Platelet glycohydrolase activities: Characterization and release

C. Emiliani, S. Martino, A. Orlacchio, R. Vezza, G. G. Nenci, P. Gresele

Research output: Contribution to journalArticlepeer-review


Granules containing acid hydrolases have been detected in human platelets but have not been thoroughly characterized. We have studied the activity and characteristics of glycohydrolases present in normal human platelets, evaluated their release upon stimulation with thrombin, and assessed the contribution of platelet-released lysosomal contents to the glycohydrolase activity present in normal serum. Platelets contained a remarkable glycohydrolase activity with a prevalence of β-N-acetylhexosaminidase. All glycohydrolases were released to some extent upon stimulation with thrombin and contributed to the glycohydrolase activity found in human serum. α-Mannosidase and α-galactosidase were partially inactivated after release by a mechanism as yet undefined. In addition, thrombin stimulation affects the intraplatelet isoenzyme pattern of β-N-acetylhexosaminidase by producing the appearance of a new form.

Original languageEnglish
Pages (from-to)31-39
Number of pages9
JournalCell Biochemistry and Function
Issue number1
Publication statusPublished - 1995


  • Activation
  • Human platelets
  • Isoenzymes
  • Lysosomal glycohydrolases
  • Secretion

ASJC Scopus subject areas

  • Clinical Biochemistry
  • Cell Biology


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