کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10803620 | 1057162 | 2014 | 8 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Proliferation and migration activities of fibroblast growth factor-2 in endothelial cells are modulated by its direct interaction with heparin affin regulatory peptide
ترجمه فارسی عنوان
فعالیت های تکثیر و مهاجرت فاکتور رشد فیبروبلاست در 2 سلول های اندوتلیالی بوسیله تعامل مستقیم با پپتید نظارتی هپارین افین
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کلمات کلیدی
HUVECHBGFHeparin affin regulatory peptideVEGF165Heparan sulfatesa.a.FGF-2MidkineCTGFASPAspartic acid - آسپارتیک اسدALK - آلکamino acid - آمینو اسیدInteraction - اثر متقابلglutamic acid - اسید گلوتامیکthrombospondin type 1 repeat - ترومبوسپوندن نوع 1 تکرار شودProliferation - ترویجHARP - ساز چنگHuman umbilical vein endothelial cells - سلول های اندوتلیالی ورید ناف انسانGrowth factors - فاکتور رشدConnective tissue growth factor - فاکتور رشد بافت همبندfibroblast growth factor-2 - فیبروبلاست رشد فاکتور 2Anaplastic lymphoma kinase - لنفوم کیناز AnaplasticMigration - مهاجرتGlu - گلو
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
چکیده انگلیسی
Angiogenesis is the physiological process involving the growth of new blood vessels from pre-existing vessels. In normal or pathological angiogenesis, angiogenic growth factors activate cognate receptors on endothelial cells. Fibroblast growth factor-2 (FGF-2) and heparin affin regulatory peptide (HARP) are two heparin-binding growth factors and were described for their pro-angiogenic properties on human umbilical endothelial cells (HUVEC). We now show that HARP acts as a mediator of FGF-2's stimulatory effects, since it is able to inhibit the proliferation and migration of HUVEC induced by FGF-2. We demonstrate by ELISA and optical biosensor binding assay that HARP and FGF-2 interact through direct binding. We have adapted a previously developed structural proteomics method for the identification of residues involved in protein-protein interactions. Application of this method showed that two sequences in HARP were involved in binding FGF-2. One was in the C-thrombospondin type 1 repeat (C-TSR-1) domain and the other in the C-terminal domain of HARP. The identification of these regions as mediating the binding of FGF-2 was confirmed by ELISA using synthetic peptides, which are as well mediators of FGF-2-induced proliferation, migration and tubes formation on HUVEC in vitro. These results imply that besides a regulation of the proliferation, migration and angiogenesis of HUVEC by direct interaction of FGF-2 with its receptors, an alternative pathway exists involving its binding to growth factors such as HARP.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimie - Volume 107, Part B, December 2014, Pages 350-357
Journal: Biochimie - Volume 107, Part B, December 2014, Pages 350-357
نویسندگان
Célia Dos Santos, Charly Blanc, Rania Elahouel, Mark Prescott, Gilles Carpentier, Alessandro Ori, José Courty, Yamina Hamma-Kourbali, David G. Fernig, Jean Delbé,