Use of D-erythro-sphingosine as a pharmacological inhibitor of protein kinase C in human platelets.
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Summary
An approach for the use of sphingosine and other parameters for determining biological activities of protein kinase C is developed, found to be a potent inhibitor of gamma-thrombin-induced aggregation and secretion of washed human platelets.
- Type
- article
- Published
- 1990-12-31
- Cited by
- 31
- References
- 0
- Access
- Open access
- OpenAlex
- https://openalex.org/W1881875906
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:20667774
Keywords
Sphingosine, Platelet, Sphingosine kinase, Protein kinase C, Biochemistry
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Cited by
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- Effects of sphingosine and other sphingolipids on protein kinase C.
- Tracking Sphingosine Metabolism and Transport in Sphingolipidoses: NPC1 Deficiency as a Test Case
- Principles of bioactive lipid signalling: lessons from sphingolipids
- Identification of Ammonium Ion and 2,6-Bis(ω-aminobutyl)- 3,5-diiminopiperazine as Endogenous Factors That Account for the “Burst” of Sphingosine upon Changing the Medium of J774 Cells in Culture*
- Effects of sphingosine stereoisomers on P-glycoprotein phosphorylation and vinblastine accumulation in multidrug-resistant MCF-7 cells.
- Modulation of cell growth and differentiation by ceramide
- Na+/H+ exchange activity induced by thrombin is not inhibited by protein kinase inhibitors, staurosporine, K-252a, H-7 and sphingosine, in human platelets.
- Dual modulation of protein kinase C activity by sphingosine.
- Protein kinase C: cellular target of the second messenger arachidonic acid?
- Sphingolipid breakdown products: anti-proliferative and tumor-suppressor lipids.
- Perturbation of the platelet plasma membrane is not sufficient for inhibition of thrombin-induced PKC-activity.
- Partial Inhibition of Multidrug Resistance by Safingol Is Independent of Modulation of P-glycoprotein Substrate Activities and Correlated with Inhibition of Protein Kinase C (*)
- Sphingosine mobilizes intracellular calcium in human neutrophils.
- The effect of long-chain bases on polysialic acid-mediated membrane interactions.
- Ceramides modulate protein kinase C activity and perturb the structure of Phosphatidylcholine/Phosphatidylserine bilayers.
- C6-ceramide maintains elevated cytosolic calcium levels in activated platelets.
- A functional homolog of mammalian protein kinase C participates in the elicitor-induced defense response in potato.
- Increased levels of protein kinase C in lymphocytes in asthma: possible mechanism of regulation.
- LIGHT MODULATION OF CELL FUNCTION
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