IL85983A - Human somatomedin carrier protein subunits, antibodies against them, pharmaceutical compostitions containing them and their use in the preparation of medicaments - Google Patents

Human somatomedin carrier protein subunits, antibodies against them, pharmaceutical compostitions containing them and their use in the preparation of medicaments

Info

Publication number: IL85983A
Authority: IL; Israel
Prior art keywords: carrier protein; human; growth; polypeptide; somatomedins
Prior art date: 1987-04-06

Application number

IL8598388A

Other languages

English (en)

Other versions

IL85983A0 (en

Original Assignee

Celtrix Pharma

Priority date (The priority date 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 date listed.)

1987-04-06

Filing date

1988-04-05

Publication date

1994-10-07

1988-04-05 Application filed by Celtrix Pharma filed Critical Celtrix Pharma

1988-09-30 Publication of IL85983A0 publication Critical patent/IL85983A0/xx

1994-10-07 Publication of IL85983A publication Critical patent/IL85983A/en

Links

108090000723 Insulin-Like Growth Factor I Proteins 0.000 title claims abstract description 58
102000013275 Somatomedins Human genes 0.000 title claims abstract description 48
238000002360 preparation method Methods 0.000 title claims abstract description 14
239000003814 drug Substances 0.000 title claims description 9
102000014914 Carrier Proteins Human genes 0.000 title abstract description 132
108010078791 Carrier Proteins Proteins 0.000 title abstract description 128
102000004196 processed proteins & peptides Human genes 0.000 claims abstract description 55
108090000765 processed proteins & peptides Proteins 0.000 claims abstract description 55
229920001184 polypeptide Polymers 0.000 claims abstract description 52
238000000034 method Methods 0.000 claims abstract description 25
230000008569 process Effects 0.000 claims abstract description 14
230000027455 binding Effects 0.000 claims description 61
102000004169 proteins and genes Human genes 0.000 claims description 31
108090000623 proteins and genes Proteins 0.000 claims description 31
235000018102 proteins Nutrition 0.000 claims description 29
239000000203 mixture Substances 0.000 claims description 26
230000012010 growth Effects 0.000 claims description 24
230000000694 effects Effects 0.000 claims description 20
241001465754 Metazoa Species 0.000 claims description 16
230000004071 biological effect Effects 0.000 claims description 14
208000027418 Wounds and injury Diseases 0.000 claims description 13
210000001519 tissue Anatomy 0.000 claims description 13
206010052428 Wound Diseases 0.000 claims description 12
102000004218 Insulin-Like Growth Factor I Human genes 0.000 claims description 10
230000002401 inhibitory effect Effects 0.000 claims description 10
230000001225 therapeutic effect Effects 0.000 claims description 10
102000003886 Glycoproteins Human genes 0.000 claims description 8
108090000288 Glycoproteins Proteins 0.000 claims description 8
230000035876 healing Effects 0.000 claims description 8
102000018997 Growth Hormone Human genes 0.000 claims description 7
108010051696 Growth Hormone Proteins 0.000 claims description 7
239000000122 growth hormone Substances 0.000 claims description 7
XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical group SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 claims description 6
125000001429 N-terminal alpha-amino-acid group Chemical group 0.000 claims description 6
230000001419 dependent effect Effects 0.000 claims description 6
150000003839 salts Chemical class 0.000 claims description 6
230000004936 stimulating effect Effects 0.000 claims description 5
235000018417 cysteine Nutrition 0.000 claims description 4
XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 claims description 4
239000012530 fluid Substances 0.000 claims description 4
206010000599 Acromegaly Diseases 0.000 claims description 3
206010012689 Diabetic retinopathy Diseases 0.000 claims description 3
210000000988 bone and bone Anatomy 0.000 claims description 3
125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 claims description 3
239000012634 fragment Substances 0.000 claims description 3
230000003211 malignant effect Effects 0.000 claims description 3
206010056438 Growth hormone deficiency Diseases 0.000 claims description 2
208000001936 exophthalmos Diseases 0.000 claims description 2
150000004676 glycans Chemical class 0.000 claims description 2
150000002632 lipids Chemical class 0.000 claims description 2
239000002773 nucleotide Substances 0.000 claims description 2
125000003729 nucleotide group Chemical group 0.000 claims description 2
229920001282 polysaccharide Polymers 0.000 claims description 2
239000005017 polysaccharide Substances 0.000 claims description 2
210000001210 retinal vessel Anatomy 0.000 claims description 2
210000002966 serum Anatomy 0.000 abstract description 16
238000011210 chromatographic step Methods 0.000 abstract description 3
QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 38
WEVYAHXRMPXWCK-UHFFFAOYSA-N Acetonitrile Chemical compound CC#N WEVYAHXRMPXWCK-UHFFFAOYSA-N 0.000 description 21
102000028416 insulin-like growth factor binding Human genes 0.000 description 16
108091022911 insulin-like growth factor binding Proteins 0.000 description 16
101001081567 Homo sapiens Insulin-like growth factor-binding protein 1 Proteins 0.000 description 15
102100027636 Insulin-like growth factor-binding protein 1 Human genes 0.000 description 15
239000000872 buffer Substances 0.000 description 14
238000000746 purification Methods 0.000 description 12
239000000243 solution Substances 0.000 description 11
229920005654 Sephadex Polymers 0.000 description 10
241000700159 Rattus Species 0.000 description 9
210000004027 cell Anatomy 0.000 description 9
239000012507 Sephadex™ Substances 0.000 description 8
238000002523 gelfiltration Methods 0.000 description 8
238000004128 high performance liquid chromatography Methods 0.000 description 8
239000003112 inhibitor Substances 0.000 description 8
239000000463 material Substances 0.000 description 8
YBYRMVIVWMBXKQ-UHFFFAOYSA-N phenylmethanesulfonyl fluoride Chemical compound FS(=O)(=O)CC1=CC=CC=C1 YBYRMVIVWMBXKQ-UHFFFAOYSA-N 0.000 description 8
239000006228 supernatant Substances 0.000 description 8
102000048143 Insulin-Like Growth Factor II Human genes 0.000 description 7
108090001117 Insulin-Like Growth Factor II Proteins 0.000 description 7
238000000159 protein binding assay Methods 0.000 description 7
238000001727 in vivo Methods 0.000 description 6
230000007935 neutral effect Effects 0.000 description 6
238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 6
206010028980 Neoplasm Diseases 0.000 description 5
235000001014 amino acid Nutrition 0.000 description 5
150000001413 amino acids Chemical class 0.000 description 5
239000012131 assay buffer Substances 0.000 description 5
210000002950 fibroblast Anatomy 0.000 description 5
-1 part Substances 0.000 description 5
238000011084 recovery Methods 0.000 description 5
238000002560 therapeutic procedure Methods 0.000 description 5
DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 0.000 description 5
229920000936 Agarose Polymers 0.000 description 4
208000026310 Breast neoplasm Diseases 0.000 description 4
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 4
DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 4
HDFGOPSGAURCEO-UHFFFAOYSA-N N-ethylmaleimide Chemical compound CCN1C(=O)C=CC1=O HDFGOPSGAURCEO-UHFFFAOYSA-N 0.000 description 4
FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 4
GPZPVAIBXPRLFD-UHFFFAOYSA-N acetic acid;azane Chemical compound N.N.CC(O)=O GPZPVAIBXPRLFD-UHFFFAOYSA-N 0.000 description 4
230000009471 action Effects 0.000 description 4
238000001042 affinity chromatography Methods 0.000 description 4
210000004381 amniotic fluid Anatomy 0.000 description 4
239000007864 aqueous solution Substances 0.000 description 4
238000003556 assay Methods 0.000 description 4
108091008324 binding proteins Proteins 0.000 description 4
230000000903 blocking effect Effects 0.000 description 4
210000002889 endothelial cell Anatomy 0.000 description 4
239000000499 gel Substances 0.000 description 4
239000008363 phosphate buffer Substances 0.000 description 4
239000002244 precipitate Substances 0.000 description 4
238000003127 radioimmunoassay Methods 0.000 description 4
230000001105 regulatory effect Effects 0.000 description 4
VGTPCRGMBIAPIM-UHFFFAOYSA-M sodium thiocyanate Chemical compound [Na+].[S-]C#N VGTPCRGMBIAPIM-UHFFFAOYSA-M 0.000 description 4
QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 description 3
108091003079 Bovine Serum Albumin Proteins 0.000 description 3
206010006187 Breast cancer Diseases 0.000 description 3
108010062580 Concanavalin A Proteins 0.000 description 3
241000282412 Homo Species 0.000 description 3
108010085220 Multiprotein Complexes Proteins 0.000 description 3
102000007474 Multiprotein Complexes Human genes 0.000 description 3
229920002684 Sepharose Polymers 0.000 description 3
ALSPKRWQCLSJLV-UHFFFAOYSA-N azanium;acetic acid;acetate Chemical compound [NH4+].CC(O)=O.CC([O-])=O ALSPKRWQCLSJLV-UHFFFAOYSA-N 0.000 description 3
230000015572 biosynthetic process Effects 0.000 description 3
230000001413 cellular effect Effects 0.000 description 3
238000012512 characterization method Methods 0.000 description 3
238000004587 chromatography analysis Methods 0.000 description 3
206010012601 diabetes mellitus Diseases 0.000 description 3
201000010099 disease Diseases 0.000 description 3
208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 3
239000002532 enzyme inhibitor Substances 0.000 description 3
238000000605 extraction Methods 0.000 description 3
230000001605 fetal effect Effects 0.000 description 3
238000005194 fractionation Methods 0.000 description 3
230000036541 health Effects 0.000 description 3
238000003018 immunoassay Methods 0.000 description 3
238000002347 injection Methods 0.000 description 3
239000007924 injection Substances 0.000 description 3
238000004255 ion exchange chromatography Methods 0.000 description 3
210000005229 liver cell Anatomy 0.000 description 3
230000002297 mitogenic effect Effects 0.000 description 3
208000001685 postmenopausal osteoporosis Diseases 0.000 description 3
230000035755 proliferation Effects 0.000 description 3
230000001737 promoting effect Effects 0.000 description 3
230000004952 protein activity Effects 0.000 description 3
238000011160 research Methods 0.000 description 3
239000011347 resin Substances 0.000 description 3
229920005989 resin Polymers 0.000 description 3
239000001488 sodium phosphate Substances 0.000 description 3
229910000162 sodium phosphate Inorganic materials 0.000 description 3
238000007920 subcutaneous administration Methods 0.000 description 3
238000003786 synthesis reaction Methods 0.000 description 3
230000032258 transport Effects 0.000 description 3
LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 3
RYFMWSXOAZQYPI-UHFFFAOYSA-K trisodium phosphate Chemical compound [Na+].[Na+].[Na+].[O-]P([O-])([O-])=O RYFMWSXOAZQYPI-UHFFFAOYSA-K 0.000 description 3
XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 3
230000029663 wound healing Effects 0.000 description 3
DGZSVBBLLGZHSF-UHFFFAOYSA-N 4,4-diethylpiperidine Chemical compound CCC1(CC)CCNCC1 DGZSVBBLLGZHSF-UHFFFAOYSA-N 0.000 description 2
108010039627 Aprotinin Proteins 0.000 description 2
102000004506 Blood Proteins Human genes 0.000 description 2
108010017384 Blood Proteins Proteins 0.000 description 2
OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 description 2
102000008186 Collagen Human genes 0.000 description 2
108010035532 Collagen Proteins 0.000 description 2
229920002307 Dextran Polymers 0.000 description 2
201000008808 Fibrosarcoma Diseases 0.000 description 2
108010075626 Nonsuppressible Insulin-Like Activity Proteins 0.000 description 2
208000001132 Osteoporosis Diseases 0.000 description 2
108091005804 Peptidases Proteins 0.000 description 2
239000004365 Protease Substances 0.000 description 2
108010001267 Protein Subunits Proteins 0.000 description 2
102000002067 Protein Subunits Human genes 0.000 description 2
102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 2
239000007983 Tris buffer Substances 0.000 description 2
238000010521 absorption reaction Methods 0.000 description 2
230000002378 acidificating effect Effects 0.000 description 2
239000003463 adsorbent Substances 0.000 description 2
BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 description 2
229910052921 ammonium sulfate Inorganic materials 0.000 description 2
235000011130 ammonium sulphate Nutrition 0.000 description 2
230000000890 antigenic effect Effects 0.000 description 2
229960004405 aprotinin Drugs 0.000 description 2
229940098773 bovine serum albumin Drugs 0.000 description 2
238000005119 centrifugation Methods 0.000 description 2
238000006243 chemical reaction Methods 0.000 description 2
239000003153 chemical reaction reagent Substances 0.000 description 2
239000003795 chemical substances by application Substances 0.000 description 2
229920001436 collagen Polymers 0.000 description 2
239000000356 contaminant Substances 0.000 description 2
230000007812 deficiency Effects 0.000 description 2
238000000502 dialysis Methods 0.000 description 2
238000010494 dissociation reaction Methods 0.000 description 2
230000005593 dissociations Effects 0.000 description 2
239000012153 distilled water Substances 0.000 description 2
230000006862 enzymatic digestion Effects 0.000 description 2
230000001747 exhibiting effect Effects 0.000 description 2
239000000284 extract Substances 0.000 description 2
239000005556 hormone Substances 0.000 description 2
229940088597 hormone Drugs 0.000 description 2
230000002218 hypoglycaemic effect Effects 0.000 description 2
238000002513 implantation Methods 0.000 description 2
238000000338 in vitro Methods 0.000 description 2
238000011534 incubation Methods 0.000 description 2
ZPNFWUPYTFPOJU-LPYSRVMUSA-N iniprol Chemical compound C([C@H]1C(=O)NCC(=O)NCC(=O)N[C@H]2CSSC[C@H]3C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@H](C(N[C@H](C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=4C=CC(O)=CC=4)C(=O)N[C@@H](CC=4C=CC=CC=4)C(=O)N[C@@H](CC=4C=CC(O)=CC=4)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C)NC(=O)[C@H](CO)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC=4C=CC=CC=4)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCCCN)NC(=O)[C@H](C)NC(=O)[C@H](CCCNC(N)=N)NC2=O)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](CC=2C=CC=CC=2)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H]2N(CCC2)C(=O)[C@@H](N)CCCNC(N)=N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N2[C@@H](CCC2)C(=O)N2[C@@H](CCC2)C(=O)N[C@@H](CC=2C=CC(O)=CC=2)C(=O)N[C@@H]([C@@H](C)O)C(=O)NCC(=O)N2[C@@H](CCC2)C(=O)N3)C(=O)NCC(=O)NCC(=O)N[C@@H](C)C(O)=O)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@H](C(=O)N[C@@H](CC=2C=CC=CC=2)C(=O)N[C@H](C(=O)N1)C(C)C)[C@@H](C)O)[C@@H](C)CC)=O)[C@@H](C)CC)C1=CC=C(O)C=C1 ZPNFWUPYTFPOJU-LPYSRVMUSA-N 0.000 description 2
NOESYZHRGYRDHS-UHFFFAOYSA-N insulin Chemical compound N1C(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(NC(=O)CN)C(C)CC)CSSCC(C(NC(CO)C(=O)NC(CC(C)C)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CCC(N)=O)C(=O)NC(CC(C)C)C(=O)NC(CCC(O)=O)C(=O)NC(CC(N)=O)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CSSCC(NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2C=CC(O)=CC=2)NC(=O)C(CC(C)C)NC(=O)C(C)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2NC=NC=2)NC(=O)C(CO)NC(=O)CNC2=O)C(=O)NCC(=O)NC(CCC(O)=O)C(=O)NC(CCCNC(N)=N)C(=O)NCC(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC(O)=CC=3)C(=O)NC(C(C)O)C(=O)N3C(CCC3)C(=O)NC(CCCCN)C(=O)NC(C)C(O)=O)C(=O)NC(CC(N)=O)C(O)=O)=O)NC(=O)C(C(C)CC)NC(=O)C(CO)NC(=O)C(C(C)O)NC(=O)C1CSSCC2NC(=O)C(CC(C)C)NC(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CC(N)=O)NC(=O)C(NC(=O)C(N)CC=1C=CC=CC=1)C(C)C)CC1=CN=CN1 NOESYZHRGYRDHS-UHFFFAOYSA-N 0.000 description 2
102000032003 insulin-like growth factor I binding proteins Human genes 0.000 description 2
108091010168 insulin-like growth factor I binding proteins Proteins 0.000 description 2
230000002608 insulinlike Effects 0.000 description 2
238000002955 isolation Methods 0.000 description 2
230000036961 partial effect Effects 0.000 description 2
KHIWWQKSHDUIBK-UHFFFAOYSA-N periodic acid Chemical compound OI(=O)(=O)=O KHIWWQKSHDUIBK-UHFFFAOYSA-N 0.000 description 2
125000001997 phenyl group Chemical group [H]C1=C([H])C([H])=C(*)C([H])=C1[H] 0.000 description 2
230000003389 potentiating effect Effects 0.000 description 2
239000000047 product Substances 0.000 description 2
239000012460 protein solution Substances 0.000 description 2
230000002829 reductive effect Effects 0.000 description 2
230000004044 response Effects 0.000 description 2
238000004007 reversed phase HPLC Methods 0.000 description 2
229920000260 silastic Polymers 0.000 description 2
239000011780 sodium chloride Substances 0.000 description 2
239000007787 solid Substances 0.000 description 2
241000894007 species Species 0.000 description 2
238000010186 staining Methods 0.000 description 2
QTBSBXVTEAMEQO-UHFFFAOYSA-M Acetate Chemical compound CC([O-])=O QTBSBXVTEAMEQO-UHFFFAOYSA-M 0.000 description 1
108010088751 Albumins Proteins 0.000 description 1
102000009027 Albumins Human genes 0.000 description 1
USFZMSVCRYTOJT-UHFFFAOYSA-N Ammonium acetate Chemical compound N.CC(O)=O USFZMSVCRYTOJT-UHFFFAOYSA-N 0.000 description 1
239000005695 Ammonium acetate Substances 0.000 description 1
208000002109 Argyria Diseases 0.000 description 1
102000000119 Beta-lactoglobulin Human genes 0.000 description 1
201000004569 Blindness Diseases 0.000 description 1
241000283690 Bos taurus Species 0.000 description 1
208000005243 Chondrosarcoma Diseases 0.000 description 1
108010038061 Chymotrypsinogen Proteins 0.000 description 1
230000006820 DNA synthesis Effects 0.000 description 1
102000004190 Enzymes Human genes 0.000 description 1
108090000790 Enzymes Proteins 0.000 description 1
WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 1
239000004471 Glycine Substances 0.000 description 1
101001075374 Homo sapiens Gamma-glutamyl hydrolase Proteins 0.000 description 1
101000599951 Homo sapiens Insulin-like growth factor I Proteins 0.000 description 1
101000664737 Homo sapiens Somatotropin Proteins 0.000 description 1
102000002265 Human Growth Hormone Human genes 0.000 description 1
108010000521 Human Growth Hormone Proteins 0.000 description 1
239000000854 Human Growth Hormone Substances 0.000 description 1
108091006905 Human Serum Albumin 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
208000013016 Hypoglycemia Diseases 0.000 description 1
102000004877 Insulin Human genes 0.000 description 1
108090001061 Insulin Proteins 0.000 description 1
102100037852 Insulin-like growth factor I Human genes 0.000 description 1
208000008839 Kidney Neoplasms Diseases 0.000 description 1
QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 1
108010060630 Lactoglobulins Proteins 0.000 description 1
102000016943 Muramidase Human genes 0.000 description 1
108010014251 Muramidase Proteins 0.000 description 1
102000003505 Myosin Human genes 0.000 description 1
108060008487 Myosin Proteins 0.000 description 1
101001055320 Myxine glutinosa Insulin-like growth factor Proteins 0.000 description 1
108010062010 N-Acetylmuramoyl-L-alanine Amidase Proteins 0.000 description 1
GHAZCVNUKKZTLG-UHFFFAOYSA-N N-ethyl-succinimide Natural products CCN1C(=O)CCC1=O GHAZCVNUKKZTLG-UHFFFAOYSA-N 0.000 description 1
108010058846 Ovalbumin Proteins 0.000 description 1
108010065081 Phosphorylase b Proteins 0.000 description 1
241000700157 Rattus norvegicus Species 0.000 description 1
206010038934 Retinopathy proliferative Diseases 0.000 description 1
241000283984 Rodentia Species 0.000 description 1
239000012506 Sephacryl® Substances 0.000 description 1
238000012300 Sequence Analysis Methods 0.000 description 1
BQCADISMDOOEFD-UHFFFAOYSA-N Silver Chemical compound [Ag] BQCADISMDOOEFD-UHFFFAOYSA-N 0.000 description 1
235000018259 Solanum vestissimum Nutrition 0.000 description 1
240000002825 Solanum vestissimum Species 0.000 description 1
208000007536 Thrombosis Diseases 0.000 description 1
DTQVDTLACAAQTR-UHFFFAOYSA-N Trifluoroacetic acid Chemical compound OC(=O)C(F)(F)F DTQVDTLACAAQTR-UHFFFAOYSA-N 0.000 description 1
230000002159 abnormal effect Effects 0.000 description 1
239000002253 acid Substances 0.000 description 1
239000003929 acidic solution Substances 0.000 description 1
239000013543 active substance Substances 0.000 description 1
210000001789 adipocyte Anatomy 0.000 description 1
210000000577 adipose tissue Anatomy 0.000 description 1
230000002411 adverse Effects 0.000 description 1
235000004279 alanine Nutrition 0.000 description 1
235000019257 ammonium acetate Nutrition 0.000 description 1
229940043376 ammonium acetate Drugs 0.000 description 1
238000004458 analytical method Methods 0.000 description 1
230000033115 angiogenesis Effects 0.000 description 1
239000003242 anti bacterial agent Substances 0.000 description 1
229940088710 antibiotic agent Drugs 0.000 description 1
239000000427 antigen Substances 0.000 description 1
108091007433 antigens Proteins 0.000 description 1
102000036639 antigens Human genes 0.000 description 1
WQZGKKKJIJFFOK-VFUOTHLCSA-N beta-D-glucose Chemical compound OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-VFUOTHLCSA-N 0.000 description 1
210000004204 blood vessel Anatomy 0.000 description 1
210000001124 body fluid Anatomy 0.000 description 1
239000010839 body fluid Substances 0.000 description 1
210000000481 breast Anatomy 0.000 description 1
239000007853 buffer solution Substances 0.000 description 1
YXMVRBZGTJFMLH-UHFFFAOYSA-N butylsilane Chemical compound CCCC[SiH3] YXMVRBZGTJFMLH-UHFFFAOYSA-N 0.000 description 1
201000011510 cancer Diseases 0.000 description 1
230000015556 catabolic process Effects 0.000 description 1
238000004113 cell culture Methods 0.000 description 1
239000003610 charcoal Substances 0.000 description 1
239000003638 chemical reducing agent Substances 0.000 description 1
238000005352 clarification Methods 0.000 description 1
238000012875 competitive assay Methods 0.000 description 1
230000000536 complexating effect Effects 0.000 description 1
239000012141 concentrate Substances 0.000 description 1
239000003636 conditioned culture medium Substances 0.000 description 1
230000008878 coupling Effects 0.000 description 1
238000010168 coupling process Methods 0.000 description 1
238000005859 coupling reaction Methods 0.000 description 1
230000006378 damage Effects 0.000 description 1
238000011161 development Methods 0.000 description 1
230000001904 diabetogenic effect Effects 0.000 description 1
CGMRCMMOCQYHAD-UHFFFAOYSA-J dicalcium hydroxide phosphate Chemical compound [OH-].[Ca++].[Ca++].[O-]P([O-])([O-])=O CGMRCMMOCQYHAD-UHFFFAOYSA-J 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
229940079593 drug Drugs 0.000 description 1
229960001484 edetic acid Drugs 0.000 description 1
238000001962 electrophoresis Methods 0.000 description 1
230000003511 endothelial effect Effects 0.000 description 1
239000003623 enhancer Substances 0.000 description 1
229940088598 enzyme Drugs 0.000 description 1
238000002474 experimental method Methods 0.000 description 1
238000001641 gel filtration chromatography Methods 0.000 description 1
238000005227 gel permeation chromatography Methods 0.000 description 1
239000008103 glucose Substances 0.000 description 1
230000013595 glycosylation Effects 0.000 description 1
238000006206 glycosylation reaction Methods 0.000 description 1
210000000224 granular leucocyte Anatomy 0.000 description 1
239000007952 growth promoter Substances 0.000 description 1
229960004198 guanidine Drugs 0.000 description 1
PJJJBBJSCAKJQF-UHFFFAOYSA-N guanidinium chloride Chemical compound [Cl-].NC(N)=[NH2+] PJJJBBJSCAKJQF-UHFFFAOYSA-N 0.000 description 1
230000009442 healing mechanism Effects 0.000 description 1
206010073071 hepatocellular carcinoma Diseases 0.000 description 1
210000003494 hepatocyte Anatomy 0.000 description 1
230000003054 hormonal effect Effects 0.000 description 1
238000004191 hydrophobic interaction chromatography Methods 0.000 description 1
229910052588 hydroxylapatite Inorganic materials 0.000 description 1
229960002591 hydroxyproline Drugs 0.000 description 1
230000001900 immune effect Effects 0.000 description 1
238000003364 immunohistochemistry Methods 0.000 description 1
239000012535 impurity Substances 0.000 description 1
238000001802 infusion Methods 0.000 description 1
230000005764 inhibitory process Effects 0.000 description 1
208000014674 injury Diseases 0.000 description 1
229940125396 insulin Drugs 0.000 description 1
PGLTVOMIXTUURA-UHFFFAOYSA-N iodoacetamide Chemical compound NC(=O)CI PGLTVOMIXTUURA-UHFFFAOYSA-N 0.000 description 1
239000003446 ligand Substances 0.000 description 1
230000002366 lipolytic effect Effects 0.000 description 1
238000004811 liquid chromatography Methods 0.000 description 1
210000004185 liver Anatomy 0.000 description 1
230000007774 longterm Effects 0.000 description 1
229960000274 lysozyme Drugs 0.000 description 1
239000004325 lysozyme Substances 0.000 description 1
235000010335 lysozyme Nutrition 0.000 description 1
101710155777 mRNA export factor ICP27 homolog Proteins 0.000 description 1
210000002540 macrophage Anatomy 0.000 description 1
125000000311 mannosyl group Chemical group C1([C@@H](O)[C@@H](O)[C@H](O)[C@H](O1)CO)* 0.000 description 1
238000004519 manufacturing process Methods 0.000 description 1
239000011159 matrix material Substances 0.000 description 1
238000005259 measurement Methods 0.000 description 1
239000012528 membrane Substances 0.000 description 1
230000002503 metabolic effect Effects 0.000 description 1
230000005012 migration Effects 0.000 description 1
238000013508 migration Methods 0.000 description 1
230000003278 mimic effect Effects 0.000 description 1
239000003226 mitogen Substances 0.000 description 1
210000000663 muscle cell Anatomy 0.000 description 1
230000003387 muscular Effects 0.000 description 1
QYSGYZVSCZSLHT-UHFFFAOYSA-N octafluoropropane Chemical compound FC(F)(F)C(F)(F)C(F)(F)F QYSGYZVSCZSLHT-UHFFFAOYSA-N 0.000 description 1
230000011164 ossification Effects 0.000 description 1
210000000963 osteoblast Anatomy 0.000 description 1
229940092253 ovalbumin Drugs 0.000 description 1
230000003076 paracrine Effects 0.000 description 1
XYJRXVWERLGGKC-UHFFFAOYSA-D pentacalcium;hydroxide;triphosphate Chemical compound [OH-].[Ca+2].[Ca+2].[Ca+2].[Ca+2].[Ca+2].[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O XYJRXVWERLGGKC-UHFFFAOYSA-D 0.000 description 1
239000008194 pharmaceutical composition Substances 0.000 description 1
230000006461 physiological response Effects 0.000 description 1
230000036470 plasma concentration Effects 0.000 description 1
229920002401 polyacrylamide Polymers 0.000 description 1
239000000843 powder Substances 0.000 description 1
230000002035 prolonged effect Effects 0.000 description 1
239000011541 reaction mixture Substances 0.000 description 1
230000009257 reactivity Effects 0.000 description 1
238000012827 research and development Methods 0.000 description 1
230000002441 reversible effect Effects 0.000 description 1
230000028327 secretion Effects 0.000 description 1
238000013207 serial dilution Methods 0.000 description 1
229910052709 silver Inorganic materials 0.000 description 1
239000004332 silver Substances 0.000 description 1
238000001179 sorption measurement Methods 0.000 description 1
238000013222 sprague-dawley male rat Methods 0.000 description 1
230000000087 stabilizing effect Effects 0.000 description 1
229910001220 stainless steel Inorganic materials 0.000 description 1
150000003431 steroids Chemical class 0.000 description 1
238000003860 storage Methods 0.000 description 1
239000000126 substance Substances 0.000 description 1
230000004083 survival effect Effects 0.000 description 1
239000000725 suspension Substances 0.000 description 1
229940124597 therapeutic agent Drugs 0.000 description 1
FGMPLJWBKKVCDB-UHFFFAOYSA-N trans-L-hydroxy-proline Natural products ON1CCCC1C(O)=O FGMPLJWBKKVCDB-UHFFFAOYSA-N 0.000 description 1
230000004614 tumor growth Effects 0.000 description 1
238000000108 ultra-filtration Methods 0.000 description 1
238000005199 ultracentrifugation Methods 0.000 description 1
230000002792 vascular Effects 0.000 description 1
238000001262 western blot 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
- C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
- C07K14/47—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
- C07K14/4701—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals not used
- C07K14/4743—Insulin-like growth factor binding protein
- 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
- A61P27/00—Drugs for disorders of the senses
- A61P27/02—Ophthalmic agents
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P3/00—Drugs for disorders of the metabolism
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P3/00—Drugs for disorders of the metabolism
- A61P3/08—Drugs for disorders of the metabolism for glucose homeostasis
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P35/00—Antineoplastic agents
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P43/00—Drugs for specific purposes, not provided for in groups A61P1/00-A61P41/00
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides

Landscapes

Health & Medical Sciences (AREA)
Chemical & Material Sciences (AREA)
Life Sciences & Earth Sciences (AREA)
Organic Chemistry (AREA)
General Health & Medical Sciences (AREA)
Medicinal Chemistry (AREA)
Animal Behavior & Ethology (AREA)
Pharmacology & Pharmacy (AREA)
Veterinary Medicine (AREA)
Chemical Kinetics & Catalysis (AREA)
General Chemical & Material Sciences (AREA)
Public Health (AREA)
Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
Engineering & Computer Science (AREA)
Bioinformatics & Cheminformatics (AREA)
Diabetes (AREA)
Obesity (AREA)
Hematology (AREA)
Toxicology (AREA)
Biochemistry (AREA)
Ophthalmology & Optometry (AREA)
Dermatology (AREA)
Endocrinology (AREA)
Zoology (AREA)
Gastroenterology & Hepatology (AREA)
Emergency Medicine (AREA)
Biophysics (AREA)
Genetics & Genomics (AREA)
Molecular Biology (AREA)
Proteomics, Peptides & Aminoacids (AREA)
Peptides Or Proteins (AREA)
Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Preparation Of Compounds By Using Micro-Organisms (AREA)

IL8598388A 1987-04-06 1988-04-05 Human somatomedin carrier protein subunits, antibodies against them, pharmaceutical compostitions containing them and their use in the preparation of medicaments IL85983A (en)

Applications Claiming Priority (1)

Application Number	Priority Date	Filing Date	Title
US3488587A	1987-04-06	1987-04-06

Publications (2)

Publication Number	Publication Date
IL85983A0 IL85983A0 (en)	1988-09-30
IL85983A true IL85983A (en)	1994-10-07

Family

ID=21879212

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
IL8598388A IL85983A (en)	1987-04-06	1988-04-05	Human somatomedin carrier protein subunits, antibodies against them, pharmaceutical compostitions containing them and their use in the preparation of medicaments

Country Status (11)

Country	Link
EP (2)	EP0308500B1 (da)
JP (1)	JP2648951B2 (da)
AT (1)	ATE90690T1 (da)
AU (1)	AU627423B2 (da)
CA (1)	CA1340295C (da)
DE (1)	DE3881801T2 (da)
DK (1)	DK677688D0 (da)
ES (1)	ES2058341T3 (da)
IL (1)	IL85983A (da)
WO (1)	WO1988007863A1 (da)
ZA (1)	ZA882407B (da)

Families Citing this family (27)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
US5973115A (en) *	1987-05-15	1999-10-26	Amgen Inc.	Method for potentiating and inhibiting insulin-like growth factor activity
US5258287A (en) *	1988-03-22	1993-11-02	Genentech, Inc.	DNA encoding and methods of production of insulin-like growth factor binding protein BP53
ATE132164T1 (de) *	1988-04-12	1996-01-15	Amgen Boulder Inc	Verfahren zur steigerung und zur hemmung der wirkung eines insulinähnlichen wachstumfaktors
US6465423B1 (en)	1988-07-15	2002-10-15	Central Sydney Area Health Service	Acid-labile subunit (ALS) of insulin-like growth factor binding protein complex
CA1341598C (en) *	1988-07-15	2009-09-29	Central Sydney Area Health Service	Acid-labile sub-unit (als) of insulin-like growth factor binding proteincomplex
US5324820A (en) *	1988-07-15	1994-06-28	Central Sydney Area Health Service	Acid-labile subunit (ALS) of insulin-like growth factor binding protein complex
US5187151A (en) *	1991-02-12	1993-02-16	Genentech, Inc.	Use of binding protein with igf-i as an anabolic growth promoting agent
RU2126683C1 (ru) *	1992-12-17	1999-02-27	Товарищество с ограниченной ответственностью "САМИ"	Способ получения антисоматотропной сыворотки
CA2195474A1 (en) *	1994-07-20	1996-02-01	Cedo Martin Bagi	Igf/igfbp complex for promoting bone formation and for regulating bone remodeling
US6420518B1 (en)	1997-04-04	2002-07-16	Genetech, Inc.	Insulin-like growth factor agonist molecules
US6121416A (en)	1997-04-04	2000-09-19	Genentech, Inc.	Insulin-like growth factor agonist molecules
JP2002535967A (ja)	1999-01-06	2002-10-29	ジェネンテック・インコーポレーテッド	インシュリン様成長因子（ｉｇｆ）ｉ変異体
AU762351B2 (en)	1999-01-06	2003-06-26	Genentech Inc.	Insulin-like growth factor (IGF) I mutant variants
ATE389416T1 (de)	2000-05-16	2008-04-15	Genentech Inc	Behandlung von knorpelerkrankungen
WO2002072780A2 (en)	2001-03-14	2002-09-19	Genentech, Inc.	Igf antagonist peptides
CA2524305C (en)	2003-05-01	2015-12-08	Imclone Systems Incorporated	Fully human antibodies directed against the human insulin-like growth factor-1 receptor
EP2274978B1 (en)	2003-09-12	2015-05-20	Tercica, Inc.	Methods for treatment of insulin-like growth factor-I(IGF-I) deficiency
US7192738B2 (en)	2003-10-03	2007-03-20	Genentech, Inc.	IGF binding proteins
CA2612449A1 (en)	2005-06-17	2006-12-28	Imclone Systems Incorporated	Receptor antagonists for treatment of metastatic bone cancer
AP2008004569A0 (en)	2006-02-03	2008-08-31	Imclone Systems Inc	IGR-IR antagonists as adjuvants for treatment of prostrate cancer
CA3075482A1 (en)	2017-09-11	2019-03-14	Shire Human Genetic Therapies, Inc.	Methods and compositions for treating chronic lung diseases
MX2023004426A (es)	2020-10-19	2023-08-04	Oak Hill Bio Ltd	Composiciones adecuadas para su uso en neonatos.
AU2023210427A1 (en)	2022-01-19	2024-08-22	Oak Hill Bio Limited	Compositions and methods for reducing oxidation of igf‐1/igfbp
WO2023242440A1 (en)	2022-06-17	2023-12-21	Oak Hill Bio Limited	Treament of lungs in infants
WO2023242442A1 (en)	2022-06-17	2023-12-21	Oak Hill Bio Limited	Method of maturing/differentiating neurons and/or modulating the vagus nerve
WO2023242439A1 (en)	2022-06-17	2023-12-21	Oak Hill Bio Limited	Vascular stabilisation (preterm infants)
CN120882420A (zh)	2023-02-14	2025-10-31	奥克希尔生物有限公司	Gi组织中愈合失调的治疗

1988
- 1988-03-31 AT AT88904042T patent/ATE90690T1/de active
- 1988-03-31 AU AU17020/88A patent/AU627423B2/en not_active Ceased
- 1988-03-31 WO PCT/US1988/001042 patent/WO1988007863A1/en not_active Ceased
- 1988-03-31 JP JP63503623A patent/JP2648951B2/ja not_active Expired - Lifetime
- 1988-03-31 ES ES88904042T patent/ES2058341T3/es not_active Expired - Lifetime
- 1988-03-31 EP EP88904042A patent/EP0308500B1/en not_active Expired - Lifetime
- 1988-03-31 DE DE88904042T patent/DE3881801T2/de not_active Expired - Fee Related
- 1988-04-05 IL IL8598388A patent/IL85983A/en unknown
- 1988-04-05 CA CA000563309A patent/CA1340295C/en not_active Expired - Fee Related
- 1988-04-06 EP EP88303041A patent/EP0294021A1/en active Pending
- 1988-04-07 ZA ZA882407A patent/ZA882407B/xx unknown
- 1988-12-05 DK DK677688A patent/DK677688D0/da not_active Application Discontinuation

Also Published As

Publication number	Publication date
EP0308500A1 (en)	1989-03-29
DK677688A (da)	1988-12-05
AU627423B2 (en)	1992-08-27
ES2058341T3 (es)	1994-11-01
DE3881801T2 (de)	1993-12-23
IL85983A0 (en)	1988-09-30
DE3881801D1 (de)	1993-07-22
EP0308500B1 (en)	1993-06-16
CA1340295C (en)	1998-12-29
DK677688D0 (da)	1988-12-05
JPH01502986A (ja)	1989-10-12
ZA882407B (en)	1988-09-28
JP2648951B2 (ja)	1997-09-03
EP0294021A1 (en)	1988-12-07
ATE90690T1 (de)	1993-07-15
AU1702088A (en)	1988-11-04
WO1988007863A1 (en)	1988-10-20

Publication	Publication Date	Title
EP0308500B1 (en)	1993-06-16	Human somatomedin carrier protein subunits and process for producing them
US5200509A (en)	1993-04-06	Human somatomedin carrier protein subunits and process for producing them; recombinant DNA molecules, hosts, processes and human somatomedin carrier protein-like polypeptides
Zapf et al.	1980	Serum levels of insulin-like growth factor (IGF) and its carrier protein in various metabolic disorders
CA2006322C (en)	2000-08-01	Recombinant dna molecules, hosts, processes and human somatomedin carrier protein-like polypeptides
Doneen et al.	1979	Studies on prolactin. Selective reduction of the disulfide bonds of the ovine hormone
HK1000826B (en)	1998-05-01	Recombinant dna molecules, hosts, processes and human somatomedin carrier protein-like polypeptides
JPH03506030A (ja)	1991-12-26	インスリン様成長因子（ｉｇｆ）結合蛋白複合体の酸不安定サブユニット（ａｌｓ）
JP2819467B2 (ja)	1998-10-30	新規なカルジオジラチン断片およびその製造方法
JP2527896B2 (ja)	1996-08-28	ヒト骨由来インスリン様成長因子結合タンパク
JPH11506337A (ja)	1999-06-08	骨刺激因子
Fryklund et al.	1978	Chemistry and biology of the somatomedins
Robbins et al.	1985	Products of therapeutic insulins in the blood of insulin-dependent (type I) diabetic patients
DEVITO	1989	Comparison of brain and pituitary immunoreactive prolactin by peptide mapping and lectin affinity chromatography
WO2003102180A1 (fr)	2003-12-11	Nouveaux peptides avec activite de production de camp
JP2803184B2 (ja)	1998-09-24	酸性線維芽細胞成長因子の抗体，その用途およびペプチド
Ooi et al.	1990	Recognition of insulin-like-growth-factor-binding proteins in serum and amniotic fluid by an antiserum against a low-molecular-mass insulin-like-growth-factor-inhibitor/binding protein
JP2562892B2 (ja)	1996-12-11	インスリン結合活性を有するポリペプチド
WO1996019501A1 (en)	1996-06-27	Modulators of bone cell function and uses thereof