ADAM7

= ADAM7 =

ADAM7, also known as A Disintegrin and Metalloproteinase domain-containing protein 7, is a member of the ADAM family of proteins. These proteins are characterized by their role in cell signaling, adhesion, and proteolysis. ADAM7 is encoded by the ADAM7 gene in humans.

Structure

ADAM7 is a type I transmembrane protein that consists of several distinct domains:

• Signal Peptide: Directs the nascent protein to the secretory pathway.
• Pro-domain: Maintains the enzyme in an inactive form until it is cleaved.
• Metalloprotease Domain: Although ADAM7 contains this domain, it is catalytically inactive due to the absence of a critical zinc-binding motif.
• Disintegrin Domain: Involved in cell adhesion processes.
• Cysteine-rich Domain: May play a role in protein-protein interactions.
• EGF-like Domain: Potentially involved in cell signaling.
• Transmembrane Domain: Anchors the protein in the cell membrane.
• Cytoplasmic Tail: May interact with intracellular signaling molecules.

Function

ADAM7 is primarily expressed in the epididymis and is thought to play a role in sperm maturation and male fertility. Unlike other ADAM proteins, ADAM7 lacks proteolytic activity, suggesting its function is more related to cell adhesion and signaling rather than proteolysis.

Expression

The expression of ADAM7 is highly tissue-specific, with significant levels found in the epididymis, pancreas, and certain cancerous tissues. Its expression is regulated by hormonal and developmental cues.

Clinical Significance

ADAM7 has been implicated in various pathological conditions, including cancer. Its expression is altered in pancreatic cancer, and it may serve as a potential biomarker for the disease. Additionally, ADAM7 has been studied in the context of male infertility, given its role in sperm maturation.

Research

Ongoing research is focused on understanding the precise biological functions of ADAM7, its role in disease, and its potential as a therapeutic target. Studies are exploring its interactions with other proteins and its involvement in signaling pathways.

References

• Blobel, C. P. (2005). ADAMs: key components in EGFR signalling and development. Nature Reviews Molecular Cell Biology, 6(1), 32-43.
• Edwards, D. R., & Handsley, M. M. (2008). ADAM metalloproteinases: biological roles and potential as therapeutic targets. Expert Opinion on Therapeutic Targets, 12(11), 1347-1357.
• Hsia, H. E., & Blobel, C. P. (2012). The ADAM family: coordinators of nervous system development, plasticity and repair. Nature Reviews Neuroscience, 13(12), 759-771.

External Links

• [GeneCards: ADAM7](https://www.genecards.org/cgi-bin/carddisp.pl?gene=ADAM7)
• [UniProt: ADAM7](https://www.uniprot.org/uniprot/Q9H2U9)