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Integrins are **transmembrane receptors** composed of alpha and beta subunits that mediate cell-cell and cell-extracellular matrix interactions. **Integrin beta subunits 1 (ITGB1), 3 (ITGB3), and 5 (ITGB5)** each pair with various alpha subunits to form heterodimeric receptors with distinct ligand specificities. **Integrin beta‑1** is widely expressed across tissues where it regulates processes such as embryogenesis, tissue repair, immune responses, hemostasis, and tumor metastasis by linking the actin cytoskeleton to extracellular matrix proteins like fibronectin.[1] It has several isoforms with tissue-specific functions. **Integrin beta‑3**, often found paired with alpha-IIb or alpha-V subunits (e.g., αIIbβ3 on platelets), plays a key role in platelet aggregation but also participates in other cellular adhesive events.[4] **Integrin beta‑5**, encoded by *ITGB5*, forms heterodimers that participate particularly in intercellular communication during tumor progression/metastasis; elevated levels have been associated with autosomal dominant osteopetrosis type II.[2] These molecules have distinct activation mechanisms depending on their structure and pairing partners,[3] which influences their biological roles across different tissues. Note: The entry "Integrin beta1/beta3/beta5" is not a standard single target but rather refers collectively to three related but separate proteins; each should be treated individually for precise scientific/therapeutic purposes.
Not specified in the search results. Generally, drugs targeting integrins act as antagonists or inhibitors of cell adhesion and signaling pathways.
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