Purification of thrombospondin receptor (CD36) from human platelet membrane

Abstract

Thrombospondin receptor (CD36) has been recently identified in platelets and various cell lines as the receptor for thrombospondin, an adhesive protein required for irreversible aggregation of platelets as well as other adhesive processes. Thrombospondin receptor, one of major glycosylated platelet membrane proteins, is thought to play an important role as a cell adhesion molecule in blood coagulation system as well as intercellular signaling. In this work, thrombospondin receptor was purified to homogeneity from human platelet by wheat germ agglutinin (WGA)-affinity chromatography and size exclusion chromatography on Ultrogel-AcA44. The molecular weight of the purified thrombospondin receptor was about 88 kDa on SDS-PAGE and its identity was confirmed by immunoblot analysis and immunodiffusion assay.

Cell-membrane engineering strategies for clinic-guided design of nanomedicine

“…1 The aggregation and adhesion of platelets involves the receptor protein of CD36. 2,3 Besides, various inflammatory factors on the surface of monocytes drive them towards inflammatory sites. [4][5][6][7] Currently, various nanoparticles (NPs) as drug carriers, imaging probes, or therapeutic agents have been widely applied for disease diagnose and therapy, [8][9][10][11] called "nanomedicine".…”