ADAM7

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ADAM7

ADAM7 is a member of the ADAM (A Disintegrin and Metalloproteinase) family of proteins, which are involved in a variety of biological processes, including cell signaling, adhesion, and migration. These proteins are characterized by their complex structure, which includes a disintegrin domain and a metalloproteinase domain, among others.

Structure

ADAM7, like other members of the ADAM family, is a type I transmembrane protein. It consists of several distinct domains:

  • Pro-domain: This domain is involved in the regulation of the protein's activity. It is typically cleaved off to activate the protein.
  • Metalloproteinase domain: This domain has enzymatic activity and is responsible for the proteolytic functions of the protein.
  • Disintegrin domain: This domain is involved in cell adhesion processes.
  • Cysteine-rich domain: This domain may play a role in protein-protein interactions.
  • EGF-like domain: This domain is similar to epidermal growth factor and may be involved in cell signaling.
  • Transmembrane domain: This domain anchors the protein in the cell membrane.
  • Cytoplasmic tail: This domain may be involved in intracellular signaling pathways.

Function

ADAM7 is primarily expressed in the testis and is thought to play a role in sperm maturation and fertilization. Unlike some other ADAM proteins, ADAM7 lacks proteolytic activity due to the absence of a critical zinc-binding motif in its metalloproteinase domain. Instead, it is believed to function in cell adhesion and signaling.

Clinical Significance

While the precise physiological role of ADAM7 is not fully understood, alterations in its expression have been associated with certain diseases. For example, changes in ADAM7 expression levels have been observed in some cancers, suggesting a potential role in tumor progression or metastasis.

Research

Ongoing research is focused on elucidating the specific functions of ADAM7 in reproductive biology and its potential implications in cancer biology. Understanding the role of ADAM7 could lead to new insights into cell adhesion mechanisms and the development of novel therapeutic strategies.

Also see


ADAM Family

A Disintegrin and Metalloproteinase

Members
Functions
Related Topics
See Also
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Contributors: Prab R. Tumpati, MD