HSP40 Ameliorates Impairment of Insulin Secretion by Inhibiting Huntingtin Aggregation in a HD Pancreatic β Cell Model

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概要

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• Diabetes frequently develops in Huntington’s disease patients. Here, we found that mutant huntingtin forms aggregates in the cytoplasm and reduces insulin secretion from huntingtin transfected pancreatic β cell lines, NIT-1 cells. Activity of the pro-survival factor, Akt, is enhanced in these cells, which might improve the maintenance of insulin content. Overexpression of heat shock protein 40 (HSP40) inhibits aggregation, reverses impaired insulin release, and blocks the enhancement of Akt activity. These results suggest that impairment of β cells is mostly linked with the aggregate formation of mutant huntingtin, and that HSP40 ameliorates the malfunction of pancreatic β cells by inhibiting aggregation.

• 社団法人 日本農芸化学会の論文

著者

• Li He

  Division Of Histology And Embryology Department Of Anatomy Tongji Medical College Huazhong Universit

• Ye Cui-Fang

  Division of Histology and Embryology, Department of Anatomy, Tongji Medical College, Huazhong Univer

関連論文

• P2-34 The Synergism of Chaperones Is Essential for Suppression of aggregation and Cellular Toxicity of Mutant Huntingtin
• P2-21 The Involvement of Huntingtin-associated protein 1 in the axonal transport
• WS6-05 The Role of Metabotropic Glutamate Receptror 5 in the Selective Cytotoxicity of Mutant Huntingtin and Its Mechanism(Molecular Pathology, Up-date)
• WS5-03 Involvement of Huntingtin-associated Protein 1 in the Secretion of Insulin from β cell of Pancreatic Islets(Histochemistry of Protein Function)
• HSP40 Ameliorates Impairment of Insulin Secretion by Inhibiting Huntingtin Aggregation in a HD Pancreatic β Cell Model
• HSP40 Ameliorates Impairment of Insulin Secretion by Inhibiting Huntingtin Aggregation in a HD Pancreatic β Cell Model

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