ADAM28 explained

Disintegrin and metalloproteinase domain-containing protein 28 is an enzyme that in humans is encoded by the ADAM28 gene.

This gene encodes a member of the ADAM (a disintegrin and metalloprotease domain) 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. The protein encoded by this gene is a lymphocyte-expressed ADAM protein. Alternative splicing results in two transcript variants. The shorter version encodes a secreted isoform, while the longer version encodes a transmembrane isoform.^[1]

Further reading

• Roberts CM, Tani PH, Bridges LC . MDC-L, a novel metalloprotease disintegrin cysteine-rich protein family member expressed by human lymphocytes. . J. Biol. Chem. . 274 . 41 . 29251–29259 . 1999 . 10506182 . 10.1074/jbc.274.41.29251 . etal. free .
• Jury JA, Perry AC, Hall L . Identification, sequence analysis and expression of transcripts encoding a putative metalloproteinase, eMDC II, in human and macaque epididymis. . Mol. Hum. Reprod. . 5 . 12 . 1127–1134 . 2000 . 10587367 . 10.1093/molehr/5.12.1127 . free .
• Howard L, Maciewicz RA, Blobel CP . Cloning and characterization of ADAM28: evidence for autocatalytic pro-domain removal and for cell surface localization of mature ADAM28 . Biochem. J. . 348 Pt 1 . Pt 1. 21–27 . 2000 . 10794709 . 10.1042/0264-6021:3480021 . 1221031 .
• Bridges LC, Tani PH, Hanson KR . The lymphocyte metalloprotease MDC-L (ADAM 28) is a ligand for the integrin alpha4beta1 . J. Biol. Chem. . 277 . 5 . 3784–3792 . 2002 . 11724793 . 10.1074/jbc.M109538200 . etal. free .
• Bridges LC, Hanson KR, Tani PH . Integrin alpha4beta1-dependent adhesion to ADAM 28 (MDC-L) requires an extended surface of the disintegrin domain . Biochemistry . 42 . 13 . 3734–3741 . 2003 . 12667064 . 10.1021/bi026871y . etal.
• Fourie AM, Coles F, Moreno V, Karlsson L . Catalytic activity of ADAM8, ADAM15, and MDC-L (ADAM28) on synthetic peptide substrates and in ectodomain cleavage of CD23 . J. Biol. Chem. . 278 . 33 . 30469–30477 . 2003 . 12777399 . 10.1074/jbc.M213157200 . free .
• Mochizuki S, Shimoda M, Shiomi T . ADAM28 is activated by MMP-7 (matrilysin-1) and cleaves insulin-like growth factor binding protein-3 . Biochem. Biophys. Res. Commun. . 315 . 1 . 79–84 . 2004 . 15013428 . 10.1016/j.bbrc.2004.01.022 . etal.
• Ohtsuka T, Shiomi T, Shimoda M . ADAM28 is overexpressed in human non-small cell lung carcinomas and correlates with cell proliferation and lymph node metastasis . Int. J. Cancer . 118 . 2 . 263–273 . 2006 . 16052521 . 10.1002/ijc.21324 . 19344958 . etal. free .
• Mitsui Y, Mochizuki S, Kodama T . ADAM28 is overexpressed in human breast carcinomas: implications for carcinoma cell proliferation through cleavage of insulin-like growth factor binding protein-3 . Cancer Res. . 66 . 20 . 9913–9920 . 2006 . 17047053 . 10.1158/0008-5472.CAN-06-0377 . etal. free .
• Shimoda M, Hashimoto G, Mochizuki S . Binding of ADAM28 to P-selectin glycoprotein ligand-1 enhances P-selectin-mediated leukocyte adhesion to endothelial cells . J. Biol. Chem. . 282 . 35 . 25864–25874 . 2007 . 17597069 . 10.1074/jbc.M702414200 . etal. free .

External links

• The MEROPS online database for peptidases and their inhibitors: M12.224

Notes and References

1. Web site: Entrez Gene: ADAM28 ADAM metallopeptidase domain 28.