کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10803085 | 1055772 | 2008 | 9 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Isolation and characterization of mutant animal cell line defective in alkyl-dihydroxyacetonephosphate synthase: Localization and transport of plasmalogens to post-Golgi compartments
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کلمات کلیدی
TFRacyl-CoA oxidasePlsEtnPlasmalogenDRMBFADHAPATNDGAAOXTLCTCAeGFPLyso-PEplasmenylethanolaminealkyl-dihydroxyacetonephosphate synthase - آلکیل دی هیدروکسی استون فسفات سنتازsphingomyelin - اسفنگومیلینtrichloroacetic acid - اسید ترشکلراکتیکnordihydroguaiaretic acid - اسید نوردی هیدروگالیارتیCho - برایbrefeldin A - برفلدین AChinese Hamster Ovary - تخمدان هامستر چینیdihydroxyacetonephosphate acyltransferase - دی هیدروکسی اکتون فسفات آکیل ترانسفرازreverse transcription - رونویسی معکوسcytochrome P450 reductase - سیتوکروم P450 ردوکتازendoplasmic reticulum - شبکه آندوپلاسمی Detergent-resistant membranes - غشای مقاوم در برابر مواد شویندهPlasma membranes - غشای پلاسماphosphatidylethanolamine - فسفاتیدیلتانولامینperoxisome - پراکسیومpost-nuclear supernatant - پس از اتمسفر هسته ایPNS - کارمندان دولتthin-layer chromatography - کروماتوگرافی نازک لایهtransferrin receptor - گیرنده انتقالین
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
We herein isolated plasmalogen-deficient Chinese hamster ovary (CHO) mutant, ZPEG251, with a phenotype of normal import of peroxisomal matrix and membrane proteins. In ZPEG251, plasmenylethanolamine (PlsEtn) was severely reduced. Complementation analysis by expression of genes responsible for the plasmalogen biogenesis suggested that alkyl-dihydroxyacetonephosphate synthase (ADAPS), catalyzing the second step of plasmalogen biogenesis, was deficient in ZPEG251. ADAPS mRNA was barely detectable as verified by Northern blot and reverse transcription-PCR analyses. Defect of ADAPS expression was also assessed by immunoblot. As a step toward delineating functional roles of PlsEtn, we investigated its subcellular localization. PlsEtn was localized to post-Golgi compartments and enriched in detergent-resistant membranes. Transport of PlsEtn to post-Golgi compartments was apparently affected by lowering cellular ATP, but not by inhibitors of microtubule assembly and vesicular transport. Partitioning of cholesterol and sphingomyelin, a typical feature of lipid rafts, was not impaired in plasmalogen-deficient cells, including peroxisome assembly-defective mutants, hence suggesting that PlsEtn was not essential for lipid-raft architecture in CHO cells.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - Molecular Cell Research - Volume 1783, Issue 10, October 2008, Pages 1857-1865
Journal: Biochimica et Biophysica Acta (BBA) - Molecular Cell Research - Volume 1783, Issue 10, October 2008, Pages 1857-1865
نویسندگان
Masanori Honsho, Yuichi Yagita, Naohiko Kinoshita, Yukio Fujiki,