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Platelet glycohydrolase activities: characterization and release

C Emiliani1, S Martino, A Orlacchio

  • 1Dipartimento di Biologia Cellulare e Molecolare, Università di Perugia, Italy.

Cell Biochemistry and Function
|March 1, 1995
PubMed
Summary

Human platelets contain significant glycohydrolase activity, particularly beta-N-acetylhexosaminidase. Thrombin stimulation releases these enzymes into serum, with some undergoing inactivation and altered isoenzyme patterns.

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Area of Science:

  • Biochemistry
  • Hematology
  • Cell Biology

Background:

  • Human platelets contain granules with acid hydrolases, but their specific characteristics and roles remain incompletely understood.
  • Glycohydrolases are enzymes crucial for cellular processes, and their presence and release from platelets warrant detailed investigation.

Purpose of the Study:

  • To characterize the activity and properties of glycohydrolases within normal human platelets.
  • To evaluate the release of these platelet glycohydrolases upon thrombin stimulation.
  • To determine the contribution of platelet-derived lysosomal contents to serum glycohydrolase activity.

Main Methods:

  • Analysis of glycohydrolase activity in normal human platelets.
  • Assessment of enzyme release following thrombin stimulation of platelets.

Related Experiment Videos

  • Quantification of glycohydrolase activity in human serum before and after platelet activation.

    • Main Results:

    • Human platelets exhibit substantial glycohydrolase activity, with beta-N-acetylhexosaminidase being the most prevalent.
    • Thrombin stimulation induced the release of all studied glycohydrolases from platelets to varying degrees.
    • Platelet-released enzymes contributed significantly to the overall glycohydrolase activity observed in normal human serum.
    • Alpha-mannosidase and alpha-galactosidase showed partial inactivation post-release, a mechanism requiring further elucidation.
    • Thrombin stimulation altered the intraplatelet isoenzyme profile of beta-N-acetylhexosaminidase, leading to the emergence of a novel form.

    Conclusions:

    • Human platelets are a significant source of serum glycohydrolases, particularly beta-N-acetylhexosaminidase.
    • Platelet activation by thrombin releases these enzymes, influencing serum enzymatic composition.
    • The observed post-release inactivation and isoenzyme modification highlight complex regulatory mechanisms of platelet enzymes.