A Disintegrin And Metalloprotease 12 (ADAM12)

MCMP; MCMPMltna; MLTN; MLTNA; Meltrin Alpha; Disintegrin and metalloproteinase domain-containing protein 12

SPN	N490
HGNC	190
MGI	105378
PubMed	18342566
RGD	1583652
UniProt	O43184
Wiki	ADAM12

ADAM12 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. Similarly to myogenin, a marker of early muscle differentiation, mouse meltrin-alpha is expressed in neonatal muscle and bone, and its expression increases dramatically in response to the induction of differentiation. Immunocytochemical localization and functional expression studies suggested that meltrin-alpha may be involved in myotube formation.

Reference

"A novel, secreted form of human ADAM 12 (meltrin alpha) provokes myogenesis in vivo."
J. Biol. Chem. 273:157-166(1998) [PubMed] [Europe PMC] [Abstract]

"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract]

"The DNA sequence and comparative analysis of human chromosome 10."
Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]

"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]

"Human ADAM 12 (meltrin alpha) is an active metalloprotease."
J. Biol. Chem. 273:16993-16997(1998) [PubMed] [Europe PMC] [Abstract]

"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. 149:1143-1156(2000) [PubMed] [Europe PMC] [Abstract]

"The adaptor protein fish associates with members of the ADAMs family and localizes to podosomes of Src-transformed cells."
J. Biol. Chem. 278:16844-16851(2003) [PubMed] [Europe PMC] [Abstract]

"FLRG, a new ADAM12-associated protein, modulates osteoclast differentiation."
Biol. Cell 97:577-588(2005) [PubMed] [Europe PMC] [Abstract]

"RACK1, a new ADAM12 interacting protein. Contribution to liver fibrogenesis."
J. Biol. Chem. 283:26000-26009(2008) [PubMed] [Europe PMC] [Abstract]

"The consensus coding sequences of human breast and colorectal cancers."
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]

"Analysis of the disintegrin-metalloproteinases family reveals ADAM29 and ADAM7 are often mutated in melanoma."
Hum. Mutat. 32:E2148-E2175(2011) [PubMed] [Europe PMC] [Abstract]