NZ529560A - Pharmaceutical compositions and methods of using secreted frizzled related protein - Google Patents

Pharmaceutical compositions and methods of using secreted frizzled related protein

Info

Publication number: NZ529560A
Authority: NZ; New Zealand
Prior art keywords: sfrp; cells; hob; lys; leu
Prior art date: 1999-09-13

Application number

NZ529560A

Other languages

English (en)

Inventor

Peter V N Bodine

Original Assignee

Wyeth Corp

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.)

1999-09-13

Filing date

2000-09-13

Publication date

2005-05-27

2000-09-13 Application filed by Wyeth Corp filed Critical Wyeth Corp

2005-05-27 Publication of NZ529560A publication Critical patent/NZ529560A/en

Links

108010020277 WD repeat containing planar cell polarity effector Proteins 0.000 title claims description 88
238000000034 method Methods 0.000 title claims description 47
102100030053 Secreted frizzled-related protein 3 Human genes 0.000 title claims description 16
239000008194 pharmaceutical composition Substances 0.000 title claims description 12
210000004027 cell Anatomy 0.000 claims description 350
108090000623 proteins and genes Proteins 0.000 claims description 131
108091033319 polynucleotide Proteins 0.000 claims description 78
102000040430 polynucleotide Human genes 0.000 claims description 78
239000002157 polynucleotide Substances 0.000 claims description 77
102000004169 proteins and genes Human genes 0.000 claims description 65
241000282414 Homo sapiens Species 0.000 claims description 51
230000000694 effects Effects 0.000 claims description 50
239000012634 fragment Substances 0.000 claims description 41
210000000988 bone and bone Anatomy 0.000 claims description 39
230000001105 regulatory effect Effects 0.000 claims description 38
150000001413 amino acids Chemical class 0.000 claims description 29
239000000203 mixture Substances 0.000 claims description 28
210000000963 osteoblast Anatomy 0.000 claims description 28
208000037265 diseases, disorders, signs and symptoms Diseases 0.000 claims description 24
125000003729 nucleotide group Chemical group 0.000 claims description 24
239000002773 nucleotide Substances 0.000 claims description 23
208000035475 disorder Diseases 0.000 claims description 20
230000011164 ossification Effects 0.000 claims description 18
230000000692 anti-sense effect Effects 0.000 claims description 15
208000020084 Bone disease Diseases 0.000 claims description 13
238000009396 hybridization Methods 0.000 claims description 12
XDMCWZFLLGVIID-SXPRBRBTSA-N O-(3-O-D-galactosyl-N-acetyl-beta-D-galactosaminyl)-L-serine Chemical compound CC(=O)N[C@H]1[C@H](OC[C@H]([NH3+])C([O-])=O)O[C@H](CO)[C@H](O)[C@@H]1OC1[C@H](O)[C@@H](O)[C@@H](O)[C@@H](CO)O1 XDMCWZFLLGVIID-SXPRBRBTSA-N 0.000 claims description 9
208000001132 Osteoporosis Diseases 0.000 claims description 9
241000124008 Mammalia Species 0.000 claims description 6
208000006386 Bone Resorption Diseases 0.000 claims description 5
230000024279 bone resorption Effects 0.000 claims description 5
238000004113 cell culture Methods 0.000 claims description 5
230000003412 degenerative effect Effects 0.000 claims description 4
208000029725 Metabolic bone disease Diseases 0.000 claims description 3
206010049088 Osteopenia Diseases 0.000 claims description 3
102000036639 antigens Human genes 0.000 claims description 3
210000002449 bone cell Anatomy 0.000 claims description 3
230000037182 bone density Effects 0.000 claims description 3
230000004770 neurodegeneration Effects 0.000 claims description 3
238000002360 preparation method Methods 0.000 claims description 3
125000002924 primary amino group Chemical group [H]N([H])* 0.000 claims description 3
230000008439 repair process Effects 0.000 claims description 3
201000008482 osteoarthritis Diseases 0.000 claims description 2
VPZXBVLAVMBEQI-UHFFFAOYSA-N glycyl-DL-alpha-alanine Natural products OC(=O)C(C)NC(=O)CN VPZXBVLAVMBEQI-UHFFFAOYSA-N 0.000 claims 3
MNZHHDPWDWQJCQ-YUMQZZPRSA-N Ala-Leu-Gly Chemical compound C[C@H](N)C(=O)N[C@@H](CC(C)C)C(=O)NCC(O)=O MNZHHDPWDWQJCQ-YUMQZZPRSA-N 0.000 claims 2
QXOHLNCNYLGICT-YFKPBYRVSA-N Met-Gly Chemical compound CSCC[C@H](N)C(=O)NCC(O)=O QXOHLNCNYLGICT-YFKPBYRVSA-N 0.000 claims 2
108010079364 N-glycylalanine Proteins 0.000 claims 2
108010049041 glutamylalanine Proteins 0.000 claims 2
108010054155 lysyllysine Proteins 0.000 claims 2
108010005942 methionylglycine Proteins 0.000 claims 2
WQVYAWIMAWTGMW-ZLUOBGJFSA-N Ala-Asp-Cys Chemical compound C[C@@H](C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CS)C(=O)O)N WQVYAWIMAWTGMW-ZLUOBGJFSA-N 0.000 claims 1
OBVSBEYOMDWLRJ-BFHQHQDPSA-N Ala-Gly-Thr Chemical compound C[C@@H](O)[C@@H](C(O)=O)NC(=O)CNC(=O)[C@H](C)N OBVSBEYOMDWLRJ-BFHQHQDPSA-N 0.000 claims 1
GFEDXKNBZMPEDM-KZVJFYERSA-N Ala-Met-Thr Chemical compound [H]N[C@@H](C)C(=O)N[C@@H](CCSC)C(=O)N[C@@H]([C@@H](C)O)C(O)=O GFEDXKNBZMPEDM-KZVJFYERSA-N 0.000 claims 1
IPWKGIFRRBGCJO-IMJSIDKUSA-N Ala-Ser Chemical compound C[C@H]([NH3+])C(=O)N[C@@H](CO)C([O-])=O IPWKGIFRRBGCJO-IMJSIDKUSA-N 0.000 claims 1
MMLHRUJLOUSRJX-CIUDSAMLSA-N Ala-Ser-Lys Chemical compound C[C@H](N)C(=O)N[C@@H](CO)C(=O)N[C@H](C(O)=O)CCCCN MMLHRUJLOUSRJX-CIUDSAMLSA-N 0.000 claims 1
LSMDIAAALJJLRO-XQXXSGGOSA-N Ala-Thr-Glu Chemical compound [H]N[C@@H](C)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CCC(O)=O)C(O)=O LSMDIAAALJJLRO-XQXXSGGOSA-N 0.000 claims 1
IYKVSFNGSWTTNZ-GUBZILKMSA-N Ala-Val-Arg Chemical compound C[C@H](N)C(=O)N[C@@H](C(C)C)C(=O)N[C@H](C(O)=O)CCCN=C(N)N IYKVSFNGSWTTNZ-GUBZILKMSA-N 0.000 claims 1
VHAQSYHSDKERBS-XPUUQOCRSA-N Ala-Val-Gly Chemical compound C[C@H](N)C(=O)N[C@@H](C(C)C)C(=O)NCC(O)=O VHAQSYHSDKERBS-XPUUQOCRSA-N 0.000 claims 1
IASNWHAGGYTEKX-IUCAKERBSA-N Arg-Arg-Gly Chemical compound NC(N)=NCCC[C@H](N)C(=O)N[C@@H](CCCN=C(N)N)C(=O)NCC(O)=O IASNWHAGGYTEKX-IUCAKERBSA-N 0.000 claims 1
NIUDXSFNLBIWOB-DCAQKATOSA-N Arg-Leu-Cys Chemical compound CC(C)C[C@@H](C(=O)N[C@@H](CS)C(=O)O)NC(=O)[C@H](CCCN=C(N)N)N NIUDXSFNLBIWOB-DCAQKATOSA-N 0.000 claims 1
NYDIVDKTULRINZ-AVGNSLFASA-N Arg-Met-Lys Chemical compound CSCC[C@@H](C(=O)N[C@@H](CCCCN)C(=O)O)NC(=O)[C@H](CCCN=C(N)N)N NYDIVDKTULRINZ-AVGNSLFASA-N 0.000 claims 1
KGCUOPPQTPZILL-CIUDSAMLSA-N Asn-Cys-His Chemical compound C1=C(NC=N1)C[C@@H](C(=O)O)NC(=O)[C@H](CS)NC(=O)[C@H](CC(=O)N)N KGCUOPPQTPZILL-CIUDSAMLSA-N 0.000 claims 1
IIFDPDVJAHQFSR-WHFBIAKZSA-N Asn-Glu Chemical compound NC(=O)C[C@H](N)C(=O)N[C@H](C(O)=O)CCC(O)=O IIFDPDVJAHQFSR-WHFBIAKZSA-N 0.000 claims 1
IICZCLFBILYRCU-WHFBIAKZSA-N Asn-Gly-Asp Chemical compound [H]N[C@@H](CC(N)=O)C(=O)NCC(=O)N[C@@H](CC(O)=O)C(O)=O IICZCLFBILYRCU-WHFBIAKZSA-N 0.000 claims 1
YUUIAUXBNOHFRJ-IHRRRGAJSA-N Asn-Phe-Met Chemical compound [H]N[C@@H](CC(N)=O)C(=O)N[C@@H](CC1=CC=CC=C1)C(=O)N[C@@H](CCSC)C(O)=O YUUIAUXBNOHFRJ-IHRRRGAJSA-N 0.000 claims 1
CJUKAWUWBZCTDQ-SRVKXCTJSA-N Asp-Leu-Lys Chemical compound OC(=O)C[C@H](N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCCN)C(O)=O CJUKAWUWBZCTDQ-SRVKXCTJSA-N 0.000 claims 1
YWLDTBBUHZJQHW-KKUMJFAQSA-N Asp-Lys-Phe Chemical compound C1=CC=C(C=C1)C[C@@H](C(=O)O)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC(=O)O)N YWLDTBBUHZJQHW-KKUMJFAQSA-N 0.000 claims 1
FIAKNCXQFFKSSI-ZLUOBGJFSA-N Asp-Ser-Cys Chemical compound OC(=O)C[C@H](N)C(=O)N[C@@H](CO)C(=O)N[C@@H](CS)C(O)=O FIAKNCXQFFKSSI-ZLUOBGJFSA-N 0.000 claims 1
OQMGSMNZVHYDTQ-ZKWXMUAHSA-N Asp-Val-Cys Chemical compound CC(C)[C@@H](C(=O)N[C@@H](CS)C(=O)O)NC(=O)[C@H](CC(=O)O)N OQMGSMNZVHYDTQ-ZKWXMUAHSA-N 0.000 claims 1
PRXCTTWKGJAPMT-ZLUOBGJFSA-N Cys-Ala-Ser Chemical compound [H]N[C@@H](CS)C(=O)N[C@@H](C)C(=O)N[C@@H](CO)C(O)=O PRXCTTWKGJAPMT-ZLUOBGJFSA-N 0.000 claims 1
LVNMAAGSAUGNIC-BQBZGAKWSA-N Cys-His Chemical compound SC[C@H](N)C(=O)N[C@H](C(O)=O)CC1=CNC=N1 LVNMAAGSAUGNIC-BQBZGAKWSA-N 0.000 claims 1
TXGDWPBLUFQODU-XGEHTFHBSA-N Cys-Pro-Thr Chemical compound [H]N[C@@H](CS)C(=O)N1CCC[C@H]1C(=O)N[C@@H]([C@@H](C)O)C(O)=O TXGDWPBLUFQODU-XGEHTFHBSA-N 0.000 claims 1
DGQJGBDBFVGLGL-ZKWXMUAHSA-N Cys-Val-Asp Chemical compound CC(C)[C@@H](C(=O)N[C@@H](CC(=O)O)C(=O)O)NC(=O)[C@H](CS)N DGQJGBDBFVGLGL-ZKWXMUAHSA-N 0.000 claims 1
OAGVHWYIBZMWLA-YFKPBYRVSA-N Glu-Gly-Gly Chemical compound OC(=O)CC[C@H](N)C(=O)NCC(=O)NCC(O)=O OAGVHWYIBZMWLA-YFKPBYRVSA-N 0.000 claims 1
DVLZZEPUNFEUBW-AVGNSLFASA-N Glu-His-Leu Chemical compound CC(C)C[C@@H](C(=O)O)NC(=O)[C@H](CC1=CN=CN1)NC(=O)[C@H](CCC(=O)O)N DVLZZEPUNFEUBW-AVGNSLFASA-N 0.000 claims 1
PMSMKNYRZCKVMC-DRZSPHRISA-N Glu-Phe-Ala Chemical compound C[C@@H](C(=O)O)NC(=O)[C@H](CC1=CC=CC=C1)NC(=O)[C@H](CCC(=O)O)N PMSMKNYRZCKVMC-DRZSPHRISA-N 0.000 claims 1
ZIYGTCDTJJCDDP-JYJNAYRXSA-N Glu-Phe-Lys Chemical compound C1=CC=C(C=C1)C[C@@H](C(=O)N[C@@H](CCCCN)C(=O)O)NC(=O)[C@H](CCC(=O)O)N ZIYGTCDTJJCDDP-JYJNAYRXSA-N 0.000 claims 1
NNQDRRUXFJYCCJ-NHCYSSNCSA-N Glu-Pro-Val Chemical compound [H]N[C@@H](CCC(O)=O)C(=O)N1CCC[C@H]1C(=O)N[C@@H](C(C)C)C(O)=O NNQDRRUXFJYCCJ-NHCYSSNCSA-N 0.000 claims 1
HHSKZJZWQFPSKN-AVGNSLFASA-N Glu-Tyr-Asp Chemical compound [H]N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC1=CC=C(O)C=C1)C(=O)N[C@@H](CC(O)=O)C(O)=O HHSKZJZWQFPSKN-AVGNSLFASA-N 0.000 claims 1
JLXVRFDTDUGQEE-YFKPBYRVSA-N Gly-Arg Chemical compound NCC(=O)N[C@H](C(O)=O)CCCN=C(N)N JLXVRFDTDUGQEE-YFKPBYRVSA-N 0.000 claims 1
KRRMJKMGWWXWDW-STQMWFEESA-N Gly-Arg-Phe Chemical compound NC(=N)NCCC[C@H](NC(=O)CN)C(=O)N[C@H](C(O)=O)CC1=CC=CC=C1 KRRMJKMGWWXWDW-STQMWFEESA-N 0.000 claims 1
JNGHLWWFPGIJER-STQMWFEESA-N Gly-Pro-Tyr Chemical compound NCC(=O)N1CCC[C@H]1C(=O)N[C@H](C(O)=O)CC1=CC=C(O)C=C1 JNGHLWWFPGIJER-STQMWFEESA-N 0.000 claims 1
TVTZEOHWHUVYCG-KYNKHSRBSA-N Gly-Thr-Thr Chemical compound [H]NCC(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H]([C@@H](C)O)C(O)=O TVTZEOHWHUVYCG-KYNKHSRBSA-N 0.000 claims 1
JBCLFWXMTIKCCB-UHFFFAOYSA-N H-Gly-Phe-OH Natural products NCC(=O)NC(C(O)=O)CC1=CC=CC=C1 JBCLFWXMTIKCCB-UHFFFAOYSA-N 0.000 claims 1
MVZASEMJYJPJSI-IHPCNDPISA-N His-Lys-Trp Chemical compound C1=CC=C2C(=C1)C(=CN2)C[C@@H](C(=O)O)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC3=CN=CN3)N MVZASEMJYJPJSI-IHPCNDPISA-N 0.000 claims 1
SVVULKPWDBIPCO-BZSNNMDCSA-N His-Phe-Leu Chemical compound [H]N[C@@H](CC1=CNC=N1)C(=O)N[C@@H](CC1=CC=CC=C1)C(=O)N[C@@H](CC(C)C)C(O)=O SVVULKPWDBIPCO-BZSNNMDCSA-N 0.000 claims 1
108010065920 Insulin Lispro Proteins 0.000 claims 1
FADYJNXDPBKVCA-UHFFFAOYSA-N L-Phenylalanyl-L-lysin Natural products NCCCCC(C(O)=O)NC(=O)C(N)CC1=CC=CC=C1 FADYJNXDPBKVCA-UHFFFAOYSA-N 0.000 claims 1
POJPZSMTTMLSTG-SRVKXCTJSA-N Leu-Asn-Lys Chemical compound CC(C)C[C@@H](C(=O)N[C@@H](CC(=O)N)C(=O)N[C@@H](CCCCN)C(=O)O)N POJPZSMTTMLSTG-SRVKXCTJSA-N 0.000 claims 1
YKNBJXOJTURHCU-DCAQKATOSA-N Leu-Asp-Arg Chemical compound CC(C)C[C@H](N)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@H](C(O)=O)CCCN=C(N)N YKNBJXOJTURHCU-DCAQKATOSA-N 0.000 claims 1
ZURHXHNAEJJRNU-CIUDSAMLSA-N Leu-Asp-Asn Chemical compound [H]N[C@@H](CC(C)C)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC(N)=O)C(O)=O ZURHXHNAEJJRNU-CIUDSAMLSA-N 0.000 claims 1
KWURTLAFFDOTEQ-GUBZILKMSA-N Leu-Cys-Glu Chemical compound CC(C)C[C@@H](C(=O)N[C@@H](CS)C(=O)N[C@@H](CCC(=O)O)C(=O)O)N KWURTLAFFDOTEQ-GUBZILKMSA-N 0.000 claims 1
PNUCWVAGVNLUMW-CIUDSAMLSA-N Leu-Cys-Ser Chemical compound [H]N[C@@H](CC(C)C)C(=O)N[C@@H](CS)C(=O)N[C@@H](CO)C(O)=O PNUCWVAGVNLUMW-CIUDSAMLSA-N 0.000 claims 1
DCGXHWINSHEPIR-SRVKXCTJSA-N Leu-Lys-Cys Chemical compound CC(C)C[C@@H](C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CS)C(=O)O)N DCGXHWINSHEPIR-SRVKXCTJSA-N 0.000 claims 1
BGZCJDGBBUUBHA-KKUMJFAQSA-N Leu-Lys-Leu Chemical compound CC(C)C[C@H](N)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(O)=O BGZCJDGBBUUBHA-KKUMJFAQSA-N 0.000 claims 1
ZDBMWELMUCLUPL-QEJZJMRPSA-N Leu-Phe-Ala Chemical compound CC(C)C[C@H](N)C(=O)N[C@H](C(=O)N[C@@H](C)C(O)=O)CC1=CC=CC=C1 ZDBMWELMUCLUPL-QEJZJMRPSA-N 0.000 claims 1
ADJWHHZETYAAAX-SRVKXCTJSA-N Leu-Ser-His Chemical compound CC(C)C[C@@H](C(=O)N[C@@H](CO)C(=O)N[C@@H](CC1=CN=CN1)C(=O)O)N ADJWHHZETYAAAX-SRVKXCTJSA-N 0.000 claims 1
JGKHAFUAPZCCDU-BZSNNMDCSA-N Leu-Tyr-Leu Chemical compound CC(C)C[C@H]([NH3+])C(=O)N[C@H](C(=O)N[C@@H](CC(C)C)C([O-])=O)CC1=CC=C(O)C=C1 JGKHAFUAPZCCDU-BZSNNMDCSA-N 0.000 claims 1
NLOZZWJNIKKYSC-WDSOQIARSA-N Lys-Arg-Trp Chemical compound C1=CC=C2C(C[C@H](NC(=O)[C@H](CCCN=C(N)N)NC(=O)[C@@H](N)CCCCN)C(O)=O)=CNC2=C1 NLOZZWJNIKKYSC-WDSOQIARSA-N 0.000 claims 1
HQVDJTYKCMIWJP-YUMQZZPRSA-N Lys-Asn-Gly Chemical compound [H]N[C@@H](CCCCN)C(=O)N[C@@H](CC(N)=O)C(=O)NCC(O)=O HQVDJTYKCMIWJP-YUMQZZPRSA-N 0.000 claims 1
MKBIVWXCFINCLE-SRVKXCTJSA-N Lys-Asn-His Chemical compound C1=C(NC=N1)C[C@@H](C(=O)O)NC(=O)[C@H](CC(=O)N)NC(=O)[C@H](CCCCN)N MKBIVWXCFINCLE-SRVKXCTJSA-N 0.000 claims 1
ZQCVMVCVPFYXHZ-SRVKXCTJSA-N Lys-Asn-Lys Chemical compound NCCCC[C@H](N)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@H](C(O)=O)CCCCN ZQCVMVCVPFYXHZ-SRVKXCTJSA-N 0.000 claims 1
ULUQBUKAPDUKOC-GVXVVHGQSA-N Lys-Glu-Val Chemical compound [H]N[C@@H](CCCCN)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](C(C)C)C(O)=O ULUQBUKAPDUKOC-GVXVVHGQSA-N 0.000 claims 1
LJADEBULDNKJNK-IHRRRGAJSA-N Lys-Leu-Val Chemical compound CC(C)C[C@H](NC(=O)[C@@H](N)CCCCN)C(=O)N[C@@H](C(C)C)C(O)=O LJADEBULDNKJNK-IHRRRGAJSA-N 0.000 claims 1
NVGBPTNZLWRQSY-UWVGGRQHSA-N Lys-Lys Chemical compound NCCCC[C@H](N)C(=O)N[C@H](C(O)=O)CCCCN NVGBPTNZLWRQSY-UWVGGRQHSA-N 0.000 claims 1
UQRZFMQQXXJTTF-AVGNSLFASA-N Lys-Lys-Glu Chemical compound [H]N[C@@H](CCCCN)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCC(O)=O)C(O)=O UQRZFMQQXXJTTF-AVGNSLFASA-N 0.000 claims 1
KJIXWRWPOCKYLD-IHRRRGAJSA-N Lys-Lys-Met Chemical compound CSCC[C@@H](C(=O)O)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCCCN)N KJIXWRWPOCKYLD-IHRRRGAJSA-N 0.000 claims 1
YXPJCVNIDDKGOE-MELADBBJSA-N Lys-Lys-Pro Chemical compound C1C[C@@H](N(C1)C(=O)[C@H](CCCCN)NC(=O)[C@H](CCCCN)N)C(=O)O YXPJCVNIDDKGOE-MELADBBJSA-N 0.000 claims 1
JMNRXRPBHFGXQX-GUBZILKMSA-N Lys-Ser-Glu Chemical compound NCCCC[C@H](N)C(=O)N[C@@H](CO)C(=O)N[C@H](C(O)=O)CCC(O)=O JMNRXRPBHFGXQX-GUBZILKMSA-N 0.000 claims 1
NYTDJEZBAAFLLG-IHRRRGAJSA-N Lys-Val-Lys Chemical compound NCCCC[C@H](N)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CCCCN)C(O)=O NYTDJEZBAAFLLG-IHRRRGAJSA-N 0.000 claims 1
241000829100 Macaca mulatta polyomavirus 1 Species 0.000 claims 1
KZNQNBZMBZJQJO-UHFFFAOYSA-N N-glycyl-L-proline Natural products NCC(=O)N1CCCC1C(O)=O KZNQNBZMBZJQJO-UHFFFAOYSA-N 0.000 claims 1
IWZRODDWOSIXPZ-IRXDYDNUSA-N Phe-Phe-Gly Chemical compound C([C@H](N)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)NCC(O)=O)C1=CC=CC=C1 IWZRODDWOSIXPZ-IRXDYDNUSA-N 0.000 claims 1
IPVPGAADZXRZSH-RNXOBYDBSA-N Phe-Tyr-Trp Chemical compound [H]N[C@@H](CC1=CC=CC=C1)C(=O)N[C@@H](CC1=CC=C(O)C=C1)C(=O)N[C@@H](CC1=CNC2=C1C=CC=C2)C(O)=O IPVPGAADZXRZSH-RNXOBYDBSA-N 0.000 claims 1
APKRGYLBSCWJJP-FXQIFTODSA-N Pro-Ala-Asp Chemical compound [H]N1CCC[C@H]1C(=O)N[C@@H](C)C(=O)N[C@@H](CC(O)=O)C(O)=O APKRGYLBSCWJJP-FXQIFTODSA-N 0.000 claims 1
JQOHKCDMINQZRV-WDSKDSINSA-N Pro-Asn Chemical compound NC(=O)C[C@@H](C([O-])=O)NC(=O)[C@@H]1CCC[NH2+]1 JQOHKCDMINQZRV-WDSKDSINSA-N 0.000 claims 1
QXNSKJLSLYCTMT-FXQIFTODSA-N Pro-Cys-Asp Chemical compound C1C[C@H](NC1)C(=O)N[C@@H](CS)C(=O)N[C@@H](CC(=O)O)C(=O)O QXNSKJLSLYCTMT-FXQIFTODSA-N 0.000 claims 1
NMELOOXSGDRBRU-YUMQZZPRSA-N Pro-Glu-Gly Chemical compound OC(=O)CNC(=O)[C@H](CCC(=O)O)NC(=O)[C@@H]1CCCN1 NMELOOXSGDRBRU-YUMQZZPRSA-N 0.000 claims 1
PTLOFJZJADCNCD-DCAQKATOSA-N Pro-Glu-Met Chemical compound CSCC[C@@H](C(=O)O)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@@H]1CCCN1 PTLOFJZJADCNCD-DCAQKATOSA-N 0.000 claims 1
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NZ529560A 1999-09-13 2000-09-13 Pharmaceutical compositions and methods of using secreted frizzled related protein NZ529560A (en)

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US39483299A	1999-09-13	1999-09-13

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NZ529560A NZ529560A (en)	1999-09-13	2000-09-13	Pharmaceutical compositions and methods of using secreted frizzled related protein

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EP (1)	EP1212355A2 (cs)
JP (1)	JP2003512304A (cs)
CN (2)	CN102988957A (cs)
AU (1)	AU7131200A (cs)
BR (1)	BR0014183A (cs)
CA (1)	CA2383360A1 (cs)
CZ (1)	CZ2002903A3 (cs)
IL (1)	IL148421A0 (cs)
MX (1)	MXPA02002624A (cs)
NZ (1)	NZ529560A (cs)
WO (1)	WO2001019855A2 (cs)

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Publication number	Priority date	Publication date	Assignee	Title
WO2001064949A2 (en)	2000-02-29	2001-09-07	Alcon Laboratories, Inc.	Diagnostics and therapeutics for glaucoma
US6600018B1 (en)	2000-04-10	2003-07-29	The United States Of America As Represented By The Department Of Health And Human Services	Secreted frizzled related protein, sFRP, fragments and methods of use thereof
EP1318840A2 (en) *	2000-07-19	2003-06-18	Genzyme Corporation	PHOSPHATONIN-RELATED GENE AND i METHODS OF USE THEREOF /i
ATE550345T1 (de) *	2001-01-10	2012-04-15	Us Health	Sfrp, mit sfrp-interagierende peptidmotive sowie verwendungsverfahren
EP1222933A1 (en) *	2001-01-15	2002-07-17	Academisch Ziekenhuis Leiden h.o.d.n., Leids Universitair Medisch Centrum	Generation and/or reduction of new lung tissue in an affected lung, by modulation of the Wnt-pathway
US20040265808A1 (en) *	2001-04-05	2004-12-30	Teresa Garcia	Genes involved in osteogenesis, and methods of use
US7713526B2 (en)	2001-05-01	2010-05-11	The Regents Of The University Of California	Wnt and frizzled receptors as targets for immunotherapy in head and neck squamous cell carcinomas
AU2002308557A1 (en)	2001-05-01	2002-11-11	The Regents Of The University Of California	Wnt and frizzled receptors as targets for immunotherapy in head and neck squamous cell carcinomas
GB0111004D0 (en) *	2001-05-04	2001-06-27	Univ Sheffield	Screening method
US20060281179A1 (en) *	2001-11-15	2006-12-14	Yoshiki Sasai	Inducer for differentiation of embryo stem cells into ectodermal cells method of obtaining the same and use thereof
CA2507496C (en) *	2002-12-05	2014-11-04	John D. Shaughnessy	Molecular determinants of myeloma bone disease and uses thereof
WO2004090161A1 (en) *	2003-04-14	2004-10-21	Novartis Ag	Gene expression associated with osteoblast differentiation
CN104726460A (zh) *	2013-12-22	2015-06-24	上海交通大学医学院	蛋白sFRP-5在治疗银屑病的药物中的应用
CN107073117A (zh) *	2014-08-26	2017-08-18	埃塔根有限公司	用于识别wls蛋白特定基序的抗体和含有其的药物组合物
EP3696192A1 (en) *	2019-02-15	2020-08-19	Consejo Superior De Investigaciones Científicas	Therapeutic target and monoclonal antibodies against it for the diagnosis and treatment of alzheimer´s disease
CN110361541A (zh) *	2019-07-23	2019-10-22	上海交通大学医学院附属瑞金医院	sFRP2和PCPE1作为联合靶点在制备纤维化疾病药物中的应用
CN114910454B (zh) *	2022-04-14	2025-06-13	中国人民解放军总医院第一医学中心	一种检测微重力条件下雄激素受体功能的方法
CN120714006A (zh) *	2025-07-11	2025-09-30	昆明理工大学	分泌型卷曲相关蛋白在制备关节炎治疗药物上的应用及关节炎治疗药物

Family Cites Families (4)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
US5681701A (en) *	1993-07-12	1997-10-28	Mayo Foundation For Medical Education And Research	Immortalized human fetal osteoblastic cells
DE69520360T2 (de) *	1994-07-04	2001-08-09	Takeda Chemical Industries, Ltd.	Phosphonsäure verbindungen imre herstellung und verwendung
AU4981797A (en) *	1996-10-11	1998-05-11	Government Of The United States Of America, The	Isolation and method of using tissue growth-inducing frzb protein
AU7704498A (en) *	1997-05-29	1998-12-30	Government Of The United States Of America, As Represented By The Secretary Of The Department Of Health And Human Services, The	Human frp and fragments thereof including methods for using them

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- 2000-09-13 MX MXPA02002624A patent/MXPA02002624A/es active IP Right Grant
- 2000-09-13 BR BR0014183-6A patent/BR0014183A/pt not_active IP Right Cessation
- 2000-09-13 WO PCT/US2000/025035 patent/WO2001019855A2/en not_active Ceased
- 2000-09-13 AU AU71312/00A patent/AU7131200A/en not_active Abandoned
- 2000-09-13 JP JP2001523632A patent/JP2003512304A/ja active Pending
- 2000-09-13 IL IL14842100A patent/IL148421A0/xx unknown
- 2000-09-13 NZ NZ529560A patent/NZ529560A/en not_active IP Right Cessation
- 2000-09-13 CZ CZ2002903A patent/CZ2002903A3/cs unknown
- 2000-09-13 CN CN200910208473XA patent/CN102988957A/zh active Pending
- 2000-09-13 CN CN00815431A patent/CN1387537A/zh active Pending
- 2000-09-13 EP EP00960097A patent/EP1212355A2/en not_active Withdrawn
- 2000-09-13 CA CA002383360A patent/CA2383360A1/en not_active Abandoned

Also Published As

Publication number	Publication date
CN102988957A (zh)	2013-03-27
AU7131200A (en)	2001-04-17
CA2383360A1 (en)	2001-03-22
WO2001019855A2 (en)	2001-03-22
WO2001019855A3 (en)	2002-01-24
CZ2002903A3 (cs)	2002-07-17
CN1387537A (zh)	2002-12-25
JP2003512304A (ja)	2003-04-02
MXPA02002624A (es)	2002-07-30
EP1212355A2 (en)	2002-06-12
IL148421A0 (en)	2002-09-12
BR0014183A (pt)	2002-05-14

Legal Events

Date	Code	Title
2004-07-30	RENW	Renewal (renewal fees accepted)
2005-09-30	PSEA	Patent sealed
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2010-07-30	RENW	Renewal (renewal fees accepted)
2014-03-28	LAPS	Patent lapsed

Publication	Publication Date	Title
NZ529560A (en)	2005-05-27	Pharmaceutical compositions and methods of using secreted frizzled related protein
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JP2003508088A (ja)	2003-03-04	５２個のヒト分泌タンパク質
US20090226463A1 (en)	2009-09-10	Novel method of modulating bone-related activity
US20110020348A1 (en)	2011-01-27	Pharmaceutical compositions and methods using secreted frizzled related protein
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US7098372B1 (en)	2006-08-29	Pharmaceutical compositions and methods of using secreted frizzled related protein
WO2006133457A2 (en)	2006-12-14	Bone morphogenetic variants, compositions and methods of treatment
WO2001062928A2 (en)	2001-08-30	Polypeptides and nucleic acids encoding same
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AU2005201918B2 (en)	2009-01-22	Pharmaceutical compositions and methods of using secreted frizzled related protein
JP2002528067A (ja)	2002-09-03	オステオプロテゲリン様タンパク質をコードする核酸およびその使用方法
CN101384619A (zh)	2009-03-11	骨形成的调节
JP2004514404A (ja)	2004-05-20	血管形成関連タンパク質及びこれをコードする核酸
JP2004527205A (ja)	2004-09-09	２９個のヒト分泌タンパク質
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JP2006525031A (ja)	2006-11-09	Ａｃｈｅｒｏｎ発現の制御方法
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