Evidence that apoB-100 of low-density lipoproteins is a novelsrc-related protein kinase |
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Authors: | Juan Guevara Jr E Timothy Walch Henry F Epstein James T Sparrow Antonio M Gotto and Natalia V Valentinova |
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Institution: | (1) Department of Medicine, Baylor College of Medicine, 77030 Houston, Texas;(2) Department of Neurology, Baylor College of Medicine, 77030 Houston, Texas |
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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 thesrc protein kinase family. |
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Keywords: | ApoB-100 lipoproteins kinase domain phosphorylation |
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