کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1941785 | 1536905 | 2015 | 15 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Conservation of structure and function in vertebrate c-FLIP proteins despite rapid evolutionary change
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کلمات کلیدی
NF-κBCellular FLICE-like inhibitory proteinCASCODCOrnithine decarboxylasec-FLIPDEDTRAF2CHXFADDRT-PCReGFPMorpholino oligonucleotide - الیگونوکلئوتید مورفولینوEmbryogenesis - جنین زاییApoptosis - خزان یاختهایdeath effector domain - دامنه موثر مرگcaspase-recruitment domain - دامنه کاریپس-استخدامcycloheximide - سیکلوهایسیمیدtumor necrosis factor receptor-associated factor 2 - عامل گیرنده فاکتور نکروز تومور عامل 2Nuclear factor-kappa B - فاکتور هسته ای-کاپا BEvolution - فرگشت reverse transcription-polymerase chain reaction - واکنش زنجیره ای رونویسی-پلیمراز معکوسpolymerase chain reaction - واکنش زنجیره ای پلیمرازPCR - واکنش زنجیرهٔ پلیمرازFAS-associated death domain protein - پروتئین دامنه مرگ مرتبط با FASenhanced green fluorescent protein - پروتئین فلورسنت سبز افزایش یافته استCARD - کارتCaspase-8 - کاسپاز-8
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
Cellular FLICE-like inhibitory protein (c-FLIP, gene symbol CFLAR) was first identified as a negative regulator of death receptor-mediated apoptosis in mammals. To understand the ubiquity and diversity of the c-FLIP protein subfamily during evolution, c-FLIP orthologs were identified from a comprehensive range of vertebrates, including birds, amphibians, and fish, and were characterized by combining experimental and computational analysis. Predictions of three-dimensional protein structures and molecular phylogenetic analysis indicated that the conserved structural features of c-FLIP proteins are all derived from an ancestral caspase-8, although they rapidly diverged from the subfamily consisting of caspases-8, -10, and -18. The functional role of the c-FLIP subfamily members is nearly ubiquitous throughout vertebrates. Exogenous expression of non-mammalian c-FLIP proteins in cultured mammalian cells suppressed death receptor-mediated apoptosis, implying that all of these proteins possess anti-apoptotic activity. Furthermore, non-mammalian c-FLIP proteins induced NF-κB activation much like their mammalian counterparts. The CFLAR mRNAs were synthesized during frog and fish embryogenesis. Overexpression of a truncated mutant of c-FLIP in the Xenopus laevis embryos by mRNA microinjection caused thorax edema and abnormal constriction of the abdomen. Depletion of cflar transcripts in zebrafish resulted in developmental abnormalities accompanied by edema and irregular red blood cell flow. Thus, our results demonstrate that c-FLIP/CFLAR is conserved in both protein structure and function in several vertebrate species, and suggest a significant role of c-FLIP in embryonic development.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemistry and Biophysics Reports - Volume 3, September 2015, Pages 175-189
Journal: Biochemistry and Biophysics Reports - Volume 3, September 2015, Pages 175-189
نویسندگان
Kazuhiro Sakamaki, Naoyuki Iwabe, Hiroaki Iwata, Kenichiro Imai, Chiyo Takagi, Kumiko Chiba, Chisa Shukunami, Kentaro Tomii, Naoto Ueno,