Distinguishing integral and receptor-bound heat shock protein 70 (Hsp70) on the cell surface by Hsp70-specific antibodies
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Cell Stress & Chaperones journal has become a major outlet for papers and review articles about anti-heat shock protein (HSP) antibodies. In the last decade, it became evident that apart from their intracellular localization, members of the heat shock protein 90 (Hsp90; HSPC) and Hsp70 (HSPA) family are also found on the cell surface. In this review, we will focus on Hsp70 (HSPA1A), the major stress-inducible member of the human Hsp70 family. Depending on the cell type, the membrane association of Hsp70 comes in two forms. In tumor cells, Hsp70 appears to be integrated within the plasma membrane, whereas in non-malignantly transformed (herein termed normal) cells, Hsp70 is associated with cell surface receptors. This observation raises the question whether or not these two surface forms of Hsp70 in tumor and normal cells can be distinguished using Hsp70 specific antibodies. Presently a number of Hsp70 specific antibodies are commercially available. These antibodies were generated by immunizing mice either with recombinant or HeLa-derived human Hsp70 protein, parts of the Hsp70 protein, or with synthetic peptides. This review aims to characterize the binding of different anti-human Hsp70 antibodies and their capacity to distinguish between integrated and receptor-bound Hsp70 in tumor and normal cells.
KeywordsCell surface Hsp70 Hsp70 antibody epitope Integrated Hsp70 Receptor-bound Hsp70
The author wants to thank Anett Lange for excellent editorial support. This work was financially supported by the multimmune GmbH (Munich, Germany), the Deutsche Forschungsgemeinschaft (DFG; SFB824/1; DFG Cluster of Excellence: Munich-Centre for Advanced Photonics), BMBF (MOBITUM, 01EZ0826; Kompetenzverbund Strahlenforschung, 03NUK007E), and the European Union (EU-STEMDIAGNOSTICS, FP7-037703; EU-CARDIORISK, FP7-211403).
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