The DOI matches its Crossref record; 24 of the 24 references it cites were found in a registry or an index.
Regulation of protein kinase C by lysophospholipids. Potential role in signal transduction.
Open accessAbstract
Certain lysophospholipids, lysophosphatidylcholine (lyso-PC) in particular, stimulated protein kinase C at low concentrations (less than 20 microM) but, conversely, inhibited it at high concentrations (greater than 30 microM). Protein kinase C stimulation by lyso-PC required the presence of phosphatidylserine (PS) and Ca2+ and was associated with a decreased Ka for PS and increased Ka for Ca2+ of the enzyme. Cardiolipin and phosphatidic acid could partially substitute for PS in supporting the stimulatory effect of lyso-PC. Lyso-PC also biphasically regulated protein kinase C activated by diolein. Of several synthetic lyso-PC preparations tested, the oleoyl, myristoyl and palmitoyl derivatives were most active. Data from the Triton X-100 mixed micellar assay indicated that 1.4 and 14.0 mol of lyso-PC/micelle produced a maximal stimulation and a complete abolishment of the stimulation of protein kinase C, respectively. Protein kinase C stimulation by lyso-PC, with a pH optimum of about 7.5, was observed for phosphorylation of histone H1, myelin basic protein, and the 35- and 47-kDa proteins from the rat brain, but not for that of other histone subfractions and protamine. Lyso-PC acted synergistically with diacylglycerol in stimulating protein kinase C, whereas the stimulation by lyso-PC was additive to that by oleic acid. Protein kinase C inhibitors (alkyllysophospholipid, sphingosine, tamoxifen, and polymyxin B) inhibited more potently the protein kinase C activity stimulated by PS/Ca2+/lyso-PC than that stimulated by PS/Ca2+. The stimulatory and inhibitory effects of lyso-PC were not observed for myosin light chain kinase and cAMP-dependent protein kinase, indicating a specificity of its actions. The present findings suggested that lyso-PC, likely derived from membrane PC by the action of phospholipase A2, might play a role in signal transduction via a dual regulation of protein kinase C, and that it could further modulate the enzyme and hence the cellular activity by interplaying with diacylglycerol and unsaturated fatty acid, the two other classes of cellular mediators also shown to be activators of protein kinase C.
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Cites
The role of protein kinase C in cell surface signal transduction and tumour promotion
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Calcium-dependent activation of a multifunctional protein kinase by membrane phospholipids.
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Lysosphingolipids Inhibit Protein Kinase C: Implications for the Sphingolipidoses
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Potential Role of Phospholipases in Virulence and Fungal Pathogenesis
Ghannoum, M. A. (2000) · Clinical Microbiology Reviews · doi:10.1128/cmr.13.1.122 · Cited by 818
Merrill, A. H., & Stevens, V. L. (1989) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/0167-4889(89)90152-3 · Cited by 280
Parhami, F., Fang, Z. T., Fogelman, A. M., Andalibi, A., Territo, M. C., & Berliner, J. A. (1993) · Journal of Clinical Investigation · doi:10.1172/jci116590 · Cited by 257
Harrison, D. G., & Ohara, Y. (1995) · The American Journal of Cardiology · doi:10.1016/0002-9149(95)80018-n · Cited by 163
Vitamin E Inhibits Lysophosphatidylcholine-Induced Endothelial Dysfunction and Platelet Activation
Murohara, T., Ikeda, H., Katoh, A., Takajo, Y., Otsuka, Y., Haramaki, N., & Imaizumi, T. (2002) · Antioxidants & Redox Signaling · doi:10.1089/152308602760598945 · Cited by 19
Metadata
- Authors
- Oishi, K., Raynor, R. L., Charp, P. A., & Kuo, J. F.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1988-05
- Volume
- 263
- Issue
- 14
- Pages
- 6865-6871
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1507801782
- Cited by
- 267
- References
- 24
- FWCI
- 9.78
- Type
- journal article
- Language
- en
- Open access
- hybrid
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