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Related Experiment Videos

Evidence for an extra-cellular function for protein kinase A

S Shaltiel1, I Schvartz, B Korc-Grodzicki

  • 1Department of Chemical Immunology, Weizmann Institute of Science, Rehovot, Israel.

Molecular and Cellular Biochemistry
|November 1, 1993
PubMed
Summary
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Cyclic adenosine monophosphate-dependent protein kinase (PKA) is released from platelets and phosphorylates vitronectin in human blood. This extracellular PKA activity alters vitronectin function, impacting hemostasis and potentially PAI-1 binding.

Area of Science:

  • Biochemistry
  • Cell Biology
  • Hematology

Background:

  • Cyclic adenosine monophosphate-dependent protein kinase (PKA) is primarily known for intracellular functions.
  • Platelets release PKA, ATP, and Mg++ upon physiological stimulation.
  • Vitronectin (V) is a multifunctional protein involved in platelet activation.

Purpose of the Study:

  • To investigate the potential extracellular regulatory role of PKA in blood.
  • To identify the endogenous substrate of extracellular PKA in human serum.
  • To determine the functional consequences of vitronectin phosphorylation.

Main Methods:

  • Analysis of protein phosphorylation in human serum and plasma.
  • Characterization of the phosphorylated protein (p75) as vitronectin.

Related Experiment Videos

  • Investigation of the effect of cAMP, PKA inhibitor, and purified PKA on vitronectin phosphorylation.
  • Identification of the phosphorylation site (Ser378) and its accessibility.
  • Assessment of the impact of phosphorylation on vitronectin's interaction with PAI-1.

    • Main Results:

    • Platelet stimulation releases PKA, which phosphorylates vitronectin (p75) in serum.
    • Phosphorylation is enhanced by cAMP and blocked by PKA inhibitors.
    • Vitronectin phosphorylation occurs at Ser378, exposed in the presence of glycosaminoglycans (GAGs).
    • Phosphorylated vitronectin shows reduced binding to plasminogen activator inhibitor-1 (PAI-1).

    Conclusions:

    • PKA has a potential extracellular regulatory role in blood, phosphorylating vitronectin.
    • Vitronectin phosphorylation, modulated by GAGs, can occur at hemostatic events.
    • This phosphorylation alters vitronectin function by reducing PAI-1 binding, suggesting a role in hemostasis regulation.