Multimerin 1

Platelets. 2008 Mar;19(2):83-95. doi: 10.1080/09537100701832157.


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 alpha-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.

Publication types

  • Review

MeSH terms

  • Animals
  • Blood Platelets / physiology
  • Blood Proteins / chemistry
  • Blood Proteins / genetics
  • Blood Proteins / physiology*
  • Cell Adhesion / physiology
  • Cytoplasmic Granules / physiology
  • Endothelial Cells / physiology
  • Extracellular Matrix Proteins / physiology
  • Factor V / metabolism
  • Humans
  • Megakaryocytes / physiology
  • Platelet Activation
  • Platelet Aggregation
  • Protein Binding
  • Protein Transport


  • Blood Proteins
  • Extracellular Matrix Proteins
  • multimerin
  • Factor V