Biology:ADAM28

Short description: Protein-coding gene in the species Homo sapiens

Generic protein structure example

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.

Further reading

• "MDC-L, a novel metalloprotease disintegrin cysteine-rich protein family member expressed by human lymphocytes.". J. Biol. Chem. 274 (41): 29251–29259. 1999. doi:10.1074/jbc.274.41.29251. PMID 10506182. 
• "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. doi:10.1093/molehr/5.12.1127. PMID 10587367. 
• "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. doi:10.1042/0264-6021:3480021. PMID 10794709. 
• "The lymphocyte metalloprotease MDC-L (ADAM 28) is a ligand for the integrin alpha4beta1". J. Biol. Chem. 277 (5): 3784–3792. 2002. doi:10.1074/jbc.M109538200. PMID 11724793. 
• "Integrin alpha4beta1-dependent adhesion to ADAM 28 (MDC-L) requires an extended surface of the disintegrin domain". Biochemistry 42 (13): 3734–3741. 2003. doi:10.1021/bi026871y. PMID 12667064. 
• "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. doi:10.1074/jbc.M213157200. PMID 12777399. 
• "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. doi:10.1016/j.bbrc.2004.01.022. PMID 15013428. 
• "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. doi:10.1002/ijc.21324. PMID 16052521. 
• "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. doi:10.1158/0008-5472.CAN-06-0377. PMID 17047053. 
• "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. doi:10.1074/jbc.M702414200. PMID 17597069. 

External links

• The MEROPS online database for peptidases and their inhibitors: M12.224
• Human ADAM28 genome location and ADAM28 gene details page in the UCSC Genome Browser.