ADAM12

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For the television show, see Adam 12

ADAM metallopeptidase domain 12
Identifiers
Symbols ADAM12 ; ADAM12-OT1; CAR10; MCMP; MCMPMltna; MLTN; MLTNA
External IDs OMIM602714 MGI105378 HomoloGene74862 ChEMBL: 5030 GeneCards: ADAM12 Gene
RNA expression pattern
PBB GE ADAM12 204943 at tn.png
PBB GE ADAM12 202952 s at tn.png
PBB GE ADAM12 213790 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 8038 11489
Ensembl ENSG00000148848 ENSMUSG00000054555
UniProt O43184 Q61824
RefSeq (mRNA) NM_001288973 NM_007400
RefSeq (protein) NP_001275902 NP_031426
Location (UCSC) Chr 10:
127.7 – 128.08 Mb
Chr 7:
133.88 – 134.23 Mb
PubMed search [1] [2]

Disintegrin and metalloproteinase domain-containing protein 12 is an enzyme that in humans is encoded by the ADAM12 gene.[1][2]

Function[edit]

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.[3]

ADAM 12, a metalloprotease that binds insulin growth factor binding protein-3 (IGFBP-3), appears to be an effective early Down syndrome marker. Decreased levels of ADAM 12 may be detected in cases of trisomy 21 as early as 8 to 10 weeks gestation. Maternal serum ADAM 12 and PAPP-A levels at 8 to 9 weeks gestation in combination with maternal age yielded a 91% detection rate for Down syndrome at a 5% false-positive rate. When nuchal translucency data from approximately 12 weeks gestation was added, this increased the detection rate to 97%.[4]

Interactions[edit]

ADAM12 has been shown to interact with:

References[edit]

  1. ^ Gilpin BJ, Loechel F, Mattei MG, Engvall E, Albrechtsen R, Wewer UM (Feb 1998). "A novel, secreted form of human ADAM 12 (meltrin alpha) provokes myogenesis in vivo". J Biol Chem 273 (1): 157–66. doi:10.1074/jbc.273.1.157. PMID 9417060. 
  2. ^ Kveiborg M, Albrechtsen R, Couchman JR, Wewer UM (Jun 2008). "Cellular roles of ADAM12 in health and disease". Int J Biochem Cell Biol 40 (9): 1685–702. doi:10.1016/j.biocel.2008.01.025. PMID 18342566. 
  3. ^ "Entrez Gene: ADAM12 ADAM metallopeptidase domain 12 (meltrin alpha)". 
  4. ^ Danforth's Obstetrics and Gynecology, 10th Edition; Copyright ©2008 Lippincott Williams & Wilkins; Chapter 7: Prenatal Diagnosis, Page 113
  5. ^ Galliano MF, Huet C, Frygelius J, Polgren A, Wewer UM, Engvall E (May 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. doi:10.1074/jbc.275.18.13933. PMID 10788519. 
  6. ^ Shi Z, Xu W, Loechel F, Wewer UM, Murphy LJ (Jun 2000). "ADAM 12, a disintegrin metalloprotease, interacts with insulin-like growth factor-binding protein-3". J. Biol. Chem. 275 (24): 18574–80. doi:10.1074/jbc.M002172200. PMID 10849447. 
  7. ^ Loechel F, Fox JW, Murphy G, Albrechtsen R, Wewer UM (Nov 2000). "ADAM 12-S cleaves IGFBP-3 and IGFBP-5 and is inhibited by TIMP-3". Biochem. Biophys. Res. Commun. 278 (3): 511–5. doi:10.1006/bbrc.2000.3835. PMID 11095942. 
  8. ^ Kang Q, Cao Y, Zolkiewska A (Jul 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:10.1074/jbc.M101162200. PMID 11313349. 

Further reading[edit]

  • 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:10.1074/jbc.M101162200. PMID 11313349. 
  • Yagami-Hiromasa T, Sato T, Kurisaki T, Kamijo K, Nabeshima Y, Fujisawa-Sehara A (1995). "A metalloprotease-disintegrin participating in myoblast fusion.". Nature 377 (6550): 652–6. doi:10.1038/377652a0. PMID 7566181. 
  • Loechel F, Gilpin BJ, Engvall E, Albrechtsen R, Wewer UM (1998). "Human ADAM 12 (meltrin alpha) is an active metalloprotease.". J. Biol. Chem. 273 (27): 16993–7. doi:10.1074/jbc.273.27.16993. 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. doi:10.1074/jbc.274.44.31693. PMID 10531379. 
  • Galliano MF, Huet C, Frygelius J, Polgren A, Wewer UM, Engvall E (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. doi:10.1074/jbc.275.18.13933. PMID 10788519. 
  • Iba K, Albrechtsen R, Gilpin B, Fröhlich C, Loechel F, Zolkiewska A, Ishiguro K, Kojima T, Liu W, Langford JK, Sanderson RD, Brakebusch C, Fässler R, Wewer UM (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. doi:10.1083/jcb.149.5.1143. PMC 2174829. PMID 10831617. 
  • Shi Z, Xu W, Loechel F, Wewer UM, Murphy LJ (2000). "ADAM 12, a disintegrin metalloprotease, interacts with insulin-like growth factor-binding protein-3.". J. Biol. Chem. 275 (24): 18574–80. doi:10.1074/jbc.M002172200. PMID 10849447. 
  • Eto K, Puzon-McLaughlin W, Sheppard D, Sehara-Fujisawa A, Zhang XP, Takada Y (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:10.1074/jbc.M001953200. PMID 10944520. 
  • Loechel F, Fox JW, Murphy G, Albrechtsen R, Wewer UM (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:10.1006/bbrc.2000.3835. PMID 11095942. 
  • Suzuki A, Kadota N, Hara T, Nakagami Y, Izumi T, Takenawa T, Sabe H, Endo T (2000). "Meltrin alpha cytoplasmic domain interacts with SH3 domains of Src and Grb2 and is phosphorylated by v-Src.". Oncogene 19 (51): 5842–50. doi:10.1038/sj.onc.1203986. PMID 11127814. 
  • Kawaguchi N, Xu X, Tajima R, Kronqvist P, Sundberg C, Loechel F, Albrechtsen R, Wewer UM (2002). "ADAM 12 protease induces adipogenesis in transgenic mice.". Am. J. Pathol. 160 (5): 1895–903. doi:10.1016/S0002-9440(10)61136-4. PMC 1850877. 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:10.1074/jbc.M110814200. PMID 12000744. 
  • Abram CL, Seals DF, Pass I, Salinsky D, Maurer L, Roth TM, Courtneidge SA (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:10.1074/jbc.M300267200. PMID 12615925. 
  • Le Pabic H, Bonnier D, Wewer UM, Coutand A, Musso O, Baffet G, Clément B, Théret N (2003). "ADAM12 in human liver cancers: TGF-beta-regulated expression in stellate cells is associated with matrix remodeling". Hepatology 37 (5): 1056–66. doi:10.1053/jhep.2003.50205. PMID 12717386. 
  • Kawaguchi N, Sundberg C, Kveiborg M, Moghadaszadeh B, Asmar M, Dietrich N, Thodeti CK, Nielsen FC, Möller P, Mercurio AM, Albrechtsen R, Wewer UM (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:10.1242/jcs.00699. PMID 12915587. 
  • Mori S, Tanaka M, Nanba D, Nishiwaki E, Ishiguro H, Higashiyama S, Matsuura N (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:10.1074/jbc.M306393200. PMID 12952982. 
  • Laigaard J, Sørensen T, Fröhlich C, Pedersen BN, Christiansen M, Schiøtt K, Uldbjerg N, Albrechtsen R, Clausen HV, Ottesen B, Wewer UM (2004). "ADAM12: a novel first-trimester maternal serum marker for Down syndrome". Prenat. Diagn. 23 (13): 1086–91. doi:10.1002/pd.762. PMID 14691998. 

External links[edit]