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Hsp27 acts as a master molecular chaperones and plays an essential role in hepatocellular carcinoma metastasis

ABSTRACT: Hsp27 can regulate multiply signaling pathway and protect HCC cells apoptosis by mediating interaction with its cochaperones

ORGANISM(S): Homo sapiens

PROVIDER: GSE38080 | GEO | 2012/05/22

SECONDARY ACCESSION(S): PRJNA167296

REPOSITORIES: GEO

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Hsp27 acts as a master molecular chaperones and plays an essential role in hepatocellular carcinoma metastasis

Project description:Hsp27 can regulate multiply signaling pathway and protect HCC cells apoptosis by mediating interaction with its cochaperones 3 HepG2 samples stably transfected with Hsp27 ORF vectors, Hsp27 shRNA or control vectors

2012-05-21 | E-GEOD-38080 | biostudies-arrayexpress

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HSP27 3A vs WT

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Project description:Transcriptional profiling of HPMECs comparing Control siRNA treated with HSP27 siRNA

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HSP27 (Heat Shock Protein 27, HSPB1) overexpression effect on bleomycin-induced PF (Pulmonary fibrosis) mice model

Project description:To analyze the role of HSP27 in bleomycin (BLM)-induced pulmonary fibrosis in vivo, we used TG mice that conventionally overexpressed HSP27. Our previously reported that HSP27 plays an important role in pulmonary fibrosis. In mice overexpressing HSPB1, BLM-induced fibrotic regions and collagen deposits were increased compared with those in control BL6 mice. Following intratracheal treatment of BLM, the HSP25 TG mice showed an abundance of mononuclear and neutrophils cells in the alveoli, greater destruction of alveolar septa, intra-alveolar hyaline membrane formation, and a marked increase in collagen deposition compared with control BL6 mice.

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Small heat shock proteins operate as molecular chaperones in the mitochondrial intermembrane space

Project description:Mitochondria are complex organelles with different compartments, each harboring their own protein quality control factors. While the chaperones of the mitochondrial matrix have been well characterized, it is poorly understood which chaperones protect the mitochondrial intermembrane space. We show that cytosolic small heat shock proteins are imported under basal conditions into the mitochondrial intermembrane space, where they operate as molecular chaperones. To identify chaperone substrates with MS/MS, we used a molecular trap variant of HSPB1/Hsp27 (S135F mutant). Through affinity-enrichment co-immunoprecipitation we identified significantly enriched substrates versus GFP-negative control.

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