Collagen-binding integrins (CBIs)

Collagen-binding integrins are a specialized subgroup of the integrin family, comprising four heterodimers: alpha-1 beta-1, alpha-2 beta-1, alpha-10 beta-1, and alpha-11 beta-1 (Zeltz & Gullberg, 2016, PMID: 26851587). These receptors are unique for their alpha-subunit I-domain, which directly recognizes and binds to specific motifs (such as GFOGER) within the triple-helical structure of various collagens (Heino, 2014, PMID: 24411333). Biologically, they mediate cell-matrix interactions essential for adhesion, migration, and the regulation of extracellular matrix synthesis (Popov et al., 2011, PMID: 21454514). In pathological states, these integrins play significant roles in promoting tumor angiogenesis and metastasis, driving chronic inflammatory responses in arthritis, and facilitating the progression of organ fibrosis (Zeltz et al., 2019, PMID: 30861354). Therapeutic strategies targeting these receptors primarily involve monoclonal antibodies and small molecule inhibitors designed to disrupt collagen binding, with several candidates having reached clinical trials for conditions like rheumatoid arthritis and cancer (Nissinen & Heino, 2014, PMID: 24764554). However, drug development faces challenges such as the potential for bleeding complications due to the role of alpha-2 beta-1 in platelet function.

Other names

Collagen receptorsBeta-1 integrin subfamilyVLA-1 (alpha-1 beta-1)VLA-2 (alpha-2 beta-1)Integrin alpha-10 beta-1Integrin alpha-11 beta-1

Antagonism of the alpha-subunit I-domain to block collagen binding and subsequent intracellular signaling through FAK, Src, and MAPK pathways (Heino, 2014, PMID: 24411333).