bone morphogenetic protein 1

• 骨形成タンパク質1

関

BMP-1

WordNet

1. remove the bones from; "bone the turkey before roasting it" (同)debone
2. the porous calcified substance from which bones are made (同)osseous_tissue
3. consisting of or made up of bone; "a bony substance"; "the bony framework of the body"
4. a shade of white the color of bleached bones (同)ivory, pearl, off-white
5. rigid connective tissue that makes up the skeleton of vertebrates (同)os
6. any of a large group of nitrogenous organic compounds that are essential constituents of living cells; consist of polymers of amino acids; essential in the diet of animals for growth and for repair of tissues; can be obtained from meat and eggs and milk and legumes; "a diet high in protein"
7. having bones as specified; "his lanky long-boned body"
8. having had the bones removed; "a boneless rib roast"; "a boned (or deboned) fish" (同)deboned
9. a percussion instrument consisting of a pair of hollow pieces of wood or bone (usually held between the thumb and fingers) that are made to click together (as by Spanish dancers) in rhythm with the dance (同)castanets, clappers, finger cymbals

PrepTutorEJDIC

1. 〈C〉骨 / 〈U〉骨を作っている物質,骨質 / 《複数形で》骨格;死骸(がい) / 〈魚など〉‘の'骨を取る
2. 蛋白(たんばく)質
3. (魚など)骨を取り除いた / (衣服が)(コルセットなどで)骨で張りをつけた[ような]

Wikipedia preview

出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2016/02/22 22:46:41」(JST)

wiki en

[Wiki en表示]

Bone morphogenetic protein 1
PDB rendering based on 3edg.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 3EDG​, 3EDH​
Identifiers
Symbols	BMP1 ; OI13; PCOLC; PCP; PCP2; TLD
External IDs	OMIM: 112264 MGI: 88176 HomoloGene: 55955 ChEMBL: 3898 GeneCards: BMP1 Gene
EC number	3.4.24.19
Gene ontology Molecular function • metalloendopeptidase activity • cytokine activity • calcium ion binding • protein binding • growth factor activity • peptidase activity • metallopeptidase activity • zinc ion binding Cellular component • extracellular region • proteinaceous extracellular matrix • extracellular space • Golgi apparatus • membrane-bounded vesicle Biological process • skeletal system development • cartilage condensation • ossification • proteolysis • multicellular organismal development • extracellular matrix disassembly • cell differentiation • extracellular matrix organization • lipoprotein metabolic process • small molecule metabolic process • positive regulation of cartilage development Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	649	12153
Ensembl	ENSG00000168487	ENSMUSG00000022098
UniProt	P13497	P98063
RefSeq (mRNA)	NM_001199	NM_009755
RefSeq (protein)	NP_001190	NP_033885
Location (UCSC)	Chr 8: 22.16 – 22.21 Mb	Chr 14: 70.47 – 70.52 Mb
PubMed search	[1]	[2]

Bone morphogenetic protein 1, also known as BMP1, is a protein which in humans is encoded by the BMP1 gene. There are seven isoforms of the protein created by alternate splicing.

Function

BMP1 belongs to the peptidase M12A family of bone morphogenetic proteins (BMPs). It induces bone and cartilage development. Unlike other BMPs, it does not belong to the TGFβ superfamily. It was initially discovered to work like other BMPs by inducing bone and cartilage development. It however, is a metalloprotease that cleaves the C-terminus of procollagen I, II and III. It has an astacin-like protease domain.

It has been shown to cleave laminin 5 and is localized in the basal epithelial layer of bovine skin.

The BMP1 locus encodes a protein that is capable of inducing formation of cartilage in vivo. Although other bone morphogenetic proteins are members of the TGF-beta superfamily, BMP1 encodes a protein that is not closely related to other known growth factors. BMP1 protein and procollagen C proteinase (PCP), a secreted metalloprotease requiring calcium and needed for cartilage and bone formation, are identical. PCP or BMP1 protein cleaves the C-terminal propeptides of procollagen I, II, and III and its activity is increased by the procollagen C-endopeptidase enhancer protein. The BMP1 gene is expressed as alternatively spliced variants that share an N-terminal protease domain but differ in their C-terminal region

Structure

The structure of BMP1 was determined through X-Ray diffraction with a resolution of 1.27 Å. Crystallization experiments were done by vapor diffusion at a pH of 7.5. This is important because it is close to the pH of the human body, where BMP1 resides in vivo. BMP1 is 202 residues in length. Its secondary structure is made up of 30% helices, or 10 helices, 61 residues in length, and 15% beta sheets, or 11 strands, 32 residues in length. It contains ligands of an acetyl group and a Zinc ion.

A Ramachandran plot was constructed for BMP. This plot shows that BMP1 most prefers Phi and Psi angles (Phi, Psi) of around (-60°,-45°) and (-60°, 140°). These preferred angles are an estimate of the most clustered data of the Ramachandran plot. The preferred region is much greater in range. 97% of the residues were in preferred regions and 100% of the residues were in the allowed region, with no outliers.

References

Further reading

• Tabas JA, Zasloff M, Wasmuth JJ; et al. (1991). "Bone morphogenetic protein: chromosomal localization of human genes for BMP1, BMP2A, and BMP3.". Genomics 9 (2): 283–9. doi:10.1016/0888-7543(91)90254-C. PMID 2004778. 
• Wozney JM, Rosen V, Celeste AJ; et al. (1989). "Novel regulators of bone formation: molecular clones and activities.". Science 242 (4885): 1528–34. doi:10.1126/science.3201241. PMID 3201241. 
• Takahara K, Lyons GE, Greenspan DS (1995). "Bone morphogenetic protein-1 and a mammalian tolloid homologue (mTld) are encoded by alternatively spliced transcripts which are differentially expressed in some tissues.". J. Biol. Chem. 269 (51): 32572–8. PMID 7798260. 
• Yoshiura K, Tamura T, Hong HS; et al. (1993). "Mapping of the bone morphogenetic protein 1 gene (BMP1) to 8p21: removal of BMP1 from candidacy for the bone disorder in Langer-Giedion syndrome.". Cytogenet. Cell Genet. 64 (3–4): 208–9. doi:10.1159/000133577. PMID 8404039. 
• Takahara K, Lee S, Wood S, Greenspan DS (1996). "Structural organization and genetic localization of the human bone morphogenetic protein 1/mammalian tolloid gene". Genomics 29 (1): 9–15. doi:10.1006/geno.1995.1209. PMID 8530106. 
• Kessler E, Takahara K, Biniaminov L; et al. (1996). "Bone morphogenetic protein-1: the type I procollagen C-proteinase". Science 271 (5247): 360–2. doi:10.1126/science.271.5247.360. PMID 8553073. 
• Li SW, Sieron AL, Fertala A; et al. (1996). "The C-proteinase that processes procollagens to fibrillar collagens is identical to the protein previously identified as bone morphogenic protein-1". Proc. Natl. Acad. Sci. U.S.A. 93 (10): 5127–30. doi:10.1073/pnas.93.10.5127. PMC 39418. PMID 8643539. 
• Janitz M, Heiser V, Böttcher U; et al. (1998). "Three alternatively spliced variants of the gene coding for the human bone morphogenetic protein-1". J. Mol. Med. 76 (2): 141–6. doi:10.1007/s001090050202. PMID 9500680. 
• Scott IC, Blitz IL, Pappano WN; et al. (1999). "Mammalian BMP-1/Tolloid-related metalloproteinases, including novel family member mammalian Tolloid-like 2, have differential enzymatic activities and distributions of expression relevant to patterning and skeletogenesis". Dev. Biol. 213 (2): 283–300. doi:10.1006/dbio.1999.9383. PMID 10479448. 
• Amano S, Scott IC, Takahara K; et al. (2000). "Bone morphogenetic protein 1 is an extracellular processing enzyme of the laminin 5 gamma 2 chain". J. Biol. Chem. 275 (30): 22728–35. doi:10.1074/jbc.M002345200. PMID 10806203. 
• Scott IC, Blitz IL, Pappano WN; et al. (2001). "Homologues of Twisted gastrulation are extracellular cofactors in antagonism of BMP signalling". Nature 410 (6827): 475–8. doi:10.1038/35068572. PMID 11260715. 
• Garrigue-Antar L, Barker C, Kadler KE (2001). "Identification of amino acid residues in bone morphogenetic protein-1 important for procollagen C-proteinase activity". J. Biol. Chem. 276 (28): 26237–42. doi:10.1074/jbc.M010814200. PMID 11283002. 
• Unsöld C, Pappano WN, Imamura Y; et al. (2002). "Biosynthetic processing of the pro-alpha 1(V)2pro-alpha 2(V) collagen heterotrimer by bone morphogenetic protein-1 and furin-like proprotein convertases". J. Biol. Chem. 277 (7): 5596–602. doi:10.1074/jbc.M110003200. PMID 11741999. 
• Rattenholl A, Pappano WN, Koch M; et al. (2002). "Proteinases of the bone morphogenetic protein-1 family convert procollagen VII to mature anchoring fibril collagen". J. Biol. Chem. 277 (29): 26372–8. doi:10.1074/jbc.M203247200. PMID 11986329. 
• Garrigue-Antar L, Hartigan N, Kadler KE (2003). "Post-translational modification of bone morphogenetic protein-1 is required for secretion and stability of the protein". J. Biol. Chem. 277 (45): 43327–34. doi:10.1074/jbc.M207342200. PMID 12218058. 
• Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. 
• Hartigan N, Garrigue-Antar L, Kadler KE (2003). "Bone morphogenetic protein-1 (BMP-1). Identification of the minimal domain structure for procollagen C-proteinase activity". J. Biol. Chem. 278 (20): 18045–9. doi:10.1074/jbc.M211448200. PMID 12637537. 
• Leighton M, Kadler KE (2003). "Paired basic/Furin-like proprotein convertase cleavage of Pro-BMP-1 in the trans-Golgi network". J. Biol. Chem. 278 (20): 18478–84. doi:10.1074/jbc.M213021200. PMID 12637569. 
• Ota T, Suzuki Y, Nishikawa T; et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039. 
• Hillman RT, Green RE, Brenner SE (2005). "An unappreciated role for RNA surveillance". Genome Biol. 5 (2): R8. doi:10.1186/gb-2004-5-2-r8. PMC 395752. PMID 14759258. 

External links

• The MEROPS online database for peptidases and their inhibitors: M12.005

External links

• bone morphogenetic protein 1 at the US National Library of Medicine Medical Subject Headings (MeSH)

UpToDate Contents

全文を閲覧するには購読必要です。 To read the full text you will need to subscribe.

• 1. 骨格の正常な発達および骨形成ならびに骨吸収の調節 normal skeletal development and regulation of bone formation and resorption
• 2. Conservative management of end-stage renal disease
• 3. 骨転移の機序 mechanisms of bone metastases
• 4. 鉄のバランス調節 regulation of iron balance
• 5. 小児および思春期における良性骨腫瘍：概要 benign bone tumors in children and adolescents an overview

English Journal

• Sizzled Is Unique among Secreted Frizzled-related Proteins for Its Ability to Specifically Inhibit Bone Morphogenetic Protein-1 (BMP-1)/Tolloid-like Proteinases.

• Bijakowski C, Vadon-Le Goff S, Delolme F, Bourhis JM, Lécorché P, Ruggiero F, Becker-Pauly C, Yiallouros I, Stöcker W, Dive V, Hulmes DJ, Moali C.SourceFrom the Institut de Biologie et Chimie des Protéines, CNRS/Université de Lyon FRE3310/FR3302, 69367 Lyon cedex 7, France.
• The Journal of biological chemistry.J Biol Chem.2012 Sep 28;287(40):33581-93. Epub 2012 Jul 23.
• BMP-1/tolloid-like proteinases (BTPs) are major enzymes involved in extracellular matrix assembly and activation of bioactive molecules, both growth factors and anti-angiogenic molecules. Although the control of BTP activity by several enhancing molecules is well established, the possibility that re
• PMID 22825851

• Tissue regulation of somitic colloid-like1 gene expression.

• Pais de Azevedo T, Zuzarte-Luís V, Gonçalves L, Marques C, Palmeirim I.SourceInstitute for Biotechnology and Bioengineering, Centro de Biomedicina Molecular e Estrutural, Universidade do Algarve, 8005-139 Faro, Portugal.
• Biochemical and biophysical research communications.Biochem Biophys Res Commun.2012 Jul 27;424(2):295-300. doi: 10.1016/j.bbrc.2012.06.110. Epub 2012 Jun 27.
• Body skeletal muscles formation starts with somite differentiation, due to signals from surrounding tissues. Somite ventral portion forms the sclerotome while its dorsal fraction constitutes the dermamyotome, and later the dermatome and myotome. Relative levels of BMP activity have been proposed to
• PMID 22749996

Japanese Journal

• Mutations in Bone Morphogenetic Protein Receptor Genes in Pulmonary Arterial Hypertension Patients : Possible Involvement of BMPRIB

• SHIRAISHI Isao
• Circulation journal : official journal of the Japanese Circulation Society 76(6), 1329-1330, 2012-05-25
• NAID 10030315891

• Distinct mechanisms control the timing of differentiation of two myeloid populations in Xenopus ventral blood islands

• MAENO Mitsugu,KOMIYAMA Kyogo,MATSUZAKI Yoko,HOSOYA Junichi,KURIHARA Sayaka,SAKATA Hiroyuki,IZUTSU Yumi
• Development, growth & differentiation 54(2), 187-201, 2012-02-01
• NAID 10030405616

Related Links

• OMIM Entry - * 112264 - BONE MORPHOGENETIC PROTEIN ...

112264 - BONE MORPHOGENETIC PROTEIN 1; BMP1 - TOLLOID, DROSOPHILA, HOMOLOG OF; TLD;; PROCOLLAGEN C-PROTEINASE - BMP1 ... 1. Amano, S., Scott, I. C., Takahara, K., Koch, M., Champliaud, M.-F ...

• Bone morphogenetic proteinとは - goo Wikipedia (ウィキペディア)

Bone morphogenetic proteins (BMPs) are a group of growth factors also known as cytokines and as metabologens. [1] Originally discovered by their ability to induce the formation of bone and cartilage, BMPs are now considered to ...

Related Pictures

---

★リンクテーブル★

リンク元	「BMP-1」「骨形成タンパク質1」
関連記事	「bone morphogenetic」「morphogenetic」「bone」

「BMP-1」

　　[★]

• 骨形成タンパク質1

関

bone morphogenetic protein 1

「骨形成タンパク質1」

　　[★]

英

bone morphogenetic protein 1、BMP-1

「bone morphogenetic」

　　[★]

• 骨形成の

関

bone formation、ossification、osteogenesis、osteogenic、osteoplastic

「morphogenetic」

　　[★]

• 形態形成の、形態発生の

関

morphogenesis、morphogenic、morphosis

「bone」

　　[★] 骨