Extracellular matrix proteins in vitreous adhesions (ECM proteins)

Extracellular matrix (ECM) proteins in vitreous adhesions are a complex group of structural molecules, primarily including collagen (Types II, IX, and V/XI), laminin, and fibronectin, that mediate the attachment between the posterior vitreous cortex and the internal limiting membrane (ILM) of the retina [1, 11, 16]. These proteins play a critical role in maintaining the structural integrity of the vitreoretinal interface; however, persistent or pathological adhesions can lead to vitreomacular traction (VMT) and the formation of macular holes [1, 18, 20]. Therapeutic strategies, known as pharmacological vitreolysis, utilize enzymes like ocriplasmin to proteolytically degrade these ECM components [1, 2, 5]. By targeting the molecular glue of the vitreoretinal interface, these drugs induce a posterior vitreous detachment (PVD), thereby relieving mechanical traction and potentially avoiding the need for invasive surgical vitrectomy [1, 3, 4]. Monitoring via optical coherence tomography (OCT) is essential to assess the efficacy and safety of these interventions, as complications such as retinal tears or detachment can occur [3, 5, 20].

Other names

Vitreoretinal interface proteinsVitreous base proteinsPosterior vitreous cortex proteinsInternal limiting membrane proteins

Pharmacological vitreolysis involves the enzymatic cleavage of extracellular matrix components, specifically laminin and fibronectin, to facilitate the separation of the posterior vitreous cortex from the internal limiting membrane of the retina [1, 2, 5]. This process induces vitreous liquefaction and posterior vitreous detachment, relieving mechanical traction on the macula [1, 4, 20].