![Sample our Bioscience journals, sign in here to start your access, Latest two full volumes FREE to you for 14 days]({"type":"image" , "src" : "/sda/5925/TOC-Subject-Sample-2021-Bioscience.jpg"})
Abstract
Multimerin 1 is a massive, soluble, disulfide-linked homopolymeric protein that is expressed in megakaryocytes, platelets and endothelial cells. Normally, multimerin 1 undergoes efficient sorting to secretion granules, and it is not detectable in plasma. Recently, multimerin 1 was designated as a member of the EMILIN protein family, a group of structurally similar, disulfide-linked multimeric proteins. Multimerin 1 has the structural features of an adhesive protein and it supports the adhesion of many different cell types in vitro, including activated platelets, neutrophils, and endothelial cells. Multimerin 1 also has the ability to self associate and form large, branching matrix fibers. In platelet α-granules, multimerin 1 functions as the binding protein for coagulation factor V, a key regulator of coagulation. This review summarizes the current knowledge on multimerin 1 including its orthologous genes, restricted pattern of expression, structure, biosynthesis and functions.