ADAM28


ADAM28

ADAM metallopeptidase domain 28, also known as ADAM28, is a human gene.cite web | title = Entrez Gene: ADAM28 ADAM metallopeptidase domain 28| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10863| accessdate = ]

PBB_Summary
section_title =
summary_text = 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.cite web | title = Entrez Gene: ADAM28 ADAM metallopeptidase domain 28| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10863| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Roberts CM, Tani PH, Bridges LC, "et al." |title=MDC-L, a novel metalloprotease disintegrin cysteine-rich protein family member expressed by human lymphocytes. |journal=J. Biol. Chem. |volume=274 |issue= 41 |pages= 29251–9 |year= 1999 |pmid= 10506182 |doi=
*cite journal | author=Jury JA, Perry AC, Hall L |title=Identification, sequence analysis and expression of transcripts encoding a putative metalloproteinase, eMDC II, in human and macaque epididymis. |journal=Mol. Hum. Reprod. |volume=5 |issue= 12 |pages= 1127–34 |year= 2000 |pmid= 10587367 |doi=
*cite journal | author=Howard L, Maciewicz RA, Blobel CP |title=Cloning and characterization of ADAM28: evidence for autocatalytic pro-domain removal and for cell surface localization of mature ADAM28. |journal=Biochem. J. |volume=348 Pt 1 |issue= |pages= 21–7 |year= 2000 |pmid= 10794709 |doi=
*cite journal | author=Bridges LC, Tani PH, Hanson KR, "et al." |title=The lymphocyte metalloprotease MDC-L (ADAM 28) is a ligand for the integrin alpha4beta1. |journal=J. Biol. Chem. |volume=277 |issue= 5 |pages= 3784–92 |year= 2002 |pmid= 11724793 |doi= 10.1074/jbc.M109538200
*cite journal | author=Bridges LC, Hanson KR, Tani PH, "et al." |title=Integrin alpha4beta1-dependent adhesion to ADAM 28 (MDC-L) requires an extended surface of the disintegrin domain. |journal=Biochemistry |volume=42 |issue= 13 |pages= 3734–41 |year= 2003 |pmid= 12667064 |doi= 10.1021/bi026871y
*cite journal | author=Fourie AM, Coles F, Moreno V, Karlsson L |title=Catalytic activity of ADAM8, ADAM15, and MDC-L (ADAM28) on synthetic peptide substrates and in ectodomain cleavage of CD23. |journal=J. Biol. Chem. |volume=278 |issue= 33 |pages= 30469–77 |year= 2003 |pmid= 12777399 |doi= 10.1074/jbc.M213157200
*cite journal | author=Mochizuki S, Shimoda M, Shiomi T, "et al." |title=ADAM28 is activated by MMP-7 (matrilysin-1) and cleaves insulin-like growth factor binding protein-3. |journal=Biochem. Biophys. Res. Commun. |volume=315 |issue= 1 |pages= 79–84 |year= 2004 |pmid= 15013428 |doi= 10.1016/j.bbrc.2004.01.022
*cite journal | author=Ohtsuka T, Shiomi T, Shimoda M, "et al." |title=ADAM28 is overexpressed in human non-small cell lung carcinomas and correlates with cell proliferation and lymph node metastasis. |journal=Int. J. Cancer |volume=118 |issue= 2 |pages= 263–73 |year= 2006 |pmid= 16052521 |doi= 10.1002/ijc.21324
*cite journal | author=Mitsui Y, Mochizuki S, Kodama T, "et al." |title=ADAM28 is overexpressed in human breast carcinomas: implications for carcinoma cell proliferation through cleavage of insulin-like growth factor binding protein-3. |journal=Cancer Res. |volume=66 |issue= 20 |pages= 9913–20 |year= 2006 |pmid= 17047053 |doi= 10.1158/0008-5472.CAN-06-0377
*cite journal | author=Shimoda M, Hashimoto G, Mochizuki S, "et al." |title=Binding of ADAM28 to P-selectin glycoprotein ligand-1 enhances P-selectin-mediated leukocyte adhesion to endothelial cells. |journal=J. Biol. Chem. |volume=282 |issue= 35 |pages= 25864–74 |year= 2007 |pmid= 17597069 |doi= 10.1074/jbc.M702414200

PBB_Controls
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