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The 170-kDa glucose-regulated stress protein is an endoplasmic reticulum protein that binds immunoglobulin.
Open accessAbstract
Anoxia, glucose starvation, calcium ionophore A23187, EDTA, glucosamine, and several other conditions that adversely affect the function of the endoplasmic reticulum (ER) induce the synthesis of the glucose-regulated class of stress proteins (GRPs). The primary GRPs induced by these stresses migrate at 78 and 94 kDa (GRP78 and GRP94). In addition, another protein of approximately 150-170 kDa (GRP170) has been previously observed and is coordinately induced with GRP78 and GRP94. To characterize this novel stress protein, we have prepared an antisera against purified GRP170. Immunofluorescence, Endoglycosidase H sensitivity, and protease resistance of this protein in microsomes indicates that GRP170 is an ER lumenal glycoprotein retained in a pre-Golgi compartment. Immunoprecipitation of GRP170 with our antibody coprecipitates the GRP78 (also referred to as the B cell immunoglobulin-binding protein) and GRP94 members of this stress protein family in Chinese hamster ovary cells under stress conditions. ATP depletion, by immunoprecipitation in the presence of apyrase, does not affect the interaction between GRP78 and GRP170 but results in the coprecipitation of an unidentified 60-kDa protein. In addition, GRP170 is found to be coprecipitated with immunoglobulin (Ig) in four different B cell hybridomas expressing surface IgM, cytoplasmic Ig light chain only, cytoplasmic Ig heavy chain only, or an antigen specific secreted IgG. In addition, in IgM surface expressing WEHI-231 B cells, anti-IgM coprecipitates GRP78, GRP94, as well as GRP170; antibodies against GRP170 and GRP94 reciprocally coprecipitate GRP94/GRP170 as well as GRP78. Results suggest that this 170-kDa GRP is a retained ER lumenal glycoprotein that is constitutively present and that may play a role in immunoglobulin folding and assembly in conjunction or consecutively with GRP78 and GRP94.
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Hendershot, L., Bole, D., Köhler, G., & Kearney, J. F. (1987) · The Journal of cell biology · doi:10.1083/jcb.104.3.761 · Cited by 340
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Toussaint, O., Medrano, E. E., & von Zglinicki, T. (2000) · Experimental Gerontology · doi:10.1016/s0531-5565(00)00180-7 · Cited by 713
Protein Glucosylation and Its Role in Protein Folding
Parodi, A. J. (2000) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.69.1.69 · Cited by 658
Role and regulation of the ER chaperone BiP
Gething, M.-J. (1999) · Seminars in Cell & Developmental Biology · doi:10.1006/scdb.1999.0318 · Cited by 555
Protein Quality Control in the Cytosol and the Endoplasmic Reticulum: Brothers in Arms
Buchberger, A., Bukau, B., & Sommer, T. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.10.001 · Cited by 483
Metadata
- Authors
- Lin, H. Y., Masso-Welch, P., Di, Y. P., Cai, J. W., Shen, J. W., & Subjeck, J. R.
- Venue
- Molecular Biology of the Cell
- Published
- 1993-11
- Volume
- 4
- Issue
- 11
- Pages
- 1109-1119
- ISSN
- 1059-1524 (ISSN-L)
- 1939-4586
- OpenAlex
- W2130106768
- Cited by
- 161
- References
- 1
- FWCI
- 1.19
- Type
- journal article
- Language
- en
- Open access
- green
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- Lin, H. Y., Masso-Welch, P., Di, Y. P., Cai, J. W., Shen, J. W., & Subjeck, J. R. (1993). The 170-kDa glucose-regulated stress protein is an endoplasmic reticulum protein that binds immunoglobulin. Molecular Biology of the Cell. https://doi.org/10.1091/mbc.4.11.1109
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