Measuring the secretion of heat shock proteins from cells

被引：38

作者：

Ireland, H. Elyse ^{[1
]}

Leoni, Francesca ^{[1
]}

Altale, Ola ^{[1
]}

Birch, Catherine S. ^{[1
]}

Coleman, Robert C. ^{[1
]}

Hunter-Lavin, Claire ^{[1
]}

Williams, John H. H. ^{[1
]}

机构：

[1] W Chester Univ, Dept Biol Sci, Chester Ctr Stress Res, Chester CH1 4BJ, Cheshire, England

来源：

METHODS | 2007年 / 43卷 / 03期

关键词：

hsp70; secretion; hsp60; necrosis; apoptosis; ELISA;

D O I：

10.1016/j.ymeth.2007.06.011

中图分类号：

Q5 [生物化学];

学科分类号：

071010 [生物化学与分子生物学]; 081704 [应用化学];

摘要：

Heat shock proteins have been shown to be secreted from a number of cell types. Necrotic cells release heat shock proteins in a passive manner, whereas we, and others, have shown that viable cells secrete Hsp70 and Hsp60 through an active mechanism involving lysosomal vesicles and lipid rafts. This release of Hsp70 and Hsp60 is regulated, for example by being increased by elevated temperature. This article outlines procedures, using Hsp70 as the example, to: ensure the status of cells (viable, apoptotic or necrotic); identify the heat shock protein secreted; and quantify the secreted protein. Hsp70 has previously been quantified by ELISA, but newer methods are now being adopted, such as BIAcore and bead-based assays for use by FACS. These methods have the advantages of being more sensitive and requiring less sample than ELISA. The BIAcore has the potential to analyse Hsp70 ligands and provide affinity constants. The FACS bead assay system can be used to run multiplex assays. (C) 2007 Published by Elsevier Inc.

引用

页码：176 / 183

页数：8

共 40 条

[1]

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[2]

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