• ekstracelularni region • ekstracelularni prostor • ćelijska površina
Biološki proces
• negativna regulacija transkripcije od promotera RNK polimeraze II • aktivacija MAPK aktivnosti • razviće skeletalnog sistema
Pregled RNK izražavanja
podaci
Ortolozi
Vrsta
Čovek
Miš
Entrez
650
12156
Ensembl
ENSG00000125845
ENSMUSG00000027358
UniProt
P12643
P21274
Ref. Sekv. (iRNK)
NM_001200
NM_007553
Ref. Sekv. (protein)
NP_001191
NP_031579
Lokacija (UCSC)
Chr 20: 6.75 - 6.76 Mb
Chr 2: 133.55 - 133.56 Mb
PubMed pretraga
[1]
[2]
Koštani morfogenetički protein 2 ili BMP-2 pripada TGF-β superfamiliji proteina.[1]
Sadržaj
1Funkcija
2Interakcije
3Reference
4Literatura
5Vanjske veze
Funkcija
BMP-2 poput drugih koštano morfogenetičkih proteina,[2] ima važnu ulogu u razviću kostiju i hrskavice. On učestvuje u hedgehog putu, TGF beta signalnom putu, i interakciji citokina sa citokinskim receptorom. On takođe učestvuje u diferencijaciji srčanih ćelija i epitelijalno mesenhimalnoj tranziciji.
BMP-2 i BMP-7 su osteoinduktivni BMP: demonstrirano je da oni potentno indukuju osteoblastnu diferencijaciju u brojnim tipovima ćelija.[3]
Interakcije
Koštani morfogenetički protein 2 formira interakcije sa BMPR1A.[4][5][6][7]
Reference
↑Sampath TK, Coughlin JE, Whetstone RM, Banach D, Corbett C, Ridge RJ, Ozkaynak E, Oppermann H, Rueger DC (August 1990). „Bovine osteogenic protein is composed of dimers of OP-1 and BMP-2A, two members of the transforming growth factor-beta superfamily”. J. Biol. Chem.265 (22): 13198–205. PMID 2376592. Arhivirano iz originala na datum 2005-05-09. Pristupljeno 2014-06-29.
↑Chen D, Zhao M, Mundy GR (December 2004). „Bone morphogenetic proteins”. Growth Factors22 (4): 233–41. DOI:10.1080/08977190412331279890. PMID 15621726.
↑Marie PJ, Debiais F, Haÿ E (2002). „Regulation of human cranial osteoblast phenotype by FGF-2, FGFR-2 and BMP-2 signaling”. Histol. Histopathol.17 (3): 877–85. PMID 12168799.
↑Nickel J, Dreyer M K, Kirsch T, Sebald W (2001). „The crystal structure of the BMP-2:BMPR-IA complex and the generation of BMP-2 antagonists”. The Journal of bone and joint surgery. American volume83-A Suppl 1 (Pt 1): S7–14. PMID 11263668.
↑Kirsch T, Nickel J, Sebald W (February 2000). „Isolation of recombinant BMP receptor IA ectodomain and its 2:1 complex with BMP-2”. FEBS Lett.468 (2-3): 215–9. DOI:10.1016/S0014-5793(00)01214-X. PMID 10692589.
↑Kirsch T, Nickel J, Sebald W (July 2000). „BMP-2 antagonists emerge from alterations in the low-affinity binding epitope for receptor BMPR-II”. EMBO J.19 (13): 3314–24. DOI:10.1093/emboj/19.13.3314. PMC 313944. PMID 10880444.
↑Gilboa L, Nohe A, Geissendörfer T, Sebald W, Henis Y I, Knaus P (March 2000). „Bone morphogenetic protein receptor complexes on the surface of live cells: a new oligomerization mode for serine/threonine kinase receptors”. Mol. Biol. Cell11 (3): 1023–35. DOI:10.1091/mbc.11.3.1023. PMC 14828. PMID 10712517.
Literatura
Nickel J, Dreyer MK, Kirsch T, Sebald W (2001). „The crystal structure of the BMP-2:BMPR-IA complex and the generation of BMP-2 antagonists.”. The Journal of bone and joint surgery. American volume83-A Suppl 1 (Pt 1): S7–14. PMID 11263668.
Kawamura C, Kizaki M, Ikeda Y (2003). „Bone morphogenetic protein (BMP)-2 induces apoptosis in human myeloma cells.”. Leuk. Lymphoma43 (3): 635–9. DOI:10.1080/10428190290012182. PMID 12002771.
Marie PJ, Debiais F, Haÿ E (2003). „Regulation of human cranial osteoblast phenotype by FGF-2, FGFR-2 and BMP-2 signaling.”. Histol. Histopathol.17 (3): 877–85. PMID 12168799.
Vanjske veze
BMPedia - the Bone Morphogenetic Protein Wiki[mrtav link]