The 170-kDa glucose-regulated stress protein is an endoplasmic reticulum protein that binds immunoglobulin.

Lin, Hung Yun; Masso-Welch, Patricia A.; Di, Y. Peter; Cai, Jei Wei; Sakata, Jun; Subjeck, John R.

doi:10.1091/mbc.4.11.1109

Cited by 160 publications

(130 citation statements)

References 42 publications

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“…Less is understood at the molecular level of grp170 structure and function; however, cellular studies have shown that it binds to Ig chain in the ER, may be the ATPase responsible for protein import into the ER, and actively binds peptides from TAP (i.e., the transporter associated with Ag processing; Refs. 11,19,20,23,24).…”

Section: Discussionmentioning

confidence: 99%

Characterization of Heat Shock Protein 110 and Glucose-Regulated Protein 170 as Cancer Vaccines and the Effect of Fever-Range Hyperthermia on Vaccine Activity

Wang¹,

Kazim²,

Repasky

et al. 2001

The Journal of Immunology

149

106

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Several studies have confirmed that certain stress proteins can function as potent vaccines against a specific cancer when purified from the same tumor. Recent studies of two long-recognized but unstudied stress proteins, heat shock protein (hsp) 110 and glucose-regulated protein (grp) 170, have shown them to be efficient peptide chain-binding proteins. The present investigation examines the vaccine potential of hsp110 and grp170. First, it is shown that prior vaccination with hsp110 or grp170 purified from methylcholanthrene-induced fibrosarcoma caused complete regression of the tumor. In a second tumor model, hsp110 or grp170 purified from Colon 26 tumors led to a significant growth inhibition of this tumor. In addition, hsp110 or grp170 immunization significantly extended the life span of Colon 26 tumor-bearing mice when applied after tumor transplantation. A tumor-specific cytotoxic T lymphocyte response developed in the mice immunized with tumor-derived hsp110 or grp170. Furthermore, treatments of the mice with bone marrow-derived dendritic cells pulsed with these two proteins from tumor also elicited a strong antitumor response. Last, we showed that mild, fever-like hyperthermic conditions enhance the vaccine efficiency of hsp110 as well as heat shock cognate 70, but not grp170. These studies indicate that hsp110 and grp170 can be used in hsp-based cancer immunotherapy, that Ag-presenting dendritic cells can be used to mediate this therapeutic approach, and that fever-level hyperthermia can significantly enhance the vaccine efficiency of hsps.

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Section: Discussionmentioning

confidence: 99%

Characterization of Heat Shock Protein 110 and Glucose-Regulated Protein 170 as Cancer Vaccines and the Effect of Fever-Range Hyperthermia on Vaccine Activity

Wang¹,

Kazim²,

Repasky

et al. 2001

The Journal of Immunology

149

106

View full text Add to dashboard Cite

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“…An anti-GRP170 antibody, prepared and characterized in this laboratory [9], was used to screen a hamster 2gtl 1 expression library. Four positive clones were identified and all of their cDNAs were found to hybridize, on a Northern blot of total RNA, to an anoxia-inducible message of approximately 4 kb.…”

Section: Resultsmentioning

confidence: 99%

“…Two of the principal members of this family, grp78 and grp94 (of 78 and 94 kDa), are resident in the endoplasmic reticulum under normal conditions and have been strongly implicated in the processing of proteins traversing the secretory pathway [4~7]. In addition to these two grps, a third grp of approximately 150 to 170 kDa has been long observed, but has only recently been characterized [9]. Biochemical analysis of grpl70 indicates that, like grp78 and grp94, it may also be involved in the processing of proteins in the secretory pathway.…”

Section: Discussionmentioning

confidence: 99%

“…Approximately 2 x 106 primary plaques were screened with the anti-CHO grp170 polyclonal antibody [9]. Positive clones were identified and inserts were isolated using appropriate restriction enzymes and subcloned into pBluescriptIIKS (Stratagene, La Jolla, CA).…”

Section: Cdna Expression Library Screeningmentioning

confidence: 99%

“…However, it has only recently been stud- ied in detail. This protein has been found to be complexed with immunoglobulin in several human and mouse cell lines, regardless of the type of immunoglobulin chain(s) produced [9] and therefore may, like grp78 and 94, function as a molecular chaperone in the protein secretion pathway.…”

Section: Introductionmentioning

confidence: 99%

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The 170 kDa glucose regulated stress protein is a large HSP70‐ HSP110‐like protein of the endoplasmic reticulum

Chen

Easton

et al. 1996

FEBS Letters

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The existence of a family of unusually large and highly diverged hsp70-1ike proteins (the hspll0/SSE family) has recently been described. The 170 kDa glucose regulated stress protein (grpl70) is a retained endoplasmic reticulum glycoprotein that may be involved in immunoglobulin folding and/or assembly. We describe here the cloning of the cDNA for grpl70 and show that it, like hspll0, is a large and highly diverged hsp70-1ike polypeptide which shares specific features with hsp70 (the dnaK family) and the hspll01SSE family, while also differing from both. Grpl70 contains an ATP binding domain and binds ATP, it possesses a carboxyl terminal NDEL sequence, and its mRNA is anoxia inducible.

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Accumulation of Misfolded Protein Aggregates Leads to the Formation of Russell Body-like Dilated Endoplasmic Reticulum in Yeast

Umebayashi

Hirata

Fukuda

et al. 1997

Yeast

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RNAP‐I, an aspartic proteinase from a filamentous fungus Rhizopus niveus, is secreted very efficiently in Saccharomyces cerevisiae. It is synthesized first as a precursor form with signal sequence and prosequence in its amino‐terminus. Our previous study indicated that the prosequence of RNAP‐I had important roles in its correct folding and secretion in yeast, and that a prosequence‐deleted derivative of RNAP‐I, Δpro, was not secreted but was retained and degraded in the yeast endoplasmic reticulum (ER). In the present study, we show that the accumulation of Δpro in the yeast ER caused elevated synthesis of ER resident chaperones, indicating that Δpro is recognized as an unfolded protein species in the ER. Our biochemical data demonstrated that Δpro formed aggregates which contained BiP, but not protein disulfide isomerase (PDI), in the ER. Immunoelectron microscopical analysis revealed that the Δpro aggregates were indeed visible as electron‐dense regions in the ER and nuclear envelope. Such ‘chaperone‐associated misfolded protein bodies’ were observed for the first time in yeast. Morphologies of the ER and nucleus were drastically altered by the accumulation of the Δpro aggregates. The ER lost its flat cisternal shape; the ER lumen extended aberrantly and the ER membrane irregularly proliferated. The misfolded Δpro proteins are probably sorted from the ordinary ER lumen to form the aggregates so that the ER function would not be grossly impaired, and the dilated ER may represent an ER subcompartment where the Δpro aggregates are degraded. © 1997 by John Wiley & Sons, Ltd.

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The 170-kDa glucose-regulated stress protein is an endoplasmic reticulum protein that binds immunoglobulin.

Cited by 160 publications

References 42 publications

Characterization of Heat Shock Protein 110 and Glucose-Regulated Protein 170 as Cancer Vaccines and the Effect of Fever-Range Hyperthermia on Vaccine Activity

Characterization of Heat Shock Protein 110 and Glucose-Regulated Protein 170 as Cancer Vaccines and the Effect of Fever-Range Hyperthermia on Vaccine Activity

The 170 kDa glucose regulated stress protein is a large HSP70‐ HSP110‐like protein of the endoplasmic reticulum

Accumulation of Misfolded Protein Aggregates Leads to the Formation of Russell Body-like Dilated Endoplasmic Reticulum in Yeast

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