Tuyển tập các báo cáo nghiên cứu về y học được đăng trên tạp chí y học Critical Care giúp cho các bạn có thêm kiến thức về ngành y học đề tài: Heat shock protein 70 expression, keratin phosphorylation and Mallory body formation in hepatocytes from griseofulvin-intoxicated mice. | Comparative Hepatology BioMed Central Research Open Access Heat shock protein 70 expression keratin phosphorylation and Mallory body formation in hepatocytes from griseofulvin-intoxicated mice Michel Fausther Louis Villeneuve and Monique Cadrin Address Département de chimie-biologie Université du Québec à Trois-Rivières 3351 boulevard des Forges . 500 Québec Trois-Rivières Canada G9A 5H7 Email Michel Fausther- fausther@ Louis Villeneuve - lvillen@ Monique Cadrin - monique_cadrin@ Corresponding author Published 12 August 2004 Received 26 February 2004 Accepted 12 August 2004 Comparative Hepatology 2004 3 5 doi 1476-5926-3-5 This article is available from http content 3 1 5 2004 Fausther et al licensee BioMed Central Ltd. This is an open-access article distributed under the terms of the Creative Commons Attribution License http licenses by which permits unrestricted use distribution and reproduction in any medium provided the original work is properly cited. Abstract Background Keratins are members of the intermediate filaments IFs proteins which constitute one of the three major cytoskeletal protein families. In hepatocytes keratin 8 and 18 K8 18 are believed to play a protective role against mechanical and toxic stress. Post-translational modifications such as phosphorylation and glycosylation are thought to modulate K8 18 functions. Treatment of mouse with a diet containing griseofulvin GF induces in hepatocytes modifications in organization expression and phosphorylation of K8 18 IFs and leads on the long term to the formation of K8 18 containing aggregates morphologically and biochemically identical to Mallory bodies present in a number of human liver diseases. The aim of the present study was to investigate the relationship between the level and localization of the stress inducible heat shock protein 70 kDa HSP70i and the level and localization of K8 18 .
