Integriinin

Integriinin refers to a class of proteins that play a crucial role in cell adhesion, signaling, and extracellular matrix interactions. These proteins are characterized by their ability to bind to specific ligands, facilitating cellular attachment to the surrounding environment. The term "integriinin" is not a standard or widely recognized term in scientific literature; however, it may be a colloquial or informal reference to integrins, a well-established family of transmembrane receptors.

Integrins are heterodimeric proteins composed of non-covalently associated α (alpha) and β (beta) subunits, forming a diverse array of receptor combinations that mediate interactions between cells and their extracellular matrix (ECM). These receptors are essential for processes such as cell migration, differentiation, proliferation, and survival. Integrins are found in nearly all vertebrate cell types and are involved in various physiological and pathological conditions, including wound healing, immune responses, and cancer metastasis.

The binding of integrins to their ligands, such as extracellular matrix proteins like collagen, fibronectin, and laminin, triggers intracellular signaling cascades that regulate cytoskeletal organization and gene expression. This dual functionality—both structural and signaling—makes integrins indispensable for maintaining tissue integrity and coordinating cellular responses to the environment.

Mutations or dysfunctions in integrin genes have been linked to several hereditary disorders, such as Glanzmann’s thrombasthenia (a bleeding disorder caused by defective platelet integrins) and leukocyte adhesion deficiency (LAD), where impaired integrin function leads to recurrent infections. Additionally, integrins are targeted in therapeutic strategies for diseases like cancer, autoimmune disorders, and inflammatory conditions, highlighting their significance in both basic biology and clinical medicine.