Integrin alpha-1 (ITGA1) (ITGA1)

Integrin alpha-1 (ITGA1), also known as CD49a, is a transmembrane glycoprotein that non-covalently pairs with the integrin beta-1 subunit to form the alpha-1 beta-1 (α1β1) heterodimer, a primary receptor for collagen and laminin (UniProt P56199). This complex, often referred to as Very Late Antigen-1 (VLA-1), plays a critical role in mediating cell-matrix interactions, cell migration, and signal transduction pathways that regulate cell survival and proliferation (PubMed: 22431567). ITGA1 is predominantly expressed on fibroblasts, smooth muscle cells, and activated leukocytes, making it a key player in inflammatory and fibrotic processes (PubMed: 25605874). It is also a defining marker for resident memory T cells (Trm), which are essential for local immune surveillance in tissues like the skin and lungs (PubMed: 28282400). In pathological states, ITGA1 contributes to the progression of chronic kidney disease, rheumatoid arthritis, and various cancers by promoting tissue remodeling and the recruitment of inflammatory cells (PubMed: 18448593). Therapeutic strategies targeting ITGA1, such as the monoclonal antibodies SAN-300 and SAR113244, aim to inhibit its binding to the extracellular matrix to reduce inflammation and fibrosis (ClinicalTrials.gov NCT01243151). Additionally, ITGA1 has been implicated in the regulation of angiogenesis and the maintenance of the vascular basement membrane, suggesting its involvement in tumor growth and metastasis (PubMed: 11805151). Despite its potential as a therapeutic target, affecting ITGA1 requires careful consideration of its role in normal physiological processes like wound healing and vascular homeostasis, as evidenced by studies in knockout models.

Other names

CD49aVLA-1Very late antigen 1Integrin subunit alpha 1ITGA1

Antagonism of the alpha-1 beta-1 integrin complex to inhibit binding to collagen and laminin, thereby reducing leukocyte recruitment and fibrotic signaling.