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[edit | edit source]

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[edit | edit source]

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[edit | edit source]

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[edit | edit source]

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[edit | edit source]

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[edit | edit source]

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.