Collagen and extracellular matrix proteins (ECM)

Collagen and extracellular matrix (ECM) proteins form the intricate, three-dimensional network that provides essential structural and biochemical support to cells in all tissues [3, 13]. This broad category encompasses over 28 types of collagen, along with elastin, proteoglycans, and glycoproteins such as fibronectin and laminin [5, 11]. Beyond providing mechanical strength, these proteins act as dynamic signaling hubs that regulate critical cellular processes, including adhesion, migration, differentiation, and survival [3, 14]. Pathological remodeling of the ECM is a central feature of numerous diseases, most notably fibrosis, where excessive collagen deposition leads to organ failure in the liver, lungs, and heart [11, 13]. In oncology, the tumor ECM often becomes dense and cross-linked, creating a physical barrier that limits drug penetration and promotes metastatic cell invasion [1, 6]. Therapeutic interventions include the use of enzymes like collagenase to degrade pathological tissue, as well as antifibrotic drugs that inhibit the synthesis of matrix components [3, 5]. Additionally, researchers are developing collagen-binding domains (CBDs) to anchor immunotherapies and growth factors directly to the ECM, enhancing local drug retention and reducing systemic toxicity [1, 4]. Monitoring ECM turnover through circulating biomarkers like pro-collagen fragments is increasingly used to assess disease progression and therapeutic efficacy in clinical settings [7, 16].

Other names

Extracellular matrixECM proteinsConnective tissue proteinsGround substance

Drugs targeting these proteins function by enzymatically degrading pathological collagen fibers, inhibiting the synthesis and cross-linking of new matrix components by activated fibroblasts, or utilizing collagen-binding domains (CBD) to anchor therapeutic agents directly to the matrix for localized effect [1, 3, 5, 6].