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

Kambe, Kenichi; Yamamoto, Akinaru; Yoshimori, Tamotsu; Hirayoshi, Kazunori; Ogawa, Ryokei; Tashiro, Yoko

doi:10.1177/42.7.8014466

Cited by 19 publications

(14 citation statements)

References 11 publications

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“…Procollagen polypeptides are found to form a complex with HSP47 in the endoplasmic reticulum which plays an important role in the intracellular processing/folding of procollagen molecules as a collagen-specific molecular chaperone [7]. The crucial role of HSP47 in regulating translocation/translation of collagen molecules has been reported elsewhere [14, 15, 16, 17, 18, 19, 20, 21]; however, its role in human kidney in relation to sclerosis/fibrosis in DN and IgAN is completely unknown.…”

Section: Discussionmentioning

confidence: 99%

“…It should be noted that while our results showed an association between HSP47 and collagen expression in sclerosis/fibrosis, no direct evidence for a causal relationship could be presented, and an exact nature of the association has yet to be defined. However, as HSP47 plays an important role(s) in the synthesis, processing and assembly of various collagens [11, 14, 15, 16, 17, 18, 19], elevated levels of HSP47 in DN and IgAN sections may play a significant role in the subsequent manifestation of glomerulosclerosis and interstitial fibrosis.…”

Section: Discussionmentioning

confidence: 99%

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Coexpression of Collagens and Collagen-Binding Heat Shock Protein 47 in Human Diabetic Nephropathy and IgA Nephropathy

Razzaque¹,

Kumatori

Harada

et al. 1998

Nephron

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The mechanism of structural changes of the kidney in human diabetic nephropathy (DN) and IgA nephropathy (IgAN) is not yet completely known, but excessive deposition of extracellular matrix (ECM), including various collagens, may be crucial to this process. Heat shock protein (HSP) 47 has been identified as collagen-binding stress protein, shown to have a specific role in the intracellular processing of procollagen molecules during collagen assembly. To determine whether increased deposition of collagens in human DN and IgAN is related to HSP47, we investigated the expression of HSP47 in renal biopsy and autopsy sections obtained from 22 DN and 45 IgAN patients. Five renal biopsy specimens, diagnosed as minor glomerular abnormalities, were simultaneously studied as controls. Monoclonal antibodies specific for HSP47, type III collagen and type IV collagen were used to assess the relative expression of their proteins in paraffin-embedded renal sections by immunohistochemistry. Increased deposition of collagens was closely related to the sclerotic activity of the disease process in DN and IgAN; increased deposition of collagens was often present in relation to a strong expression of HSP47, a stress protein known to regulate collagen synthesis/assembly. By double immunostaining, we found colocalization of collagens and their molecular chaperone HSP47 in the sclerotic glomeruli and tubulointerstitium in DN and IgAN. Our results strongly support a pathologic role for HSP47 in both these diseases and that increased levels of HSP47 may play an important role in the excessive assembly of collagens resulting in glomerulosclerosis and interstitial fibrosis found in DN and IgAN patients.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Coexpression of Collagens and Collagen-Binding Heat Shock Protein 47 in Human Diabetic Nephropathy and IgA Nephropathy

Razzaque¹,

Kumatori

Harada

et al. 1998

Nephron

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“…There are several recent reports indicating that dilated rough ER stores various materials including precursor proteins and stress proteins, all of which are under the influence of drug metabolism and/or neoplastic change. [20][21][22][23][24][25][26][27][28] Several explanations have likewise been proposed to explain why acidophilic substances are stored in the rough ER. We hypothesize that such materials form as the result of a problem in transport from the ribosome and/or rough ER for further maturation in the Golgi apparatus.…”

Section: Discussionmentioning

confidence: 99%

Aly/Aly mice: A unique model of biliary disease

et al. 1998

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An autosomal recessive murine mutation, coined ''aly/ aly'' or ''alymphoplasia,'' was recently reported. Homozygotes for aly are defective in both humoral and cellmediated immune function and have diffuse lymphoid cell infiltration of various tissues, particularly around the conduit ducts of the pancreas and salivary glands. In pilot studies in our laboratories, aly/aly mice were found to have peculiar biliary tract lesions, which were analyzed histologically and immunohistochemically in the present study. The livers of aly/aly mice older than 8 weeks consistently showed a variable lymphoid cell infiltration with lymph follicle formation in portal tracts; intrahepatic biliary epithelial cells showed various types of damage including pseudopyloric gland metaplasia and proliferative changes. In addition, the extrahepatic bile duct and intrahepatic large bile duct were found to contain an acidophilic substance in their epithelial cytoplasm. In the lumen and occasionally in the cytoplasm of these bile ducts, acidophilic crystals were also seen. Ultrastructurally, the intracytoplasmic acidophilic substances consisted of membrane-bound intracytoplasmic inclusions with homogeneous electron density, likely derived from rough endoplasmic reticulum (ER). Immunohistochemically, the cytoplasmic acidophilic substances were simultaneously positive for cystatin C, gastrin, serotonin, and somatostatin. In contrast, the acidophilic crystals did not react with any of these antibodies. These findings suggest that the intracytoplasmic acidophilic substances may contain a precursor of the peptide hormones, possibly because of defective secretion or intracellular transport. We believe that the aly/aly mouse is a useful model for the analysis of biliary metabolic events, and for studies of the interaction of the immune system and biliary destruction. (HEPATOLOGY 1998;27:1499-1507.)

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“…It was shown that HSP47 (also known as colligin, J6, gp46, and CB48) is co-expressed with collagens in cells such as fibroblasts and chondrocytes (4,5). In mouse embryo development, HSP47 is expressed mainly in mesoderm and mesoderm-derived tissues, and the expression correlates both temporally and spatially with that of type I and II collagen (6).…”

mentioning

confidence: 99%

HSP47 Binds Cooperatively to Triple Helical Type I Collagen but Has Little Effect on the Thermal Stability or Rate of Refolding

Macdonald

Bächinger

2001

Journal of Biological Chemistry

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HSP47, a collagen-specific molecular chaperone, interacts with unfolded and folded procollagens. Binding of chicken HSP47 to native bovine type I collagen was studied by fluorescence quenching and cooperative binding with a collagen concentration at half saturation (K half ) of 1.4 ؋ 10 ؊7 M, and a Hill coefficient of 4.3 was observed. Similar results are observed for the binding of mouse HSP47 recombinantly expressed in Escherichia coli. Chicken HSP47 binds equally well to native type II and type III procollagen without the carboxyl-terminal propeptide (pN type III collagen), but binding to triple helical collagen-like peptides is much weaker. Weak binding occurred to both hydroxylated and nonhydroxylated collagen-like peptides, and a significant chain length dependence was observed. Binding of HSP47 to native type I collagen had no effect on the thermal stability of the triple helix. Refolding of type I collagen in the presence of HSP47 showed minor changes, but these are probably not biologically significant. Binding of HSP47 to bovine pN type III collagen has only minor effects on the thermal stability of the triple helix and does not influence the refolding kinetics of the triple helix.HSP47 (47-kDa heat shock protein) is a rough endoplasmic reticulum protein believed to function as a collagen-specific molecular chaperone (1-3). It was shown that HSP47 (also known as colligin, J6, gp46, and CB48) is co-expressed with collagens in cells such as fibroblasts and chondrocytes (4,5). In mouse embryo development, HSP47 is expressed mainly in mesoderm and mesoderm-derived tissues, and the expression correlates both temporally and spatially with that of type I and II collagen (6). HSP47 knockout mice show an embryonic lethal phenotype (7). HSP47 is isolated easily by affinity chromatography on gelatin-Sepharose (8, 9) and was later shown to interact also with triple helical collagen types I-V (10). It was found that all these collagens have a similar affinity for HSP47 with dissociation constants of about 10 Ϫ7 M (10). The interaction of HSP47 with both unfolded and folded procollagens is unusual and distinguishes HSP47 from other molecular chaperones.A number of potential functions for HSP47 during procollagen biosynthesis have been described. HSP47 binds to nascent procollagen chains and therefore may help prevent the premature association of procollagen chains and/or assist with the translocation of procollagen chains into the rough endoplasmic reticulum (11). HSP47 also interacts with procollagen chains in the rough endoplasmic reticulum when triple helix formation is inhibited by ␣,␣Ј-dipyridyl, an inhibitor of prolyl-4-hydroxylase (9). A potential role in vesicular trafficking was explored with Brefeldin A and monensin (9,12,13). In Brefeldin A-treated cells HSP47 remained associated with procollagen, whereas in cells treated with monensin no HSP47 binding was detected.Together this shows that HSP47 seems to release procollagen on entry to the Golgi. Procollagens are not secreted as individual molecules, but ...

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

Cited by 19 publications

References 11 publications

Coexpression of Collagens and Collagen-Binding Heat Shock Protein 47 in Human Diabetic Nephropathy and IgA Nephropathy

Coexpression of Collagens and Collagen-Binding Heat Shock Protein 47 in Human Diabetic Nephropathy and IgA Nephropathy

Aly/Aly mice: A unique model of biliary disease

HSP47 Binds Cooperatively to Triple Helical Type I Collagen but Has Little Effect on the Thermal Stability or Rate of Refolding

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