Prostaglandin-E1- and Sodium Nitroprusside-Regulated Protein Phosphorylation in Platelets

  • Maria Nieberding
  • Rainer Waldmann
  • Ulrich Walter
Conference paper
Part of the NATO ASI Series book series (NSSA, volume 135)


A variety of agents like ADP, collagen, thrombin, platelet-activating- factor (PAF)* and others activate platelets with a concomitant increase in the phosphorylation of myosin light chain (Mr 20 K) and of a soluble protein with apparent Mr of 44 K 1,2. Certain vasodilators such as cGMP-elevating agents (SNP, nitroglycerin) and cAMP-elevating agents (PGE1 PGI2) are able to inhibit platelet activation and the activation-associated protein phosphorylation 1,2. Since cAK and cGK may mediate the effects of cyclic nucleotide-regulating agents in platelets, we have now compared the vasodilator-regulated protein phosphorylation observed in intact platelets with the cyclic nucleotide stimulated protein phosphorylation found in platelet membranes 3,4. The results show for at least one phosphoprotein that the SNP-and PGE1 -stimulated protein phosphorylation is mediated by cGK and cAK, respectively.


Protein Phosphorylation Myosin Light Chain Cyclic Nucleotide Platelet Membrane Inhibit Platelet Activation 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.





sodium nitroprusside




prostaglandin I2


cAMP-dependent protein kinase


cGMP-dependent protein kinase






inositol triphosphate


1, 2 discylglycerol


protein kinase C




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Copyright information

© Plenum Press, New York 1987

Authors and Affiliations

  • Maria Nieberding
    • 1
  • Rainer Waldmann
    • 1
  • Ulrich Walter
    • 1
  1. 1.Labor für Klinische BiochemieMedizinische Univ.-Klinik WürzburgWürzburgGermany

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