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      Heat Shock Protein 47 in Renal Scarring

      a,b , b , a
      S. Karger AG
      Heat shock protein 47, Collagen, Renal scarring

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          Heat shock protein 47 (HSP47) is a collagen-binding protein, thought to play an essential mechanistic role in the assembly and processing of procollagens. HSP47 is increasingly being implicated in the pathogenesis of several human and experimental fibrotic diseases. HSP47 could mediate increased accumulation of collagens in the fibrotic mass, possibly by regulating increased assembly of procollagens. Therefore, modulation of HSP47 might be a valuable tool for manipulation of some fibrotic diseases, including renal scarring

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          Most cited references2

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          Expression and function of heat shock protein 47: a collagen-specific molecular chaperone in the endoplasmic reticulum.

          Heat shock protein (HSP) 47 is a collagen-binding stress protein localized in the endoplasmic reticulum (ER). In addition to stress-inducibility through heat shock element-heat shock factor interaction, the expression of HSP47 under normal conditions always correlates with that of collagens in various cell types and tissues. Both HSP47 and types I and III collagens are also dramatically induced under pathophysiological conditions such as liver fibrosis. HSP47 transiently associates with procollagen in the ER and dissociates from it in the cis-Golgi compartment. Possible functions of HSP47 as a molecular chaperone specific for procollagen are discussed: prevention of nascent procollagen chains from forming aggregates, effect on the modification of procollagen, inhibition of intracellular degradation of procollagen, quality control mechanisms under stress conditions, and effect on the secretion from the ER to the Golgi compartment.
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            Coexpression of Collagens and Collagen-Binding Heat Shock Protein 47 in Human Diabetic Nephropathy and IgA Nephropathy

            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.

              Author and article information

              S. Karger AG
              November 2000
              08 November 2000
              : 86
              : 3
              : 339-341
              a2nd Department of Pathology, Nagasaki University School of Medicine, Nagasaki, Japan; bDivision of Nephrology, Pennsylvania State University College of Medicine, Hershey, Pa., USA
              45790 Nephron 2000;86:339–341
              © 2000 S. Karger AG, Basel

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              Page count
              References: 26, Pages: 3
              Self URI (application/pdf): https://www.karger.com/Article/Pdf/45790
              Self URI (text/html): https://www.karger.com/Article/FullText/45790
              Self URI (journal page): https://www.karger.com/SubjectArea/Nephrology

              Cardiovascular Medicine,Nephrology
              Renal scarring,Heat shock protein 47,Collagen
              Cardiovascular Medicine, Nephrology
              Renal scarring, Heat shock protein 47, Collagen


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