Evidence that apoB-100 of low-density lipoproteins is a novel Src-related protein kinase. Academic Article uri icon

Overview

abstract

  • Protein-tyrosine kinases of signal transduction pathways occur and function intracellularly. In contrast, the low-density lipoprotein (LDL) particle circulates in plasma, where its function is to solubilize and transport lipid. Recently, several reports showed that LDL may have a role in signal transduction. We have identified a region in the apoB-100 primary structure which shows similarity to Src-homology-1 (SH1) domains, the kinase region of protein-tyrosine kinases. Results obtained in protein kinase assays of highly purified LDL showed that only the apoB-100 was phosphorylated, suggesting that apoB-100 has the capacity to undergo autophosphorylation like known protein-tyrosine kinases. Phosphorylation was not observed for any other apolipoprotein in LDL or for any component of high-density lipoprotein and lipoprotein [a]. Our results suggest that apoB-100 may be a novel and functional member of the src protein kinase family.

publication date

  • October 1, 1995

Research

keywords

  • Apolipoproteins B
  • Lipoproteins, LDL
  • src Homology Domains
  • src-Family Kinases

Identity

Scopus Document Identifier

  • 0028972905

PubMed ID

  • 8561859

Additional Document Info

volume

  • 14

issue

  • 7