ADAM15 - ADAM metallopeptidase domain 15 | Elisa - Clia - Antibody - Protein

Background

ADAM15, also known as ADAM metallopeptidase domain 15, is a member of the ADAM (a disintegrin and metalloproteinase) family . These proteins are involved in various biological processes, including cell adhesion, migration, proteolysis, and signaling. ADAM15 is a transmembrane protein, meaning it spans the cell membrane, with both extracellular and intracellular domains.ADAM15 consists of several distinct domains, including a metalloproteinase domain responsible for its proteolytic activity, a disintegrin domain involved in cell-cell and cell-matrix interactions, a cysteine-rich domain, an EGF-like domain, a transmembrane domain, and a cytoplasmic tail.ADAM15 is implicated in various physiological and pathological processes, including cell adhesion, migration, proliferation, and signaling. It can cleave cell surface proteins, releasing soluble forms of these proteins into the extracellular environment. Is also involved in cell-cell and cell-matrix interactions. It interacts with various proteins on the cell surface and in the extracellular matrix, including integrins, growth factors, cytokines, and cell adhesion molecules.ADAM15 has been linked to cancer progression and metastasis. Its expression is often elevated in various cancers, including breast, lung, colon, prostate, and pancreatic cancers. ADAM15 can promote tumor cell invasion and metastasis by facilitating cell migration and invasion through the extracellular matrix.

Protein Structure

ADAM15 has a typical ADAM protein structure consisting of several functional domains:

• Signal Peptide: Directs the nascent protein to the secretory pathway.
• Prodomain: Maintains the enzyme in an inactive form until it reaches its proper cellular location.
• Metalloprotease Domain: Contains the active site with a zinc-binding motif essential for its proteolytic function.
• Disintegrin Domain: Interacts with integrins and other cell surface receptors, facilitating cell adhesion and signaling.
• Cysteine-Rich Domain: Contributes to the protein’s stability and interactions.
• EGF-Like Domain: Participates in protein-protein interactions.
• Transmembrane Domain: Anchors the protein in the cell membrane.
• Cytoplasmic Tail: Involved in intracellular signaling and interactions with cytoskeletal components.

Classification and Subtypes

ADAM15 belongs to the ADAM family, which includes proteins with metalloprotease and disintegrin domains. ADAM15 is specifically classified under metalloproteases due to its catalytic activity.

Function and Biological Significance

ADAM15 performs several crucial functions:

1. Proteolysis: The metalloprotease domain cleaves various substrates, including membrane-bound precursors of signaling molecules.
2. Cell Adhesion: The disintegrin domain interacts with integrins, mediating cell adhesion, migration, and signaling.
3. Angiogenesis: Involved in the formation of new blood vessels, which is critical in both normal physiological processes and pathological conditions like cancer.
4. Inflammation: Modulates inflammatory responses by shedding cytokine receptors and other immune-related molecules.
5. Tissue Remodeling: Plays a role in remodeling the extracellular matrix, important for development, wound healing, and disease processes.

Interactions

ADAM15 interacts with a variety of proteins and cellular components:

1. Integrins: The disintegrin domain interacts with integrins such as αvβ3, influencing cell adhesion and migration.
2. Extracellular Matrix Proteins: Involved in the degradation and remodeling of extracellular matrix components.
3. Signaling Molecules: Modulates the activity of various signaling pathways by shedding membrane-bound receptors and ligands.
4. Cell Surface Receptors: Interacts with and sheds receptors involved in immune responses and cell communication.

Clinical Significance

The function and regulation of ADAM15 have significant implications in various diseases and conditions:

1. Cancer: ADAM15 is implicated in cancer progression and metastasis through its roles in cell adhesion, migration, and proteolysis. It is often overexpressed in tumors and associated with poor prognosis.
2. Cardiovascular Diseases: ADAM15 activity affects vascular remodeling and angiogenesis, impacting conditions like atherosclerosis and myocardial infarction.
3. Inflammatory Diseases: By modulating inflammatory responses, ADAM15 is involved in diseases such as rheumatoid arthritis and inflammatory bowel disease.
4. Osteoarthritis: ADAM15 contributes to cartilage degradation and inflammation in osteoarthritis, making it a potential therapeutic target.

Summary

ADAM15, a member of the ADAM family, is integral to processes such as proteolysis, cell adhesion, signaling, angiogenesis, and inflammation. It has a multi-domain structure, including a metalloprotease domain for proteolytic activity and a disintegrin domain for cell adhesion. ADAM15 interacts with integrins, extracellular matrix proteins, signaling molecules, and cell surface receptors. Clinically, ADAM15 is significant in the context of cancer, cardiovascular diseases, inflammatory diseases, and osteoarthritis. Understanding its structure, function, interactions, and clinical implications provides valuable insights into its role in cellular processes and potential as a therapeutic target.