Immunocytochemical colocalization of adhesive proteins with clathrin in human blood platelets: further evidence for coated vesicle-mediated transport of von Willebrand factor, fibrinogen and fibronectin

Cell Tissue Res. 1995 Mar;279(3):453-7. doi: 10.1007/BF00318157.

Abstract

Coated membranes and vesicles play an important role in receptor-mediated endocytosis and intracellular trafficking in various cell types, and are also present in blood platelets. Platelets take up certain proteins from the blood plasma, such as von Willebrand factor and fibrinogen, and these substances are transferred to storage granules. The receptors for these plasma proteins on the platelet plasma membrane have been well characterized, but morphological evidence for their transport to the storage granules is not yet available. In an attempt to clarify this aspect, we employed postembedding immunocytochemistry on platelets embedded in the acrylic resin LR White. Clathrin as the major coat component of coated vesicles was localized in the cytoplasm, on the plasmic faces of alpha-granules and the open canalicular system, and on the plasmic face of the plasma membrane. Colocalizations of the adhesive proteins, von Willebrand factor, fibrinogen and fibronectin, with clathrin could be observed at the same typical locations as coated vesicles were seen in Araldite-embedded material. These colocalizations have not been reported to date and furnish further evidence for a coated vesicle-mediated transport of blood plasma-derived adhesive proteins from their receptors on the outer plasma membrane to the alpha-granules.

MeSH terms

  • Biological Transport / physiology
  • Blood Platelets / chemistry*
  • Cell Adhesion Molecules / blood*
  • Clathrin / blood*
  • Coated Vesicles / physiology*
  • Fibrinogen / analysis
  • Fibronectins / analysis
  • Humans
  • Immunohistochemistry
  • Platelet Adhesiveness / physiology*
  • von Willebrand Factor / analysis

Substances

  • Cell Adhesion Molecules
  • Clathrin
  • Fibronectins
  • von Willebrand Factor
  • Fibrinogen