DROBNIK, W and MOLLERS, C and RESINK, T and SCHMITZ, G (1995) ACTIVATION OF PHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE-C IN RESPONSE TO HDL(3) AND LDL IS MARKEDLY REDUCED IN CULTURED FIBROBLASTS FROM TANGIER PATIENTS. ARTERIOSCLEROSIS THROMBOSIS AND VASCULAR BIOLOGY, 15 (9). pp. 1369-1377. ISSN 1079-5642,
Full text not available from this repository.Abstract
We compared HDL(3)- and LDL-induced signal transduction in normal and Tangier fibroblasts to elucidate whether impaired signal transduction responses to lipoproteins might contribute to disturbed cellular lipid and lipoprotein metabolism in Tangier disease, a rare autosomal disorder of cellular lipid and lipoprotein metabolism. In several cell types HDL and LDL activate a currently unknown isoform of phosphatidylinositol-specific phospholipase C (PI-PLC) that results in the generation of 1,2-diacylglycerol and inositol 1,4,5-trisphosphate. Compared with normal fibroblasts, Tangier fibroblasts stimulated with HDL(3) or LDL resulted in a significantly reduced accumulation of inositol phosphates and 1,2-diacylglycerol formation. Furthermore, in Tangier fibroblasts both lipoproteins failed to mobilize calcium from internal pools, and the cytosol-to-membrane redistribution of protein kinase C (in both the alpha and epsilon isoforms) was markedly reduced. Thus, the data indicate an impaired PI-PLC activation in response to lipoproteins in Tangier fibroblasts.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | PROTEIN-KINASE-C; FREE-FLOW ISOTACHOPHORESIS; HIGH-DENSITY LIPOPROTEINS; SMOOTH-MUSCLE CELLS; INOSITOL PHOSPHATES; RECEPTOR ACTIVATION; A-I; CHOLESTEROL; DISEASE; METABOLISM; SIGNAL TRANSDUCTION; TANGIER DISEASE; LIPOPROTEINS; PROTEIN KINASE C; CALCIUM |
| Depositing User: | Dr. Gernot Deinzer |
| Last Modified: | 19 Oct 2022 08:37 |
| URI: | https://pred.uni-regensburg.de/id/eprint/52326 |
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