Thromb Haemost 2000; 83(01): 157-164
DOI: 10.1055/s-0037-1613772
Commentary
Schattauer GmbH

Platelets Release their Lysosomal Content In Vivo in Humans upon Activation

Silvia Ciferri
1   From the Institute of Internal and Vascular Medicine, University of Perugia, Italy
2   Department of Cellular and Molecular Biology, University of Perugia, Italy
,
Carla Emiliani
2   Department of Cellular and Molecular Biology, University of Perugia, Italy
,
Giuseppe Guglielmini
1   From the Institute of Internal and Vascular Medicine, University of Perugia, Italy
,
Antonio Orlacchio3
1   From the Institute of Internal and Vascular Medicine, University of Perugia, Italy
,
Giuseppe G. Nenci
1   From the Institute of Internal and Vascular Medicine, University of Perugia, Italy
,
Paolo Gresele
1   From the Institute of Internal and Vascular Medicine, University of Perugia, Italy
› Author Affiliations
Further Information

Publication History

Received 31 December 1998

Accepted after resubmission 27 August 1999

Publication Date:
06 December 2017 (online)

Summary

Platelets contain, besides α- and δ-granules, lysosomes which store glycohydrolases able to degrade glycoproteins, glycolipids and glycosaminoglycans. While several studies have shown that α- and δ-granule secretion takes place “in vivo” in humans upon platelet activation, no data are available on the “in vivo” release of lysosomes. We have studied the release of platelet lysosomal contents “in vivo” in healthy volunteers at a localized site of platelet activation by measuring markers of lysosomal secretion in the blood oozing from a skin wound inflicted for the measurement of the bleeding-time. The levels of β-N-acetylhexosaminidase (Hex) were 13.1 ± 0.85 mU/ml in bleedingtime blood and 10.2 ± 0.66 mU/ml in plasma (p <0.001). Hex in serum was 16.4 ± 0.72 mU/ml. The levels of β-galactosidase were also higher in bleeding-time blood than in plasma (0.85 ± 0.07 mU/ml vs 0.4 ± 0.05 mU/ml, p <0.001). In bleeding-time blood collected at one minute intervals, Hex rose progressively consistent with ongoing platelet activation and flow-cytometry showed a progressive increase of the expression of LIMP and LAMP-2, two lysosomal associated proteins. In conclusion, our data demonstrate that platelet lysosomal glycohydrolases are released “in vivo” in humans upon platelet activation.

3 Present address: Centre for Research in Neurodegenerative Diseases, University of Toronto, Ontario (Canada).


Presented in part at the XVIth Congress of the International Society on Thrombosis and Haemostasis, Florence, Italy, June 1997 and at the XVth Congress of the Italian Society on Haemostasis and Thrombosis, Naples, Italy, September 1998.


 
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