 2.請求の範囲第1項記載の組成物において、成長因子中和剤が成長因子中和抗 体であることを特徴とする組成物。
- 3.請求の範囲第2項記載の組成物において、成長因子中和抗体が、抗TGFβ −1抗体、抗TGFβ−2抗体および抗PDGF抗体から選んだものであること を特徴とする組成物。
- 4.請求の範囲第1項記載の組成物において、成長因子中和剤が成長因子レセプ タ阻害剤であることを特徴とする組成物。
- 5.請求の範囲第4項記載の組成物において、成長因子レセプタ阻害剤が成長因 子のレセプタ結合部位を含むペプチドであることを特徴とする組成物。
- 6.請求の範囲第5項記載の組成物において、ペプチドがTGFβ−1またはT GFβ−2またはPDGFのためのレセプタ結合部位を含むことを特徴とする組 成物。
- 7.請求の範囲第1項記載の組成物において、成長因子中和剤がレセプタ結合を 抑制するように成長因子に結合する分子であることを特徴とする組成物。
- 8.請求の範囲第7項記載の組成物におし、て、成長因子がTGFβ−1および TGFβ−2から選ばれ、分子がDecorinおよびBiglycanから選 ばれることを特徴とする組成物。
- 9.請求の範囲第1項記載の組成物において、成長因子中和剤が成長因子mRN Aに対するアンチセンス・オリゴヌクレオチドであることを特徴とする組成物。
- 10.請求の範囲第1項記載の組成物において、成長因子中和剤が成長因子mR NAに対して活性のあるribosyme(s)であることを特徴とする組成物 。
- 11.請求の範囲第1項記載の組成物において、成長因子中和剤がレセプタの可 溶性形態あるいはレセプタの成長因子結合ドメインであることを特徴とする組成 物。
- 12.請求の範囲第1項から第11項までのいずれか1つの項に記載の組成物に おいて、成長因子中和剤が活性形態で存在することを特徴とする組成物。
- 13.請求の範囲第1項から第11項までに記載の組成物において、成長因子中 和剤が不活性形態で存在することを特徴とする組成物。
- 14.請求の範囲第13項記載の組成物において、成長因子中和剤がカプセル封 入によって不活性化されることを特徴とする組成物。
- 15.請求の範囲第14項記載の組成物においてカプセルが、必要なときに、外 部刺激によって分解し、活性成長因子中和剤を放出することを特徴とする組成物 。
- 16.請求の範囲第15項記載の組成物において、外部刺激が紫外線光、生体内 酵素、超音波、熱を含むことを特徴とする組成物。
- 17.請求の範囲第13項記載の組成物において、成長因子中和剤が結合分子の 分子添加によって不活性化されることを特徴とする組成物。
- 18.請求の範囲第17項記載の組成物において、結合分子が、紫外線光、生体 内酵素、超音波、熱を含む外部刺激によって活性成長因子中和剤から剥離され、 それを放出させることを特徴とする組成物。
- 19.請求の範囲第1項から第18項までのいずれか1つの項に記載の組成物に おいて、製薬上許容なキャリヤが、局所適用のために中性滅菌クリーム、ゲル、 エアロゾルまたは粉末からなることを特徴とする組成物。
- 20.請求の範囲第1項から第18項までに記載の組成物において、製薬上許容 なキャリヤが注射、灌流または吸入のための滅菌溶液からなることを特徴とする 組成物。
- 21.請求の範囲第1項から第18項までに記載の組成物において、製薬上許容 なキャリヤが創傷を局所的に覆うための滅菌ドレッシングからなることを特徴と する組成物。
- 22.請求の範囲第21項記載の組成物において、ドレッシングが生体分解性/ 吸収性高分子からなることを特徴とする組成物。
- 23.請求の範囲第1項から第18項までに記載の組成物において、製薬上許容 なキャリヤが創傷内に移植するための生体高分子/高分子からなることを特徴と する組成物。
- 24.請求の範囲第1項から第18項までのいずれか1つの項に記載の組成物に おいて、活性サイトカインからなることを特徴とする組成物。
- 25.線維性成長因子にのみ特効のある1種類または複数種類の成長因子中和剤 を包含する製薬組成物の調製方法であって、この組成物を局所的にクリーム、ゲ ル、エアロゾル、粉末、ドレッシング、パッチの形で、あるいは、注射、灌流、 吸入のための溶液の形で、あるいは、制御放出移植体として適用することを特徴 とする調製方法。
- 26.請求の範囲第25項記載の調製方法において、組成物が活性サイトカイン からなることを特徴とする方法。
- 27.創傷治療中に瘢痕組織の形成を抑制する方法であって、組織創傷を受けた ホストヘ、創傷領域における線維性成長因子にのみ特効のある1種類または榎数 種類の成長因子中和剤を、治療中に瘢痕組織を形成することに通じる、この治療 過程に伴う1つまたはそれ以上の成長因子の活性度を低下させるに有効な投与量 で投与することからなることを特徴とする方法。
Applications Claiming Priority (3)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
GB9106678.7 | 1991-03-28 | ||
GB919106678A GB9106678D0 (en) | 1991-03-28 | 1991-03-28 | Wound healing |
PCT/GB1992/000570 WO1992017206A1 (en) | 1991-03-28 | 1992-03-30 | Wound healing |
Related Child Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
JP2002029691A Division JP2002275094A (ja) | 1991-03-28 | 2002-02-06 | 成長因子中和剤含有医薬組成物 |
Publications (2)
Publication Number | Publication Date |
---|---|
JPH06506205A true JPH06506205A (ja) | 1994-07-14 |
JP3333507B2 JP3333507B2 (ja) | 2002-10-15 |
Family
ID=10692386
Family Applications (3)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
JP50694492A Expired - Fee Related JP3333507B2 (ja) | 1991-03-28 | 1992-03-30 | 創傷治療 |
JP2002029691A Pending JP2002275094A (ja) | 1991-03-28 | 2002-02-06 | 成長因子中和剤含有医薬組成物 |
JP2005267284A Pending JP2006001949A (ja) | 1991-03-28 | 2005-09-14 | 成長因子中和剤含有医薬組成物 |
Family Applications After (2)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
JP2002029691A Pending JP2002275094A (ja) | 1991-03-28 | 2002-02-06 | 成長因子中和剤含有医薬組成物 |
JP2005267284A Pending JP2006001949A (ja) | 1991-03-28 | 2005-09-14 | 成長因子中和剤含有医薬組成物 |
Country Status (13)
Country | Link |
---|---|
US (4) | US5662904A (ja) |
EP (1) | EP0585242B2 (ja) |
JP (3) | JP3333507B2 (ja) |
AT (1) | ATE182792T1 (ja) |
AU (1) | AU661840B2 (ja) |
CA (2) | CA2105652C (ja) |
DE (1) | DE69229729T3 (ja) |
DK (1) | DK0585242T4 (ja) |
ES (1) | ES2136618T5 (ja) |
GB (1) | GB9106678D0 (ja) |
GR (1) | GR3030924T3 (ja) |
IE (1) | IE921013A1 (ja) |
WO (1) | WO1992017206A1 (ja) |
Families Citing this family (69)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US5654270A (en) | 1988-06-28 | 1997-08-05 | La Jolla Cancer Research Foundation | Use of fibromodulin to prevent or reduce dermal scarring |
US5571714A (en) * | 1988-12-22 | 1996-11-05 | Celtrix Pharmaceuticals, Inc. | Monoclonal antibodies which bind both transforming growth factors β1 and β2 and methods of use |
US5177197A (en) * | 1990-02-27 | 1993-01-05 | Ludwig Institute For Cancer Research | Isolated nucleotide sequence expressing human transforming growth factor-β1-binding protein |
US6117425A (en) | 1990-11-27 | 2000-09-12 | The American National Red Cross | Supplemented and unsupplemented tissue sealants, method of their production and use |
US6197325B1 (en) | 1990-11-27 | 2001-03-06 | The American National Red Cross | Supplemented and unsupplemented tissue sealants, methods of their production and use |
US7196054B1 (en) * | 1990-11-27 | 2007-03-27 | The American National Red Cross | Methods for treating wound tissue and forming a supplemented fibrin matrix |
US6054122A (en) | 1990-11-27 | 2000-04-25 | The American National Red Cross | Supplemented and unsupplemented tissue sealants, methods of their production and use |
GB9106678D0 (en) * | 1991-03-28 | 1991-05-15 | Ferguson Mark W J | Wound healing |
ES2188585T3 (es) * | 1991-11-14 | 2003-07-01 | Jolla Cancer Res Found | Inhibidores de factores reguladores celulares y procedimientos para evitar o reducir la formacion de cicatrices. |
WO1993014782A1 (en) * | 1992-01-29 | 1993-08-05 | La Jolla Cancer Research Foundation | Methods of controlling the proliferation of macrophages |
GB9205800D0 (en) * | 1992-03-17 | 1992-04-29 | British Tech Group | Treatment of fibrotic disorders |
GB9206861D0 (en) * | 1992-03-28 | 1992-05-13 | Univ Manchester | Wound healing and treatment of fibrotic disorders |
EP1251170A3 (en) * | 1992-07-17 | 2002-10-30 | Ribozyme Pharmaceuticals, Inc. | Method and reagent for treatment of NF-kappaB dependent animal diseases |
CA2146973C (en) * | 1992-10-29 | 2008-09-02 | Patricia R. Segarini | Uses of tgf-.beta. receptor fragment as a therapeutic agent |
AU7053894A (en) * | 1993-06-09 | 1995-01-03 | Ribozyme Pharmaceuticals, Inc. | Enzymatic rna molecules and their application in the treatment of fibrosis and fibrous tissue disease |
AU6984594A (en) * | 1993-06-15 | 1995-01-17 | Hun Taeg Chung | Anti-sense oligodeoxynucleotide to fibrogenic cytokines and use thereof |
DE69434617D1 (de) * | 1993-11-19 | 2006-04-06 | Univ Sydney | Verfahren zur prophylaxe oder kontrolle des katarakts |
AU5698094A (en) * | 1993-12-09 | 1995-06-27 | Biognostik Gesellschaft Fur Biomolekulare Diagnostik Mbh | Antisense nucleic acid for the treatment of diseases in which expression of bfgf, pdgf-a or pdgf-b plays a pathogenic role |
US5834440A (en) * | 1994-03-07 | 1998-11-10 | Immusol Incorporated | Ribozyme therapy for the inhibition of restenosis |
CA2184989A1 (en) * | 1994-03-07 | 1995-09-14 | Tsvi Goldenberg | Ribozyme therapy for restenosis |
GB9405046D0 (en) * | 1994-03-15 | 1994-04-27 | Unilever Plc | Skin treatment composition |
JP4083794B2 (ja) * | 1994-03-29 | 2008-04-30 | レノボ・リミテッド | 創傷の治癒 |
GB2288118A (en) * | 1994-03-29 | 1995-10-11 | Univ Manchester | Wound healing composition |
US5824655A (en) * | 1995-02-15 | 1998-10-20 | The University Of Utah | Anti-transforming growth factor-β gene therapy |
GB2304045A (en) * | 1995-08-04 | 1997-03-12 | Univ Manchester | Betaglycan compositions for promoting the healing of wounds and fibrotic diseases |
GB2304047A (en) * | 1995-08-09 | 1997-03-12 | Univ Manchester | Pharmaceutical compositions containing cytokines |
GB9601081D0 (en) * | 1995-10-06 | 1996-03-20 | Cambridge Antibody Tech | Specific binding members for human transforming growth factor beta;materials and methods |
US7368111B2 (en) | 1995-10-06 | 2008-05-06 | Cambridge Antibody Technology Limited | Human antibodies specific for TGFβ2 |
GB2306481A (en) * | 1995-10-21 | 1997-05-07 | Univ Manchester | Pharmaceutical comprising a stimulator of activin and/or inhibin |
GB9702943D0 (en) * | 1997-02-13 | 1997-04-02 | Univ Manchester | Wound healing |
ATE270113T1 (de) * | 1997-08-27 | 2004-07-15 | Harvard College | Zusammenstellungen zur verbesserten wundheilung |
US6444657B1 (en) | 1998-12-31 | 2002-09-03 | Guilford Pharmaceuticals Inc. | Methods for treating certain diseases using naaladase inhibitors |
AU3615700A (en) * | 1999-03-04 | 2000-09-21 | United States Surgical Corporation | Scar reduction |
US6492497B1 (en) * | 1999-04-30 | 2002-12-10 | Cambridge Antibody Technology Limited | Specific binding members for TGFbeta1 |
US6630142B2 (en) | 1999-05-03 | 2003-10-07 | Zymogenetics, Inc. | Method of treating fibroproliferative disorders |
US7261881B1 (en) | 1999-05-20 | 2007-08-28 | Yale University | Modulation of angiogenesis and wound healing |
US7078390B1 (en) | 1999-10-15 | 2006-07-18 | Gentier Biosystems Incorporation | Ribozymes to growth factor originating in human platelet |
US6893637B1 (en) | 1999-10-21 | 2005-05-17 | Zymogenetics, Inc. | Method of treating fibrosis |
US20040197333A1 (en) * | 2000-02-10 | 2004-10-07 | Cornell Research Foundation, Inc. | Use of TGF-beta antagonists to inhibit tumor cell formation or progression |
US7255883B2 (en) * | 2000-06-23 | 2007-08-14 | Healagenics, Inc. | Agent for reduction of scar formation by using wound alkalinization |
US6509318B1 (en) * | 2000-09-29 | 2003-01-21 | The Regents Of The University Of California | TGF-B inhibitors and methods |
AU2002227052A1 (en) * | 2000-11-30 | 2002-06-11 | University Of Florida | Treatments for neurogenetic disorders, impulse control disorders, and wound healing |
US20040235791A1 (en) * | 2002-01-25 | 2004-11-25 | Gruskin Elliott A. | Scar reduction |
GB0217136D0 (en) | 2002-07-24 | 2002-09-04 | Renovo Ltd | Wound healing & treatment of fibrosis |
GB0309064D0 (en) | 2003-04-22 | 2003-05-28 | Univ Manchester | Modified peptides and their uses |
NZ592039A (en) | 2003-08-27 | 2013-03-28 | Ophthotech Corp | Combination therapy for the treatment of ocular neovascular disorders |
JP2007513650A (ja) * | 2003-11-20 | 2007-05-31 | アンジオテック インターナショナル アーゲー | 移植可能なセンサーおよび移植可能なポンプならびに瘢痕化抑制剤 |
US7527791B2 (en) | 2004-03-31 | 2009-05-05 | Genentech, Inc. | Humanized anti-TGF-beta antibodies |
DE102004025881A1 (de) * | 2004-05-19 | 2006-01-05 | Beiersdorf Ag | Oligoribonukleotide zur Beeinflussung des Haarwachstums |
WO2006029046A2 (en) * | 2004-09-03 | 2006-03-16 | Yale University | Use of leptin in wound healing |
US8109981B2 (en) | 2005-01-25 | 2012-02-07 | Valam Corporation | Optical therapies and devices |
JP5153639B2 (ja) * | 2005-10-25 | 2013-02-27 | ウィミンズ アンド チルドレンズ ヘルス リサーチ インスティテュート | 創傷修復を調節するための方法及び組成物 |
US8353881B2 (en) * | 2005-12-28 | 2013-01-15 | Abbott Diabetes Care Inc. | Infusion sets for the delivery of a therapeutic substance to a patient |
US7981034B2 (en) | 2006-02-28 | 2011-07-19 | Abbott Diabetes Care Inc. | Smart messages and alerts for an infusion delivery and management system |
US9119582B2 (en) | 2006-06-30 | 2015-09-01 | Abbott Diabetes Care, Inc. | Integrated analyte sensor and infusion device and methods therefor |
US8932216B2 (en) | 2006-08-07 | 2015-01-13 | Abbott Diabetes Care Inc. | Method and system for providing data management in integrated analyte monitoring and infusion system |
US8206296B2 (en) | 2006-08-07 | 2012-06-26 | Abbott Diabetes Care Inc. | Method and system for providing integrated analyte monitoring and infusion system therapy management |
US8641618B2 (en) | 2007-06-27 | 2014-02-04 | Abbott Diabetes Care Inc. | Method and structure for securing a monitoring device element |
US8085151B2 (en) | 2007-06-28 | 2011-12-27 | Abbott Diabetes Care Inc. | Signal converting cradle for medical condition monitoring and management system |
KR20110074611A (ko) * | 2008-10-21 | 2011-06-30 | 노보더믹스 인터내셔널 리미티드 | 상피 조직의 치료 조성물 |
JP2012518657A (ja) | 2009-02-25 | 2012-08-16 | オーエスアイ・ファーマシューティカルズ,エルエルシー | 併用抗癌治療 |
JP2012519281A (ja) | 2009-02-27 | 2012-08-23 | オーエスアイ・ファーマシューティカルズ,エルエルシー | 間葉様腫瘍細胞またはその生成を阻害する薬剤を同定するための方法 |
WO2010099138A2 (en) | 2009-02-27 | 2010-09-02 | Osi Pharmaceuticals, Inc. | Methods for the identification of agents that inhibit mesenchymal-like tumor cells or their formation |
JP2012519282A (ja) | 2009-02-27 | 2012-08-23 | オーエスアイ・ファーマシューティカルズ,エルエルシー | 間葉様腫瘍細胞またはその生成を阻害する薬剤を同定するための方法 |
WO2012149014A1 (en) | 2011-04-25 | 2012-11-01 | OSI Pharmaceuticals, LLC | Use of emt gene signatures in cancer drug discovery, diagnostics, and treatment |
WO2013152252A1 (en) | 2012-04-06 | 2013-10-10 | OSI Pharmaceuticals, LLC | Combination anti-cancer therapy |
WO2015027082A1 (en) | 2013-08-22 | 2015-02-26 | Acceleron Pharma, Inc. | Tgf-beta receptor type ii variants and uses thereof |
CN108348578B (zh) | 2015-08-04 | 2022-08-09 | 阿塞勒隆制药公司 | 用于治疗骨髓增生性病症的方法 |
ES2948647T3 (es) | 2017-05-04 | 2023-09-15 | Acceleron Pharma Inc | Proteínas de fusión del receptor TGF-beta tipo II y usos de las mismas |
Family Cites Families (38)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US5145676A (en) * | 1981-09-08 | 1992-09-08 | The Rockefeller University | Method and agents for promoting wound healing |
US5104977A (en) * | 1982-09-24 | 1992-04-14 | The United States Of America As Represented By The Department Of Health And Human Services | Purified transforming growth factor beta |
EP0105014B1 (en) * | 1982-09-24 | 1992-05-20 | THE UNITED STATES OF AMERICA as represented by the Secretary United States Department of Commerce | Repair of tissue in animals |
AU3108984A (en) * | 1983-06-03 | 1985-01-04 | United States of America, as represented by the Secretary, U.S. Department of Commerce, The | Purified transforming growth factor-beta derived from human platelets and placentas |
DE3629640A1 (de) * | 1986-08-30 | 1988-03-03 | Behringwerke Ag | Verwendung monoklonaler antikoerper zur therapie von tumoren |
US4708948A (en) * | 1984-04-20 | 1987-11-24 | The United States Of America As Represented By The Department Of Health And Human Services | Substantially purified tumor growth inhibitory factor |
DE3588058T3 (de) * | 1984-07-16 | 2005-04-07 | Celtrix Pharmaceuticals, Inc., Palo Alto | Knorpel-induzierende Polypeptid-Faktoren aus Knochen |
US4886747A (en) * | 1985-03-22 | 1989-12-12 | Genentech, Inc. | Nucleic acid encoding TGF-β and its uses |
IL78197A (en) * | 1985-03-22 | 1991-07-18 | Genentech Inc | Nucleic acid encoding tgf-beta and its uses |
US5168051A (en) * | 1985-03-22 | 1992-12-01 | Genentech, Inc. | Nucleic acid encoding TGF-β its uses |
US5262319A (en) * | 1985-04-19 | 1993-11-16 | Oncogene Science, Inc. | Method for obtaining bone marrow free of tumor cells using transforming growth factor β3 |
IE60059B1 (en) * | 1985-04-19 | 1994-05-18 | Oncogene Science Inc | Tissue-derived tumor growth inhibitors, methods of preparation and uses thereof |
WO1989012101A1 (en) * | 1988-06-08 | 1989-12-14 | Genentech, Inc. | NUCLEIC ACID ENCODING TGF-beta3 AND ITS USE |
US4837381A (en) * | 1986-08-11 | 1989-06-06 | American Cyanamid Company | Compositions for parenteral administration and their use |
US4931548A (en) * | 1987-01-30 | 1990-06-05 | Techne Corporation | Heterodimer form of transforming growth factor-beta |
AU624789B2 (en) * | 1987-02-19 | 1992-06-25 | Amgen, Inc. | Purified platelet-derived growth factor and methods for purification thereof |
US5055447A (en) * | 1988-07-28 | 1991-10-08 | Genentech, Inc. | Method and compositions for the treatment and prevention of septic shock |
GB8823649D0 (en) * | 1988-10-07 | 1988-11-16 | Geistlich Soehne Ag | Chemical compounds |
US5135915A (en) * | 1988-10-14 | 1992-08-04 | Genentech, Inc. | Method for the treatment of grafts prior to transplantation using TGF-.beta. |
IE61346B1 (en) * | 1988-11-02 | 1994-11-02 | Genentech Inc | A permeable material to fit around the teeth or gums of a mammal |
CA2005120A1 (en) * | 1988-12-15 | 1990-06-15 | Anthony F. Purchio | Tgf-beta 1/beta 2: a novel chimeric transforming growth factor-beta |
US5061786A (en) * | 1989-05-25 | 1991-10-29 | Genentech, Inc. | Biologically active polypeptides based on transforming growth factor-β |
US5118791A (en) * | 1989-05-25 | 1992-06-02 | Genentech, Inc. | Biologically active polypeptides based on transforming growth factor-β |
EP0494264B1 (en) * | 1989-09-29 | 1997-06-18 | La Jolla Cancer Research Foundation | Inhibiting transforming growth factor to prevent accumulation of extracellular matrix |
GB8927546D0 (en) * | 1989-12-06 | 1990-02-07 | Ciba Geigy | Process for the production of biologically active tgf-beta |
WO1991010727A1 (en) * | 1990-01-22 | 1991-07-25 | La Jolla Cancer Research Foundation | Inhibitors of cell regulatory factors |
US5147854A (en) * | 1990-05-22 | 1992-09-15 | Hoffmann-La Roche Inc. | Tgf-b compositions and method |
CA2084992A1 (en) * | 1990-06-25 | 1991-12-26 | Osi Pharmaceuticals, Inc. | Tissue-derived tumor growth inhibitors, methods for preparation and uses thereof |
US5149801A (en) * | 1990-11-21 | 1992-09-22 | The Regents Of The University Of California | Boronated porphyrin compounds |
GB9101645D0 (en) * | 1991-01-25 | 1991-03-06 | British Bio Technology | Compounds |
AU1426792A (en) * | 1991-02-04 | 1992-09-07 | Oncogene Science, Inc. | Inhibition of multidrug transport by transforming growth factor beta and uses thereof |
GB9106678D0 (en) * | 1991-03-28 | 1991-05-15 | Ferguson Mark W J | Wound healing |
CA2071137A1 (en) * | 1991-07-10 | 1993-01-11 | Clarence C. Lee | Composition and method for revitalizing scar tissue |
AU2738392A (en) * | 1991-11-11 | 1993-05-13 | Ciba-Geigy Ag | Novel hybrid transforming growth factors |
GB9205800D0 (en) * | 1992-03-17 | 1992-04-29 | British Tech Group | Treatment of fibrotic disorders |
GB9206861D0 (en) * | 1992-03-28 | 1992-05-13 | Univ Manchester | Wound healing and treatment of fibrotic disorders |
AU6984594A (en) * | 1993-06-15 | 1995-01-17 | Hun Taeg Chung | Anti-sense oligodeoxynucleotide to fibrogenic cytokines and use thereof |
JP4083794B2 (ja) * | 1994-03-29 | 2008-04-30 | レノボ・リミテッド | 創傷の治癒 |
-
1991
- 1991-03-28 GB GB919106678A patent/GB9106678D0/en active Pending
-
1992
- 1992-03-30 AU AU14368/92A patent/AU661840B2/en not_active Ceased
- 1992-03-30 US US08/122,508 patent/US5662904A/en not_active Expired - Lifetime
- 1992-03-30 WO PCT/GB1992/000570 patent/WO1992017206A1/en active IP Right Grant
- 1992-03-30 ES ES92907214T patent/ES2136618T5/es not_active Expired - Lifetime
- 1992-03-30 EP EP92907214A patent/EP0585242B2/en not_active Expired - Lifetime
- 1992-03-30 CA CA002105652A patent/CA2105652C/en not_active Expired - Lifetime
- 1992-03-30 JP JP50694492A patent/JP3333507B2/ja not_active Expired - Fee Related
- 1992-03-30 AT AT92907214T patent/ATE182792T1/de not_active IP Right Cessation
- 1992-03-30 DK DK92907214T patent/DK0585242T4/da active
- 1992-03-30 IE IE101392A patent/IE921013A1/en not_active IP Right Cessation
- 1992-03-30 CA CA002387247A patent/CA2387247C/en not_active Expired - Lifetime
- 1992-03-30 DE DE69229729T patent/DE69229729T3/de not_active Expired - Lifetime
-
1999
- 1999-08-05 GR GR990401862T patent/GR3030924T3/el unknown
-
2002
- 2002-02-06 JP JP2002029691A patent/JP2002275094A/ja active Pending
- 2002-04-08 US US10/117,351 patent/US20020187149A1/en not_active Abandoned
-
2005
- 2005-06-16 US US11/153,897 patent/US20050287139A1/en not_active Abandoned
- 2005-09-14 JP JP2005267284A patent/JP2006001949A/ja active Pending
-
2009
- 2009-06-08 US US12/457,346 patent/US20100152095A1/en not_active Abandoned
Also Published As
Publication number | Publication date |
---|---|
EP0585242B2 (en) | 2007-03-07 |
IE921013A1 (en) | 1992-10-07 |
CA2105652A1 (en) | 1992-09-29 |
US5662904A (en) | 1997-09-02 |
CA2387247C (en) | 2009-05-19 |
AU661840B2 (en) | 1995-08-10 |
JP2006001949A (ja) | 2006-01-05 |
US20050287139A1 (en) | 2005-12-29 |
CA2387247A1 (en) | 1992-10-15 |
GR3030924T3 (en) | 1999-11-30 |
US20020187149A1 (en) | 2002-12-12 |
DK0585242T4 (da) | 2007-07-02 |
DK0585242T3 (da) | 1999-12-06 |
EP0585242A1 (en) | 1994-03-09 |
EP0585242B1 (en) | 1999-08-04 |
ES2136618T5 (es) | 2007-10-16 |
JP3333507B2 (ja) | 2002-10-15 |
US20100152095A1 (en) | 2010-06-17 |
ATE182792T1 (de) | 1999-08-15 |
DE69229729T2 (de) | 2000-01-13 |
ES2136618T3 (es) | 1999-12-01 |
CA2105652C (en) | 2005-09-06 |
WO1992017206A1 (en) | 1992-10-15 |
AU1436892A (en) | 1992-11-02 |
DE69229729D1 (de) | 1999-09-09 |
JP2002275094A (ja) | 2002-09-25 |
DE69229729T3 (de) | 2007-10-18 |
GB9106678D0 (en) | 1991-05-15 |
Similar Documents
Publication | Publication Date | Title |
---|---|---|
JPH06506205A (ja) | 創傷治療 | |
JP6247692B2 (ja) | 皮膚瘢痕を治療する組成物及び方法 | |
EP0527787B1 (en) | Method of predisposing mammals to accelerated tissue repair | |
US5788967A (en) | Composition and method for enhancing wound healing | |
JP4083794B2 (ja) | 創傷の治癒 | |
HUT68905A (en) | Pharmaceutical compositions for wound healing and treatment of fibrotic disorders and process for production of them | |
EP3185888B1 (en) | Extracellular matrix compositions | |
JPH07504650A (ja) | 細胞外マトリックスの蓄積を防止するためのトランスフォーミング増殖因子βの阻害 | |
Jones et al. | Effect of topical recombinant TGF-β on healing of partial thickness injuries | |
EP0855916B1 (en) | Pharmaceutical composition containing an activin stimulator | |
CN110903348A (zh) | 一种促进伤口愈合的小肽及其应用 | |
US8357655B2 (en) | Wound healing peptides and methods of use thereof | |
JPH07316066A (ja) | 創傷治癒剤 | |
Ksander et al. | Exogenous transforming growth factor‐β2 enhances connective tissue formation in transforming growth factor‐β1—deficient, healing‐impaired dermal wounds in mice | |
CN115721638B (zh) | 月桂酰精氨酸乙酯盐酸盐在制备促伤口愈合药物中的应用 | |
JPH03502922A (ja) | インターロイキン‐1蛋白質を含む局所創傷治療用製剤 | |
JPH08502496A (ja) | 傷の治癒促進方法およびそのための組成物 |
Legal Events
Date | Code | Title | Description |
---|---|---|---|
R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
FPAY | Renewal fee payment (event date is renewal date of database) |
Free format text: PAYMENT UNTIL: 20070726 Year of fee payment: 5 |
|
FPAY | Renewal fee payment (event date is renewal date of database) |
Free format text: PAYMENT UNTIL: 20080726 Year of fee payment: 6 |
|
FPAY | Renewal fee payment (event date is renewal date of database) |
Free format text: PAYMENT UNTIL: 20080726 Year of fee payment: 6 |
|
FPAY | Renewal fee payment (event date is renewal date of database) |
Free format text: PAYMENT UNTIL: 20090726 Year of fee payment: 7 |
|
FPAY | Renewal fee payment (event date is renewal date of database) |
Free format text: PAYMENT UNTIL: 20090726 Year of fee payment: 7 |
|
FPAY | Renewal fee payment (event date is renewal date of database) |
Free format text: PAYMENT UNTIL: 20100726 Year of fee payment: 8 |
|
FPAY | Renewal fee payment (event date is renewal date of database) |
Free format text: PAYMENT UNTIL: 20110726 Year of fee payment: 9 |
|
LAPS | Cancellation because of no payment of annual fees |