Koštani morfogenetički protein 2

BMP2
Available structures
PDB	Pretraga ortologa: PDBe RCSB
List of PDB id codes
	1ES7, 1REU, 1REW, 2GOO, 2H62, 2H64, 2QJ9, 2QJA, 2QJB, 3BK3, 3BMP, 4MID, 4N1D, 4UHY, 4UHZ, 4UI0, 4UI1, 4UI2
Identifikatori
Alijasi	BMP2
Spoljašnji ID	OMIM: 112261 MGI: 88177 HomoloGene: 926 GeneCards: BMP2
Genska lokacija (miš)
Hr.	Chromosome 2 (mouse)
Kraj	133,404,805 bp
Obrazac RNK izražavanja
	; ;
	More reference expression data
Genska ontologija
Molecular function	• везивања рецептора; • активност цитокина; • co-receptor binding; • phosphatase activator activity; • активност фактора раста; • BMP receptor binding; • GO:0001948, GO:0016582 везивање за протеине плазме; • NAD-retinol dehydrogenase activity; • SMAD binding; • protein heterodimerization activity; • transforming growth factor beta receptor binding;
Cellular component	• ванћелијска област; • површина ћелије; • BMP receptor complex; • ванћелијски простор; • intracellular membrane-bounded organelle;
Biological process	• skeletal system development; • positive regulation of Wnt signaling pathway by BMP signaling pathway; • positive regulation of protein phosphorylation; • mesenchyme development; • negative regulation of cell cycle; • odontogenesis of dentin-containing tooth; • telencephalon regionalization; • protein phosphorylation; • atrioventricular valve morphogenesis; • proteoglycan metabolic process; • mesenchymal cell differentiation; • pericardium development; • positive regulation of ERK1 and ERK2 cascade; • BMP signaling pathway involved in heart induction; • animal organ morphogenesis; • inner ear development; • cardiocyte differentiation; • negative regulation of canonical Wnt signaling pathway; • negative regulation of cell population proliferation; • positive regulation of p38MAPK cascade; • pathway-restricted SMAD protein phosphorylation; • cell fate commitment; • GO:0009373 regulation of transcription, DNA-templated; • SMAD protein signal transduction; • ossification; • in utero embryonic development; • mesenchymal cell proliferation involved in ureteric bud development; • regulation of odontogenesis of dentin-containing tooth; • GO:0060469, GO:0009371 positive regulation of transcription, DNA-templated; • positive regulation of Wnt signaling pathway; • heart development; • telencephalon development; • branching involved in ureteric bud morphogenesis; • negative regulation of Wnt signaling pathway involved in heart development; • cartilage development; • bone mineralization involved in bone maturation; • positive regulation of cartilage development; • positive regulation of neuron differentiation; • positive regulation of cell differentiation; • thyroid-stimulating hormone-secreting cell differentiation; • запаљенска реакција; • positive regulation of fat cell differentiation; • negative regulation of steroid biosynthetic process; • positive regulation of MAPK cascade; • Notch signaling pathway; • bone mineralization; • диференцијација; • chondrocyte differentiation; • corticotropin hormone secreting cell differentiation; • positive regulation of astrocyte differentiation; • positive regulation of bone mineralization; • GO:1904579 cellular response to organic cyclic compound; • positive regulation of ossification; • GO:1901227 negative regulation of transcription by RNA polymerase II; • positive regulation of epithelial to mesenchymal transition; • positive regulation of phosphatase activity; • negative regulation of calcium-independent cell-cell adhesion; • positive regulation of osteoblast differentiation; • protein destabilization; • embryonic heart tube anterior/posterior pattern specification; • osteoblast differentiation; • epithelial to mesenchymal transition; • positive regulation of protein binding; • GO:0045996 negative regulation of transcription, DNA-templated; • positive regulation of odontogenesis; • GO:0007329 positive regulation of transcription from RNA polymerase II promoter involved in cellular response to chemical stimulus; • negative regulation of aldosterone biosynthetic process; • positive regulation of osteoblast proliferation; • реакција на хипоксију; • positive regulation of endothelial cell proliferation; • positive regulation of cell migration; • negative regulation of cortisol biosynthetic process; • cell-cell signaling; • positive regulation of pathway-restricted SMAD protein phosphorylation; • cellular response to growth factor stimulus; • cellular response to BMP stimulus; • cardiac muscle tissue morphogenesis; • endocardial cushion morphogenesis; • multicellular organism development; • negative regulation of cardiac muscle cell differentiation; • positive regulation of apoptotic process; • negative regulation of insulin-like growth factor receptor signaling pathway; • GO:0003257, GO:0010735, GO:1901228, GO:1900622, GO:1904488 positive regulation of transcription by RNA polymerase II; • cardiac epithelial to mesenchymal transition; • positive regulation of pri-miRNA transcription by RNA polymerase II; • GO:1901313 positive regulation of gene expression; • BMP signaling pathway; • cardiac muscle cell differentiation; • cell development; • regulation of signaling receptor activity; • negative regulation of gene expression; • response to bacterium; • regulation of apoptotic process; • regulation of MAPK cascade;
	Sources:Amigo / QuickGO
Ortolozi
	650
	12156
	ENSG00000125845
	ENSMUSG00000027358
	P12643
	P21274
	NM_001200
	NM_007553
	NP_001191
	NP_031579
	Wikidata
View/Edit Human	View/Edit Mouse

Koštani morfogenetički protein 2 ili BMP-2 pripada TGF-β superfamiliji proteina.^[4]

Funkcija

BMP-2 poput drugih koštano morfogenetičkih proteina,^[5] 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.^[6]

Interakcije

Koštani morfogenetički protein 2 formira interakcije sa BMPR1A.^[7]^[8]^[9]^[10]

Reference

^ ^а ^б ^в GRCm38: Ensembl release 89: ENSMUSG00000027358 - Ensembl, May 2017
^ „Human PubMed Reference:”. National Center for Biotechnology Information, U.S. National Library of Medicine.
^ „Mouse PubMed Reference:”. National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Sampath TK, Coughlin JE, Whetstone RM, Banach D, Corbett C, Ridge RJ, Ozkaynak E, Oppermann H, Rueger DC (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. Архивирано из оригинала 09. 05. 2005. г. Приступљено 21. 12. 2016.
^ Chen D, Zhao M, Mundy GR (2004). „Bone morphogenetic proteins”. Growth Factors. 22 (4): 233—41. PMID 15621726. doi:10.1080/08977190412331279890.
^ 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 MK, Kirsch T, Sebald W (2001). „The crystal structure of the BMP-2:BMPR-IA complex and the generation of BMP-2 antagonists”. J Bone Joint Surg Am. 83-A Suppl 1 (Pt 1): S7—14. PMID 11263668.
^ Kirsch T, Nickel J, Sebald W (2000). „Isolation of recombinant BMP receptor IA ectodomain and its 2:1 complex with BMP-2”. FEBS Lett. 468 (2-3): 215—9. PMID 10692589. doi:10.1016/S0014-5793(00)01214-X.
^ Kirsch T, Nickel J, Sebald W (2000). „BMP-2 antagonists emerge from alterations in the low-affinity binding epitope for receptor BMPR-II”. EMBO J. 19 (13): 3314—24. PMC 313944 . PMID 10880444. doi:10.1093/emboj/19.13.3314.
^ Gilboa L, Nohe A, Geissendörfer T, Sebald W, Henis YI, Knaus P (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. PMC 14828 . PMID 10712517. doi:10.1091/mbc.11.3.1023.

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”. J Bone Joint Surg Am. 83-A Suppl 1 (Pt 1): S7—14. PMID 11263668.
Kawamura C, Kizaki M, Ikeda Y (2002). „Bone morphogenetic protein (BMP)-2 induces apoptosis in human myeloma cells”. Leuk. Lymphoma. 43 (3): 635—9. PMID 12002771. doi:10.1080/10428190290012182.
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.

Spoljašnje veze

bone morphogenetic protein 2 на US National Library of Medicine Medical Subject Headings (MeSH)

[refGRCm38Ensembl-1] а ^б ^в GRCm38: Ensembl release 89: ENSMUSG00000027358 - Ensembl, May 2017

[2] „Human PubMed Reference:”. National Center for Biotechnology Information, U.S. National Library of Medicine.

[3] „Mouse PubMed Reference:”. National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid2376592-4] Sampath TK, Coughlin JE, Whetstone RM, Banach D, Corbett C, Ridge RJ, Ozkaynak E, Oppermann H, Rueger DC (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. Архивирано из оригинала 09. 05. 2005. г. Приступљено 21. 12. 2016.

[pmid15621726-5] Chen D, Zhao M, Mundy GR (2004). „Bone morphogenetic proteins”. Growth Factors. 22 (4): 233—41. PMID 15621726. doi:10.1080/08977190412331279890.

[pmid12168799-6] 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.

[pmid11263668-7] 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”. J Bone Joint Surg Am. 83-A Suppl 1 (Pt 1): S7—14. PMID 11263668.

[pmid10692589-8] Kirsch T, Nickel J, Sebald W (2000). „Isolation of recombinant BMP receptor IA ectodomain and its 2:1 complex with BMP-2”. FEBS Lett. 468 (2-3): 215—9. PMID 10692589. doi:10.1016/S0014-5793(00)01214-X.

[pmid10880444-9] Kirsch T, Nickel J, Sebald W (2000). „BMP-2 antagonists emerge from alterations in the low-affinity binding epitope for receptor BMPR-II”. EMBO J. 19 (13): 3314—24. PMC 313944 . PMID 10880444. doi:10.1093/emboj/19.13.3314.

[pmid10712517-10] Gilboa L, Nohe A, Geissendörfer T, Sebald W, Henis YI, Knaus P (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. PMC 14828 . PMID 10712517. doi:10.1091/mbc.11.3.1023.

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