Heat Shock Protein 47

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Heat shock protein 47 : a chaperone for the fibrous cap?

According to The American Heritage College Dictionary,1 a chaperone is “a guide or companion whose purpose is to ensure propriety or restrict activity.” The term “molecular chaperone” is applied to proteins that control the proper folding of nascent polypeptides into the correct 3D structure (ensure propriety) or maintain polypeptides in an inactive state (restrict activity) until they have bee...

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Serum heat shock protein 47 levels in patients with drug-induced lung disease

BACKGROUND Heat shock protein (HSP) 47 is a collagen-specific molecular chaperone that is required for molecular maturation of various types of collagens. We recently reported that HSP47 serum levels were markedly higher in patients with acute exacerbations of idiopathic pulmonary fibrosis (IPF) when compared with patients with stable IPF, suggesting that serum HSP47 levels correlate with inter...

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Role of Heat Shock Protein 47 in Transdifferentiation of Human Tenon's Fibroblasts to Myofibroblasts

BACKGROUND Heat shock protein 47 (Hsp47) is a well-known molecular chaperone in collagen synthesis and maturation. The aim of this study is to investigate its putative role in the transdifferentiation of Tenon's fibroblasts to myofibroblasts. METHODS Primary cultured human Tenon's fibroblasts were exposed to transforming growth factor-β1 (TGF-β1) for up to 48 hours. The mRNA levels of Hsp47 a...

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Antisense oligonucleotide inhibition of Heat Shock Protein (HSP) 47 improves bleomycin-induced pulmonary fibrosis in rats

BACKGROUND The most common pathologic form of pulmonary fibrosis arises from excessive deposition of extracellular matrix proteins such as collagen. 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. OBJECTIVES To determine whether inhibition of HSP47 could have ben...

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ژورنال

عنوان ژورنال: Circulation

سال: 2000

ISSN: 0009-7322,1524-4539

DOI: 10.1161/01.cir.101.11.1227