scholarly journals A cDNA Encoding the Endoplasmic Reticulum-Luminal Heat-Shock Protein from Spinach (Spinacia oleracea L.)

1994 ◽  
Vol 104 (1) ◽  
pp. 303-304 ◽  
Author(s):  
J. V. Anderson ◽  
L. G. Neven ◽  
Q. B. Li ◽  
D. W. Haskell ◽  
C. L. Guy
Keyword(s):  
Endoplasmic Reticulum ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Spinacia Oleracea ◽  
Spinacia Oleracea L

scholarly journals The Endoplasmic Reticulum-resident Heat Shock Protein Gp96 Activates Dendritic Cells via the Toll-like Receptor 2/4 Pathway

2002 ◽  
Vol 277 (23) ◽  
pp. 20847-20853 ◽  
Author(s):  
Ramunas M. Vabulas ◽  
Sibylla Braedel ◽  
Norbert Hilf ◽  
Harpreet Singh-Jasuja ◽  
Sylvia Herter ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Dendritic Cells ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Toll Like Receptor ◽  
Heat Shock Protein Gp96 ◽  
Toll Like Receptor 2

scholarly journals Calreticulin, a Peptide-binding Chaperone of the Endoplasmic Reticulum, Elicits Tumor- and Peptide-specific Immunity

1999 ◽  
Vol 189 (5) ◽  
pp. 797-802 ◽  
Author(s):  
Sreyashi Basu ◽  
Pramod K. Srivastava
Keyword(s):  
Endoplasmic Reticulum ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Antigen Processing ◽  
Peptide Binding ◽  
Cd8 T Cell ◽  
T Cell Response ◽  
Specific Immunity ◽  
Per Se

Calreticulin (CRT), a peptide-binding heat shock protein (HSP) of the endoplasmic reticulum (ER), has been shown previously to associate with peptides transported into the ER by transporter associated with antigen processing (Spee, P., and J. Neefjes. 1997. Eur. J. Immunol. 27: 2441–2449). Our studies show that CRT preparations purified from tumors elicit specific immunity to the tumor used as the source of CRT but not to an antigenically distinct tumor. The immunogenicity is attributed to the peptides associated with the CRT molecule and not to the CRT molecule per se. It is further shown that CRT molecules can be complexed in vitro to unglycosylated peptides and used to elicit peptide-specific CD8+ T cell response in spite of exogenous administration. These characteristics of CRT closely resemble those of HSPs gp96, hsp90, and hsp70, although CRT has no apparent structural homologies to them.

scholarly journals Biophysical Analysis of the Endoplasmic Reticulum-Resident Chaperone/Heat Shock Protein gp96/GRP94 and Its Complex with Peptide Antigen†

Biochemistry ◽  
2001 ◽  
Vol 40 (5) ◽  
pp. 1483-1495 ◽  
Author(s):  
Nora A. Linderoth ◽  
Martha N. Simon ◽  
Natalia A. Rodionova ◽  
Martine Cadene ◽  
William R. Laws ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Peptide Antigen ◽  
Biophysical Analysis ◽  
Heat Shock Protein Gp96

scholarly journals A yeast gene important for protein assembly into the endoplasmic reticulum and the nucleus has homology to DnaJ, an Escherichia coli heat shock protein.

1989 ◽  
Vol 109 (6) ◽  
pp. 2665-2675 ◽  
Author(s):  
I Sadler ◽  
A Chiang ◽  
T Kurihara ◽  
J Rothblatt ◽  
J Way ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Endoplasmic Reticulum ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Nuclear Localization ◽  
Protein Localization ◽  
Hybrid Protein ◽  
Nuclear Localization Signals ◽  
Hybrid Proteins ◽  
Cytochrome C1

When nuclear localization sequences (termed NLS) are placed at the N terminus of cytochrome c1, a mitochondrial inner membrane protein, the resulting hybrid proteins do not assemble into mitochondria when synthesized in the yeast Saccharomyces cerevisiae. Cells lacking mitochondrial cytochrome c1, but expressing the hybrid NLS-cytochrome c1 proteins, are unable to grow on glycerol since the hybrid proteins are associated primarily with the nucleus. A similar hybrid protein with a mutant NLS is transported to and assembled into the mitochondria. To identify proteins that might be involved in recognition of nuclear localization signals, we isolated conditional-lethal mutants (npl, for nuclear protein localization) that missorted NLS-cytochrome c1 to the mitochondria, allowing growth on glycerol. The gene corresponding to one complementation group (NPL1) encodes a protein with homology to DnaJ, an Escherichia coli heat shock protein. npl1-1 is allelic to sec63, a gene that affects transit of nascent secretory proteins across the endoplasmic reticulum. Rothblatt, J. A., R. J. Deshaies, S. L. Sanders, G. Daum, and R. Schekman. 1989. J. Cell Biol. 109:2641-2652. The npl1 mutants reported here also weakly affect translocation of preprocarboxypeptidaseY across the ER membrane. A normally nuclear hybrid protein containing a NLS fused to invertase and a nucleolar protein are not localized to the nucleus in npl1/sec63 cells at the nonpermissive temperature. Thus, NPL1/SEC63 may act at a very early common step in localization of proteins to the nucleus and the ER. Alternatively, by affecting ER and nuclear envelope assembly, npl1 may indirectly alter assembly of proteins into the nucleus.

Endoplasmic reticulum stress induces the phosphorylation of small heat shock protein, Hsp27

2005 ◽  
Vol 95 (5) ◽  
pp. 932-941 ◽  
Author(s):  
Hidenori Ito ◽  
Ikuko Iwamoto ◽  
Yutaka Inaguma ◽  
Takenori Takizawa ◽  
Koh-ichi Nagata ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Heat Shock ◽  
Endoplasmic Reticulum Stress ◽  
Heat Shock Protein ◽  
Small Heat Shock Protein

Two stress proteins of the endoplasmic reticulum bind denatured collagen

1990 ◽  
Vol 68 (7-8) ◽  
pp. 1057-1061 ◽  
Author(s):  
Devki Nandan ◽  
Eric H. Ball ◽  
Bishnu D. Sanwal
Keyword(s):  
Endoplasmic Reticulum ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Protein Level ◽  
Stress Proteins ◽  
Fold Increase ◽  
Low Ph ◽  
Simple Method ◽  
Collagen Binding ◽  
Glucose Regulated Protein

A differentiation-related gelatin-binding 46 kilodalton (kDa) glycoprotein in myoblasts (GP46, colligin) shares several properties with the 78-kDa glucose-regulated protein (GRP78), including location in the endoplasmic reticulum and related C-terminal sequences. These similarities extend to stress inducibility, since we find that GP46 is a heat-shock protein; its synthesis is elevated at 42 °C, resulting in a two- to three-fold increase in protein level. Further, GRP78 is a gelatin-binding protein; together with GP46 it is retained on gelatin–Sepharose beads. GRP78 and GP46 do not interact; each protein can be individually eluted, GP46 at low pH and GRP78 by ATP. These results suggest that the proteins have distinct roles in the synthesis of collagen and point to a simple method for purification.Key words: stress proteins, collagen-binding proteins, endoplasmic reticulum, 78-kilodalton glucose-regulated protein, 46-kilodalton glycoprotein.

scholarly journals The Endoplasmic Reticulum-Resident Chaperone Heat Shock Protein 47 Protects the Golgi Apparatus from the Effects of O-Glycosylation Inhibition

PLoS ONE ◽  
2013 ◽  
Vol 8 (7) ◽  
pp. e69732 ◽  
Author(s):  
Shingo Miyata ◽  
Tatsunori Mizuno ◽  
Yoshihisa Koyama ◽  
Taiichi Katayama ◽  
Masaya Tohyama
Keyword(s):  
Endoplasmic Reticulum ◽  
Heat Shock ◽  
Golgi Apparatus ◽  
Heat Shock Protein ◽  
Heat Shock Protein 47 ◽  
Glycosylation Inhibition
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