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Intracellular Trafficking, Localization, and Mobilization of Platelet-Borne Thiol Isomerases
Author(s) -
Marilena Crescente,
Fred G. Pluthero,
Ling Li,
Richard Lo,
Tony G. Walsh,
Michael P. Schenk,
LisaMarie Holbrook,
Silvia Louriero,
Marfoua S. Ali,
Sakthivel Vaiyapuri,
Hervé Falet,
Ian M. Jones,
Alastair W. Poole,
Walter H.A. Kahr,
Jonathan M. Gibbins
Publication year - 2016
Publication title -
arteriosclerosis thrombosis and vascular biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.007
H-Index - 270
eISSN - 1524-4636
pISSN - 1079-5642
DOI - 10.1161/atvbaha.116.307461
Subject(s) - endoplasmic reticulum , protein disulfide isomerase , microbiology and biotechnology , calnexin , secretory pathway , platelet , biochemistry , platelet activation , chemistry , calreticulin , subcellular localization , brefeldin a , biology , golgi apparatus , cytoplasm , immunology
Thiol isomerases facilitate protein folding in the endoplasmic reticulum, and several of these enzymes, including protein disulfide isomerase and ERp57, are mobilized to the surface of activated platelets, where they influence platelet aggregation, blood coagulation, and thrombus formation. In this study, we examined the synthesis and trafficking of thiol isomerases in megakaryocytes, determined their subcellular localization in platelets, and identified the cellular events responsible for their movement to the platelet surface on activation.

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