Altmeyer, A., Maki, R. G., Feldweg, A. M., Heike, M., Protopopov, V. P., Masur, S. K., Srivastava, P. K. (August 1996) Tumor-specific cell surface expression of the-KDEL containing, endoplasmic reticular heat shock protein gp96. Int J Cancer, 69 (4). pp. 340-9. ISSN 0020-7136 (Print)0020-7136 (Linking)
Abstract
Heat shock protein (HSP) gp96/grp94 contains a signal peptide at the amino terminus and a -KDEL sequence at the carboxy terminus and is a major component of the lumen of the mammalian endoplasmic reticulum (ER). We show, by a number of immunolocalization methods using light and electron microscopy, that a significant proportion of intact gp96 molecules is also expressed on the cell surface. Surface gp96 molecules truly represent surface expression and do not result from adventitious deposition of gp96 released by dead cells on to the live cells in culture. Cell surface expression of gp96 is enhanced by heat shock and exposure to reducing agents. Gp96 molecules are not released from plasma membranes by repeated salt washes, and gp96 is not an integral membrane protein. Our observations suggest that gp96 and perhaps other HSPs are anchored to the cell surface as part of larger molecular complexes, which also transport them to the cell surface.
Item Type: | Paper |
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Uncontrolled Keywords: | Amino Acid Sequence Animals Antigens, Neoplasm/*analysis Cell Membrane/chemistry Embryo, Mammalian Fibroblasts/chemistry Fibrosarcoma/*chemistry Flow Cytometry Fluorescent Antibody Technique, Indirect Mercaptoethanol/pharmacology Mice Mice, Inbred BALB C Microscopy, Immunoelectron Molecular Sequence Data Oligopeptides/*analysis *Protein Sorting Signals Tumor Cells, Cultured |
Subjects: | diseases & disorders > cancer > cancer types > sarcoma |
CSHL Authors: | |
Communities: | CSHL labs > Maki lab |
Depositing User: | Matt Covey |
Date: | 22 August 1996 |
Date Deposited: | 26 Oct 2016 21:32 |
Last Modified: | 26 Oct 2016 21:32 |
Related URLs: | |
URI: | https://repository.cshl.edu/id/eprint/33640 |
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