ADAM28

ADAM metallopeptidase domain 28
Identifiers
SymbolsADAM28 ; ADAM 28; ADAM23; MDC-L; MDC-Lm; MDC-Ls; MDCL; eMDC II; eMDCII
External IDsOMIM: 606188 MGI: 105988 HomoloGene: 40705 IUPHAR: 1669 GeneCards: ADAM28 Gene
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez1086313522
EnsemblENSG00000042980ENSMUSG00000014725
UniProtQ9UKQ2Q9JLN6
RefSeq (mRNA)NM_014265NM_001048175
RefSeq (protein)NP_055080NP_001041640
Location (UCSC)Chr 8:
24.15 – 24.22 Mb		Chr 14:
68.61 – 68.66 Mb
PubMed search

Disintegrin and metalloproteinase domain-containing protein 28 is an enzyme that in humans is encoded by the ADAM28 gene.[1]

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]

References

  1. ↑ 1.0 1.1 "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): 29251–9. 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): 1127–34. 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): 21–7. 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): 3784–92. 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): 3734–41. 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): 30469–77. 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): 263–73. doi:10.1002/ijc.21324. PMID 16052521.
  • 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): 9913–20. 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): 25864–74. doi:10.1074/jbc.M702414200. PMID 17597069.

External links