Evidence that apoB-100 of low-density lipoproteins is a novel src-related protein kinase

Juan Guevara, E. Timothy Walch, Henry F. Epstein, James T. Sparrow, Antonio Gotto, Natalia V. Valentinova

Research output: Contribution to journalArticle

7 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)627-631
Number of pages5
JournalJournal of Protein Chemistry
Volume14
Issue number7
DOIs
StatePublished - Oct 1995

Keywords

  • ApoB-100
  • domain
  • kinase
  • lipoproteins
  • phosphorylation

ASJC Scopus subject areas

  • Biochemistry

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