ADAM28
Protein-coding gene in humans
ADAM28 Identifiers Aliases ADAM28 , ADAM 28, ADAM23, MDC-L, MDC-Lm, MDC-Ls, MDCL, eMDC II, eMDCII, ADAM metallopeptidase domain 28External IDs OMIM : 606188 ; MGI : 105988 ; GeneCards : ADAM28 Gene location (Mouse ) Chr. Chromosome 14 (mouse) Band 14| 14 D1 Start 68,843,476 bp End 68,893,291 bp
RNA expression patternBgee Human Mouse (ortholog)Top expressed in corpus epididymis nasal epithelium olfactory zone of nasal mucosa gallbladder pancreatic ductal cell right uterine tube epithelium of nasopharynx mucosa of paranasal sinus bronchial epithelial cell appendix
Top expressed in superior surface of tongue gallbladder Ileal epithelium nasal epithelium olfactory epithelium transitional epithelium of urinary bladder corneal stroma plantaris muscle extensor digitorum longus muscle interventricular septum
More reference expression data
BioGPS
Wikidata
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
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. Bibcode :2004BBRC..315...79M . 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
Activity Regulation Classification Kinetics Types