scholarly journals Heat shock protein 47 and 65-kDa FK506-binding protein weakly but synergistically interact during collagen folding in the endoplasmic reticulum

2017 ◽  
Vol 292 (42) ◽  
pp. 17216-17224 ◽  
Author(s):  
Yoshihiro Ishikawa ◽  
Paul Holden ◽  
Hans Peter Bächinger
Keyword(s):  
Endoplasmic Reticulum ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Binding Protein ◽  
Heat Shock Protein 47 ◽  
Fk506 Binding Protein

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.

scholarly journals The 59 kDa FK506-binding protein, a 90 kDa heat shock protein binding immunophilin (FKBP59-HBI), is associated with the nucleus, the cytoskeleton and mitotic apparatus

1995 ◽  
Vol 108 (5) ◽  
pp. 2037-2051 ◽  
Author(s):  
M. Perrot-Applanat ◽  
C. Cibert ◽  
G. Geraud ◽  
J.M. Renoir ◽  
E.E. Baulieu
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Protein Binding ◽  
Steroid Receptors ◽  
Binding Protein ◽  
Lymphoid Cells ◽  
Confocal Laser ◽  
Mitotic Apparatus ◽  
Fk506 Binding Protein

FKBP59-HBI, a 59 kDa FK506 binding protein which binds the 90 kDa heat shock protein hsp90 and thus is a heat shock protein binding immunophilin (HBI), was originally discovered in association with unliganded steroid receptors in their heat shock protein containing heterooligomer form. It belongs to a growing family including other FKBPs which bind the immunosuppressants FK506 and rapamycin, and cyclophilins which bind cyclosporin A, all having rotamase (peptidyl-prolyl cis-trans isomerase) activity which may be involved in protein folding. Targets for drug-immunophilin complexes have been mostly studied in vivo in T lymphocytes; however, immunophilins are present in all cell types, where their role and distribution are still unknown. Here we report the localization of FKBP59-HBI in various non lymphoid cells (mouse fibroblasts (L-929), monkey kidney cells (Cos-7), Madin-Darby canine kidney epithelial cells (MDCK), and mouse neuronal cells (GT1)). Two polyclonal antipeptide antibodies directed against the C-terminal end (amino acids 441–458) (Ab 173) or the sequence 182–201 (Ab 790) of the FKBP59-HBI were used in light and confocal laser immunofluorescence. FKBP59-HBI was found in the cytoplasm and nucleus of interphase cells. Specific immunofluorescence was much stronger in the cytoplasm than in the nucleus when using Ab 173, and stronger in the nucleus than in the cytoplasm with Ab 790. Detailed observations of L-cells, which have a particularly flat morphology, showed a punctate as well as a fibrous cytoskeletal staining in the cytoplasm using antibody 173, a result which suggests interactions of FKBP59-HBI with an organized network. Colocalization experiments (using antibodies against tubulin, vimentin or actin) and use of cytoskeletal-disrupting drugs revealed partial association of FKBP59-HBI with the microtubules. Western blot experiments confirmed that the protein was present in the subcellular fractions containing either ‘soluble’ proteins released from cells exposed to NP40 detergent, or proteins released from the cytoskeleton exposed to calcium ions (i.e. in microtubule depolymerizing conditions). Exposure of cells to 1 microM FK506 and rapamycin for 1 hour did not modify significantly the staining, although rapamycin treatment rendered the network stained by 173 clearly visible. Interestingly, during mitosis FKBP59-HBI segregated from the region of the chromosomes; it mainly localized with the mitotic apparatus (centrosome, spindle and interzone separating the chromosomes), the cleavage furrow and the midbodies during cytokinesis. It appeared again as a fibrous network in the cytoplasm of the two daughters cells.(ABSTRACT TRUNCATED AT 400 WORDS)

scholarly journals Structure-Function Analysis of Squirrel Monkey FK506-Binding Protein 51, a Potent Inhibitor of Glucocorticoid Receptor Activity

Endocrinology ◽  
2005 ◽  
Vol 146 (7) ◽  
pp. 3194-3201 ◽  
Author(s):  
Wesley B. Denny ◽  
Viravan Prapapanich ◽  
David F. Smith ◽  
Jonathan G. Scammell
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Glucocorticoid Receptor ◽  
Squirrel Monkey ◽  
Inhibitory Activity ◽  
Function Analysis ◽  
Binding Protein ◽  
Heat Shock Protein 90 ◽  
Ppiase Activity ◽  
Fk506 Binding Protein

Abstract FK506-binding protein 51 (FKBP51) and FKBP52 are large molecular weight immunophilins that are part of the mature glucocorticoid receptor (GR) heterocomplex. These proteins possess peptidyl-prolyl isomerase (PPIase) and tetratricopeptide repeats (TPR) domains that are important for modulation of GR activity. A naturally occurring animal model of glucocorticoid resistance, the squirrel monkey, results from the relative overexpression of FKBP51 that renders the GR in a low-affinity state. In vitro studies demonstrated that the squirrel monkey form of FKBP51 is greater than 6-fold more potent than human FKBP51 in this respect. The goals of these studies were to determine the roles of the TPR and PPIase domains in the inhibitory activity of squirrel monkey FKBP51 and to gain insight into structural features of squirrel monkey FKBP51 responsible for potent inhibition of dexamethasone-stimulated GR activity. Mutations in the TPR of squirrel monkey FKBP51 that inhibit association with heat shock protein 90 blocked GR inhibitory activity. Mutations that abrogate the PPIase activity of squirrel monkey FKBP51 had no effect on GR inhibitory activity. Chimeras of squirrel monkey and human FKBP51 were tested to identify domains responsible for their different inhibitory potencies. Amino acid differences in domains FK1 and FK2 between squirrel monkey and human FKBP51 contribute equally to the enhanced inhibitory activity of squirrel monkey FKBP51. Furthermore, squirrel monkey FKBP51 in which either FK1 or FK2 was deleted lacked GR inhibitory activity. Thus, the potent inhibitory activity of squirrel monkey FKBP51 involves both FK domains and the heat shock protein 90-binding TPR domain.

scholarly journals Identification of cytosolic peroxisome proliferator binding protein as a member of the heat shock protein HSP70 family.

1990 ◽  
Vol 87 (14) ◽  
pp. 5293-5297 ◽  
Author(s):  
K. Alvares ◽  
A. Carrillo ◽  
P. M. Yuan ◽  
H. Kawano ◽  
R. I. Morimoto ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Binding Protein ◽  
Peroxisome Proliferator ◽  
Hsp70 Family ◽  
Heat Shock Protein Hsp70

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.

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