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Human platelet osteonectin: release, surface expression, and partial characterization.

R J Kelm1, K G Mann

  • 1University of Vermont, College of Medicine, Department of Biochemistry, Burlington 05405.

Blood
|March 1, 1990
PubMed
Summary
This summary is machine-generated.

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Human platelets secrete osteonectin, a bone protein. Activated platelets release osteonectin, with a small amount expressed on the surface, suggesting structural differences from bone osteonectin.

Area of Science:

  • Biochemistry
  • Hematology
  • Molecular Biology

Background:

  • Osteonectin is an abundant noncollagenous bone protein.
  • Previous studies showed osteonectin is present in and secreted by human platelets.

Purpose of the Study:

  • To quantify osteonectin distribution on platelet surfaces and in supernatants after activation.
  • To investigate the structural characteristics of platelet-derived osteonectin and compare it to bone osteonectin.

Main Methods:

  • Radioimmunoassay (RIA) for fluid-phase and solid-phase measurements.
  • Platelet activation using collagen and thrombin.
  • Immunoaffinity chromatography and Western blotting.
  • Automated Edman degradation for N-terminal sequencing.

Related Experiment Videos

Main Results:

  • Osteonectin content ranged from 0.65 to 2.2 µg/10^8 platelets.
  • Platelets released up to 61% of total osteonectin upon activation with collagen and thrombin.
  • Approximately 0.8% of platelet osteonectin is expressed on the surface after activation.
  • Platelet osteonectin is a single polypeptide chain with a higher apparent molecular weight than bone osteonectin, but shares identical N-terminal sequence.

Conclusions:

  • Platelets actively secrete osteonectin in response to activation.
  • A small fraction of platelet osteonectin is exposed on the platelet surface upon activation.
  • Platelet osteonectin is structurally distinct from bone osteonectin, likely in a region distant from the N-terminus.