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

scholarly journals Preferential localization of heat shock protein 47 in dilated endoplasmic reticulum of chicken chondrocytes.

1994 ◽  
Vol 42 (7) ◽  
pp. 833-841 ◽  
Author(s):  
K Kambe ◽  
A Yamamoto ◽  
T Yoshimori ◽  
K Hirayoshi ◽  
R Ogawa ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Type Ii Collagen ◽  
Epiphyseal Cartilage ◽  
Confocal Laser ◽  
Immunogold Electron Microscopy ◽  
Type Ii ◽  
Heat Shock Protein 47 ◽  
Cultured Chondrocytes

We investigated the distribution of heat shock protein 47 (hsp47) in cultured chicken embryonic chondrocytes and epiphyseal chondrocytes of tibial bones from 1-day-old to 6-week-old chickens. Northern blot and immunoblot analyses revealed that hsp47 exists in epiphyseal cartilage and cultured chondrocytes. Confocal laser immunofluorescence microscopy showed that hsp47 was localized mainly in the many granular structures found in the cytoplasm that contain Type II collagen. Epiphyseal cartilage and cultured chondrocytes were embedded in LR White resin and hsp47 was detected by protein A-immunogold electron microscopy. Gold particles were localized exclusively in the cisternal space of the endoplasmic reticulum (ER), and the labeling density of the cisternal space of the dilated ER was always higher than that of the non-dilated ER. In all the differentiating zones of epiphyseal cartilage, the labeling density was highest in the hypertrophic cells. These findings suggest that hsp47 plays an important role(s) in the synthesis, processing, and assembly of Type II collagen.

Increased expression of collagen-binding heat shock protein 47 in murine bleomycin-induced pneumopathy

2003 ◽  
Vol 285 (4) ◽  
pp. L957-L963 ◽  
Author(s):  
Hiroshi Ishii ◽  
Hiroshi Mukae ◽  
Tomoyuki Kakugawa ◽  
Tetsuji Iwashita ◽  
Hideyuki Kaida ◽  
...  
Keyword(s):  
Heat Shock ◽  
Pulmonary Fibrosis ◽  
Heat Shock Protein ◽  
Smooth Muscle Actin ◽  
Protein A ◽  
Immunohistochemical Analysis ◽  
Rt Pcr ◽  
Heat Shock Protein 47 ◽  
Positive Type ◽  
Fibrotic Process

The 47-kDa heat shock protein 47 (HSP47) is a collagen-specific molecular chaperone that has been shown to play a major role during the processing and/or secretion of procollagen. Expression of HSP47 has been reported to increase in parallel with expression of collagens during the progression of various fibrosis models. The aim of the present study was to investigate the association between HSP47 expression and collagen accumulation in bleomycin (BLM)-induced murine fibrosis. We investigated the expression of HSP47 protein and mRNA using immunohistochemical analysis and semi-quantitative RT-PCR in murine BLM-induced pulmonary fibrosis. Immunohistochemical analysis showed that higher expression of HSP47 protein was present in BLM-induced pulmonary fibrosis compared with controls. HSP47 was localized predominantly in α-smooth muscle actin-positive myofibroblasts, F4/80 negative, surfactant protein-A-positive type II pneumocytes, and F4/80-positive macrophages. RT-PCR also demonstrated an increase of HSP47 mRNA expression in BLM-treated lungs. Moreover, the relative amounts of HSP47 mRNA correlated significantly with the lung hydroxyproline content as an indicator of pulmonary fibrosis in BLM-treated lungs ( r = 0.406, P <0.05). Our results suggest that these cells may play a role in the fibrotic process of BLM-treated lungs through upregulation of HSP47.

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.

Heat Shock Protein 47 (HSP47)

2018 ◽  
pp. 1-7
Author(s):  
Fatin Hazwani Ibrahim ◽  
Normala Abd Latip ◽  
Mohd Firdaus Abdul-Wahab
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Heat Shock Protein 47
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