tailieunhanh - Báo cáo khoa học: Fatty aldehyde dehydrogenase is up-regulated by polyunsaturated fatty acid via peroxisome proliferatoractivated receptor a and suppresses polyunsaturated fatty acid-induced endoplasmic reticulum stress

Fatty aldehyde dehydrogenase (FALDH; also known as ALDH3A2 or ALDH10) oxidizes medium- or long-chain aliphatic aldehydes. FALDH deficiency in humans is known to be the cause of Sjo¨gren–Larsson syn-drome, in which individuals display neurological symptoms and cutaneous abnormality. | ễFEBS Journal Fatty aldehyde dehydrogenase is up-regulated by polyunsaturated fatty acid via peroxisome proliferator-activated receptor a and suppresses polyunsaturated fatty acid-induced endoplasmic reticulum stress Bunichiro Ashibe1 2 and Kiyoto Motojima1 1 Department of Biochemistry Meiji PharmaceuticalUniversity Kiyose Tokyo Japan 2 Yomeishu Seizo Co. Ltd Shibuya-ku Tokyo Japan Keywords alternative splicing fatty aldehyde dehydrogenase free fatty acid lipotoxicity unfolded protein response Correspondence K. Motojima Department of Biochemistry Meiji PharmaceuticalUniversity Noshio 2-522-1 Kiyose Tokyo 204-8588 Japan Fax 81 42 495 8474 Tel 81 42 495 8474 E-mail motojima@ Received 26 June 2009 revised 17 September 2009 accepted 24 September 2009 doi Fatty aldehyde dehydrogenase FALDH also known as ALDH3A2 or ALDH10 oxidizes medium- or long-chain aliphatic aldehydes. FALDH deficiency in humans is known to be the cause of Sjogren-Larsson syndrome in which individuals display neurological symptoms and cutaneous abnormality. FALDH-V a splice isoform of FALDH is localized in the peroxisome and contributes to the oxidization of pristanal an intermediate of the a-oxidation pathway. FALDH-N another splice isoform of FALDH is induced by peroxisomal proliferator-activated receptor a ligands although its activation mechanism has not been clarified. In the present study we show that transcriptional activation of FALDH is directly regulated by peroxisomal proliferator-activated receptor a through a direct repeat-1 site located in the FALDH promoter. In addition FALDH is efficiently induced by linoleic acid in rat hepatoma Fao cells through transcriptional activation by peroxisomal proliferator-activated receptor a. Furthermore ectopic expression of endoplasmic reticulum-localizing FALDH-N but not peroxisome-localizing FALDH-V suppresses endoplasmic reticulum stress caused by linoleic acid in HEK293 cells. These results suggest the

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