Hemicentin-1 (HMCN1)

Hemicentin-1 (HMCN1) is a very large, evolutionarily conserved extracellular matrix glycoprotein that is part of the fibulin family and is sometimes called fibulin-6[1][5]. It contains multiple structural domains, including a von Willebrand A (VWA) domain, a long stretch of immunoglobulin-like domains, multiple epidermal growth factor (EGF) domains, and a fibulin-type carboxy-terminal module[1][5]. Hemicentin-1 is expressed in a variety of tissues, especially those with rich connective tissue matrices, and is essential for maintaining tissue structure, particularly through its role in cell adhesion, basement membrane organization, and cellular junctions in tissues such as skin, muscle-tendon connections, eye, and kidney[1][2][4][5]. Hemicentin-1 supports cell migration, most notably in dental pulp and root dentin formation, and is important for tissue integrity during development and wound healing[1][3]. It is also uniquely required in mitotic cytokinesis as a secreted extracellular protein that stabilizes the cleavage furrow during cell division[3][6]. In disease, mutations, or dysregulation of HMCN1 have been implicated in several pathological states—including age-related macular degeneration, kidney disease, cardiomyopathy, and have emerging roles in regulating tumor microenvironments and cancer cell invasion[1][3]. There is currently no evidence that hemicentin-1 serves as a direct drug target, and it is not classified as a receptor, enzyme, transporter, or canonical therapeutic target[1][2][3][4][5][6].

Other names

fibulin-6FBLN6FIBL6FIBL-6ARMD1hemicentin 1hemicentin-1fibulin 6LOC100507250/HMCN1 fusion