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Disintegrin and metalloproteinase domain-containing protein 28 is an enzyme that in humans is encoded by the ADAM28 gene.[5]
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.[5]
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000042980 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000014725 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ a b "Entrez Gene: ADAM28 ADAM metallopeptidase domain 28".
Further reading
- Roberts CM, Tani PH, Bridges LC, et al. (1999). "MDC-L, a novel metalloprotease disintegrin cysteine-rich protein family member expressed by human lymphocytes". J. Biol. Chem. 274 (41): 29251–29259. doi:10.1074/jbc.274.41.29251. PMID 10506182.
- Jury JA, Perry AC, Hall L (2000). "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. doi:10.1093/molehr/5.12.1127. PMID 10587367.
- Howard L, Maciewicz RA, Blobel CP (2000). "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. doi:10.1042/0264-6021:3480021. PMC 1221031. PMID 10794709.
- Bridges LC, Tani PH, Hanson KR, et al. (2002). "The lymphocyte metalloprotease MDC-L (ADAM 28) is a ligand for the integrin alpha4beta1". J. Biol. Chem. 277 (5): 3784–3792. doi:10.1074/jbc.M109538200. PMID 11724793.
- Bridges LC, Hanson KR, Tani PH, et al. (2003). "Integrin alpha4beta1-dependent adhesion to ADAM 28 (MDC-L) requires an extended surface of the disintegrin domain". Biochemistry. 42 (13): 3734–3741. doi:10.1021/bi026871y. PMID 12667064.
- Fourie AM, Coles F, Moreno V, Karlsson L (2003). "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. doi:10.1074/jbc.M213157200. PMID 12777399.
- Mochizuki S, Shimoda M, Shiomi T, et al. (2004). "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. doi:10.1016/j.bbrc.2004.01.022. PMID 15013428.
- Ohtsuka T, Shiomi T, Shimoda M, et al. (2006). "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. doi:10.1002/ijc.21324. PMID 16052521. S2CID 19344958.
- Mitsui Y, Mochizuki S, Kodama T, et al. (2006). "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. doi:10.1158/0008-5472.CAN-06-0377. PMID 17047053.
- Shimoda M, Hashimoto G, Mochizuki S, et al. (2007). "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. 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.
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