Koštani morfogenetički protein 2

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Koštani morfogenetički protein 2

PDB prikaz baziran na 3bmp.
Dostupne strukture
1ES7, 1REU, 1REW, 2GOO, 2H62, 2H64, 2QJ9, 2QJA, 2QJB, 3BK3, 3BMP
Identifikatori
SimboliBMP2; BDA2; BMP2A
Vanjski IDOMIM112261 MGI88177 HomoloGene926 GeneCards: BMP2 Gene
Pregled RNK izražavanja
podaci
Ortolozi
VrstaČovekMiš
Entrez65012156
EnsemblENSG00000125845ENSMUSG00000027358
UniProtP12643P21274
Ref. Sekv. (iRNK)NM_001200NM_007553
Ref. Sekv. (protein)NP_001191NP_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]

Funkcija

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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

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Koštani morfogenetički protein 2 formira interakcije sa BMPR1A.[4][5][6][7]

Reference

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  1. 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. 
  2. Chen D, Zhao M, Mundy GR (December 2004). „Bone morphogenetic proteins”. Growth Factors 22 (4): 233–41. DOI:10.1080/08977190412331279890. PMID 15621726. 
  3. 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. 
  4. 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 volume 83-A Suppl 1 (Pt 1): S7–14. PMID 11263668. 
  5. 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. 
  6. 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. 
  7. 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. Cell 11 (3): 1023–35. DOI:10.1091/mbc.11.3.1023. PMC 14828. PMID 10712517. 

Literatura

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  • 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 volume 83-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. Lymphoma 43 (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

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