ADAM12
From Wikipedia, the free encyclopedia
|
ADAM metallopeptidase domain 12 (meltrin alpha)
|
||||||||||||||
| Identifiers | ||||||||||||||
| Symbol(s) | ADAM12; MCMP; MCMPMltna; MLTN; MLTNA | |||||||||||||
| External IDs | OMIM: 602714 MGI: 105378 HomoloGene: 74862 | |||||||||||||
|
||||||||||||||
| RNA expression pattern | ||||||||||||||
|
|
||||||||||||||
| Orthologs | ||||||||||||||
| Human | Mouse | |||||||||||||
| Entrez | 8038 | 11489 | ||||||||||||
| Ensembl | ENSG00000148848 | n/a | ||||||||||||
| Uniprot | O43184 | n/a | ||||||||||||
| Refseq | NM_003474 (mRNA) NP_003465 (protein) |
NM_007400 (mRNA) NP_031426 (protein) |
||||||||||||
| Location | Chr 10: 127.69 - 128.07 Mb | n/a | ||||||||||||
| Pubmed search | [1] | [2] | ||||||||||||
ADAM metallopeptidase domain 12 (meltrin alpha), also known as ADAM12, is a human gene.
This gene encodes a member of the ADAM (a disintegrin and metalloprotease) protein family. Members of this family are membrane-anchored proteins structurally related to snake venom disintegrins, and have been implicated in a variety of biological processes involving cell-cell and cell-matrix interactions, including fertilization, muscle development, and neurogenesis. This gene has two alternatively spliced transcripts: a shorter secreted form and a longer membrane-bound form. The shorter form is found to stimulate myogenesis.[1]
[edit] References
[edit] Further reading
- Yagami-Hiromasa T, Sato T, Kurisaki T, et al. (1995). "A metalloprotease-disintegrin participating in myoblast fusion.". Nature 377 (6550): 652–6. doi:. PMID 7566181.
- Gilpin BJ, Loechel F, Mattei MG, et al. (1998). "A novel, secreted form of human ADAM 12 (meltrin alpha) provokes myogenesis in vivo.". J. Biol. Chem. 273 (1): 157–66. PMID 9417060.
- Loechel F, Gilpin BJ, Engvall E, et al. (1998). "Human ADAM 12 (meltrin alpha) is an active metalloprotease.". J. Biol. Chem. 273 (27): 16993–7. PMID 9642263.
- Howard L, Nelson KK, Maciewicz RA, Blobel CP (1999). "Interaction of the metalloprotease disintegrins MDC9 and MDC15 with two SH3 domain-containing proteins, endophilin I and SH3PX1.". J. Biol. Chem. 274 (44): 31693–9. PMID 10531379.
- Galliano MF, Huet C, Frygelius J, et al. (2000). "Binding of ADAM12, a marker of skeletal muscle regeneration, to the muscle-specific actin-binding protein, alpha -actinin-2, is required for myoblast fusion.". J. Biol. Chem. 275 (18): 13933–9. PMID 10788519.
- Iba K, Albrechtsen R, Gilpin B, et al. (2000). "The cysteine-rich domain of human ADAM 12 supports cell adhesion through syndecans and triggers signaling events that lead to beta1 integrin-dependent cell spreading.". J. Cell Biol. 149 (5): 1143–56. PMID 10831617.
- Shi Z, Xu W, Loechel F, et al. (2000). "ADAM 12, a disintegrin metalloprotease, interacts with insulin-like growth factor-binding protein-3.". J. Biol. Chem. 275 (24): 18574–80. doi:. PMID 10849447.
- Eto K, Puzon-McLaughlin W, Sheppard D, et al. (2001). "RGD-independent binding of integrin alpha9beta1 to the ADAM-12 and -15 disintegrin domains mediates cell-cell interaction.". J. Biol. Chem. 275 (45): 34922–30. doi:. PMID 10944520.
- Loechel F, Fox JW, Murphy G, et al. (2001). "ADAM 12-S cleaves IGFBP-3 and IGFBP-5 and is inhibited by TIMP-3.". Biochem. Biophys. Res. Commun. 278 (3): 511–5. doi:. PMID 11095942.
- Suzuki A, Kadota N, Hara T, et al. (2000). "Meltrin alpha cytoplasmic domain interacts with SH3 domains of Src and Grb2 and is phosphorylated by v-Src.". Oncogene 19 (51): 5842–50. PMID 11127814.
- Kang Q, Cao Y, Zolkiewska A (2001). "Direct interaction between the cytoplasmic tail of ADAM 12 and the Src homology 3 domain of p85alpha activates phosphatidylinositol 3-kinase in C2C12 cells.". J. Biol. Chem. 276 (27): 24466–72. doi:. PMID 11313349.
- Kawaguchi N, Xu X, Tajima R, et al. (2002). "ADAM 12 protease induces adipogenesis in transgenic mice.". Am. J. Pathol. 160 (5): 1895–903. PMID 12000741.
- Cao Y, Kang Q, Zhao Z, Zolkiewska A (2002). "Intracellular processing of metalloprotease disintegrin ADAM12.". J. Biol. Chem. 277 (29): 26403–11. doi:. PMID 12000744.
- 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:. PMID 12477932.
- Abram CL, Seals DF, Pass I, et al. (2003). "The adaptor protein fish associates with members of the ADAMs family and localizes to podosomes of Src-transformed cells.". J. Biol. Chem. 278 (19): 16844–51. doi:. PMID 12615925.
- Le Pabic H, Bonnier D, Wewer UM, et al. (2003). "ADAM12 in human liver cancers: TGF-beta-regulated expression in stellate cells is associated with matrix remodeling.". Hepatology 37 (5): 1056–66. doi:. PMID 12717386.
- Kawaguchi N, Sundberg C, Kveiborg M, et al. (2004). "ADAM12 induces actin cytoskeleton and extracellular matrix reorganization during early adipocyte differentiation by regulating beta1 integrin function.". J. Cell. Sci. 116 (Pt 19): 3893–904. doi:. PMID 12915587.
- Mori S, Tanaka M, Nanba D, et al. (2003). "PACSIN3 binds ADAM12/meltrin alpha and up-regulates ectodomain shedding of heparin-binding epidermal growth factor-like growth factor.". J. Biol. Chem. 278 (46): 46029–34. doi:. PMID 12952982.
- Clark HF, Gurney AL, Abaya E, et al. (2003). "The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment.". Genome Res. 13 (10): 2265–70. doi:. PMID 12975309.
- Laigaard J, Sørensen T, Fröhlich C, et al. (2004). "ADAM12: a novel first-trimester maternal serum marker for Down syndrome.". Prenat. Diagn. 23 (13): 1086–91. doi:. PMID 14691998.
 |
This article on a gene on chromosome 10 is a stub. You can help Wikipedia by expanding it. |
|
|||||||||||
