integrini

Integrins are a family of cell surface receptors crucial for mediating cell adhesion to the extracellular matrix (ECM) and facilitating cell-cell interactions. They are transmembrane heterodimeric proteins composed of alpha and beta subunits, with at least 24 known combinations in humans, each exhibiting distinct binding specificities and functions.

Functionally, integrins play vital roles in numerous biological processes, including tissue development, immune responses, wound healing, and cell migration. They transmit mechanical and chemical signals from the ECM into the cell, a process known as signal transduction, which influences cellular behaviors such as proliferation, differentiation, and survival. Integrins also facilitate the organization of the cytoskeleton and influence cellular morphology.

Structurally, integrins exist in different conformational states, transitioning between inactive and active forms to regulate adhesion strength. Their activation is controlled by inside-out signaling mechanisms within the cell and outside-in signals from the ECM. Upon ligand binding—typically to proteins like fibronectin, collagen, or laminin—they cluster and form focal adhesion complexes that connect to the cytoskeleton.

Integrins are involved in various pathological conditions when dysfunctional, including cancer metastasis, chronic inflammation, and fibrosis. Due to their central role in cell adhesion and signaling, they are targets for therapeutic intervention in disease treatments.

Research on integrins continues to explore their diverse functions and mechanisms, expanding understanding of their importance in health and disease. Their capacity to sense and respond to mechanical forces makes them key components of cellular mechanotransduction pathways.