کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1983352 | 1539871 | 2016 | 8 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
TIMAP-protein phosphatase 1-complex controls endothelin-1 production via ECE-1 dephosphorylation
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کلمات کلیدی
PP1MYPTBPAECPP1CHPAECezrin-radixin-moesinECE-1TIMAPphorbol 12-myristate 13-acetateECISPKCET-1ERMpKaPMA - LDC هاEndothelin Converting Enzyme-1 - آنتلیون تبدیل آنزیم-1endothelin-1 - اندوتلین-1human pulmonary artery endothelial cells - سلول اندوتلیال عروق ریوی انسانEndothelial cell - سلول های اندوتلیالEndothelial cells - سلولهای اندوتلیالElectric cell-substrate impedance sensing - سنجش امپدانس الکتریکی سلول-سوبستراprotein phosphatase 1 - پروتئین فسفاتاز 1protein kinase A - پروتئین کیناز AProtein kinase C - پروتئین کیناز سی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
Endothelin induced signaling pathways can affect blood pressure and vascular tone, but the influence of endothelins on tumor cells is also significant. We have detected elevated endothelin-1 secretion from TIMAP (TGF-β inhibited membrane associated protein) depleted vascular endothelial cells. The autocrine signaling activated by the elevated endothelin-1 level through the ETB receptors evoked an angiogenic-like phenotype, the cells assumed an elongated morphology, and enhanced tube formation and wound healing abilities. The depleted protein, TIMAP, is a highly specific and abundant protein in the endothelial cells, and it is a regulatory/targeting subunit for the catalytic subunit of protein phosphatase 1 (PP1c). Protein-protein interaction between the TIMAP-PP1c complex and the endothelin converting enzyme-1 (ECE-1) was detected, the latter of which is a transmembrane protein that produces the biologically active 21-amino acid form of endothelin-1 from proendothelin. The results indicate that silencing of TIMAP induces a reduction in TIMAP-PP1c activity connected to ECE-1. This leads to an increase in the amount of ECE-1 protein in the plasma membrane and a consequent increase in endothelin-1 secretion. Similarly, activation of PKC, the kinase responsible for ECE-1 phosphorylation increased ECE-1 protein level in the membrane fraction of the endothelial cells. The elevated ECE-1 level was mitigated in time in normal cells, but was clearly preserved in TIMAP-depleted cells. Overall, our results indicate that PKC-phosphorylated ECE-1 is a TIMAP-PP1c substrate and this phosphatase complex has an important role in endothelin-1 production of EC through the regulation of ECE-1 activity.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: The International Journal of Biochemistry & Cell Biology - Volume 73, April 2016, Pages 11-18
Journal: The International Journal of Biochemistry & Cell Biology - Volume 73, April 2016, Pages 11-18
نویسندگان
Anita Boratkó, Zoltán Veréb, Goran Petrovski, Csilla Csortos,