Developer site: The content shown here is test data.

MyEClinic
MyEClinic
Health Dictionary AI Health Chat Find an Online Doctor
A serene Zen garden with raked sand and smooth stones, symbolising clarity and calm

Health Dictionary

Reliable, easy-to-read patient information on common medical conditions — written in plain language, free of jargon, and grounded in current evidence. Browse the most frequent diagnoses, understand what they mean for everyday life, and learn which steps and questions help you have a focused conversation with your doctor.

Back to skin conditions

ADAM28

Introduction

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

References

  1. ↑ 1.0 1.1 “Entrez Gene: ADAM28 ADAM metallopeptidase domain 28”.
Further reading

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