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Review
. 2020 Apr;18(4):771-780.
doi: 10.1111/jth.14730. Epub 2020 Jan 29.

Structure and function of the ubiquitin-proteasome system in platelets

Lisa Colberg  1   2 , Clemens Cammann  1 , Andreas Greinacher  2 , Ulrike Seifert  1
Affiliations
Free article
Review

Structure and function of the ubiquitin-proteasome system in platelets

Lisa Colberg et al. J Thromb Haemost. 2020 Apr.
Free article

Abstract

Platelets are small anucleate blood cells with a life span of 7 to 10 days. They are main regulators of hemostasis. Balanced platelet activity is crucial to prevent bleeding or occlusive thrombus formation. Growing evidence supports that platelets also participate in immune reactions, and interaction between platelets and leukocytes contributes to both thrombosis and inflammation. The ubiquitin-proteasome system (UPS) plays a key role in maintaining cellular protein homeostasis by its ability to degrade non-functional self-, foreign, or short-lived regulatory proteins. Platelets express standard and immunoproteasomes. Inhibition of the proteasome impairs platelet production and platelet function. Platelets also express major histocompatibility complex (MHC) class I molecules. Peptide fragments released by proteasomes can bind to MHC class I, which makes it also likely that platelets can activate epitope specific cytotoxic T lymphocytes (CTLs). In this review, we focus on current knowledge on the significance of the proteasome for the functions of platelets as critical regulators of hemostasis as well as modulators of the immune response.

Keywords: MHC class I; antigen presentation; platelet activation; proteasome endopeptidase complex; ubiquitin.

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References

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