کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10756258 | 1050382 | 2014 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
A critical role for the regulation of Syk from agglutination to aggregation in human platelets
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کلمات کلیدی
PI3Klinker for activation of T-cellsFc receptor γ-chainphospholipase Cγ2SLP-76FcRγPLCγ2glycoprotein IbαADAPPrPPKCPABmAbWPSFITCvWFPTPMonoclonal antibody - آنتی بادی مونوکلونالPolyclonal antibody - آنتی بادی های پلی کلونالintegrin αIIbβ3 - انتگرال αIIbβ3Syk - بیمارLAT - سالVon Willebrand factor - عامل فون ویلبراندProtein tyrosine phosphorylation - فسفوریلاسیون پروتئین تیروزینphosphoinositide 3-kinase - فسفینوزیتید 3-کینازfluorescein isothiocyanate - فلوئورسین ایسوتیوسیاناتProtein kinase C - پروتئین کیناز سیplatelet-rich plasma - پلاسمای غنی از پلاکت، PRP، پی آر پیwashed platelets - پلاکت های شسته شدهconvulxin - کانولکسینGlycoprotein - گلیکوپروتئین
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
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چکیده انگلیسی
Agglucetin, a tetrameric glycoprotein (GP) Ibα agonist from Formosan Agkistrodon acutus venom, has been characterized as an agglutination inducer in human washed platelets (WPs). In platelet-rich plasma (PRP), agglucetin dramatically elicits a biphasic response of agglutination and subsequent aggregation. For clarifying the intracellular signaling events from agglutination to aggregation in human platelets, we examined the essential signaling molecules involved through the detection of protein tyrosine phosphorylation (PTP). In WPs, an anti-GPIbα monoclonal antibody (mAb) AP1, but not a Src kinase inhibitor PP1, completely inhibited agglucetin-induced agglutination. However, PP1 but not AP1 had a potent suppression on platelet aggregation by a GPVI activator convulxin. The PTP analyses showed agglucetin alone can cause a weak pattern involving sequential phosphorylation of Lyn/Fyn, Syk, SLP-76 and phospholipase Cγ2 (PLCγ2). Furthermore, a Syk-selective kinase inhibitor, piceatannol, significantly suppressed the aggregating response in agglucetin-activated PRP. Analyzed by flow cytometry, the binding capacity of fluorophore-conjugated PAC-1, a mAb recognizing activated integrin αIIbβ3, was shown to increase in agglucetin-stimulated platelets. Again, piceatannol but not PP1 had a concentration-dependent suppression on agglucetin-induced αIIbβ3 exposure. Moreover, the formation of signalosome, including Syk, SLP-76, VAV, adhesion and degranulation promoting adapter protein (ADAP) and PLCγ2, are required for platelet aggregation in agglucetin/fibrinogen-activated platelets. In addition, GPIbα-ligation via agglucetin can substantially promote the interactions between αIIbβ3 and fibrinogen. Therefore, the signal pathway of Lyn/Fyn/Syk/SLP-76/ADAP/VAV/PLCγ2/PKC is sufficient to trigger platelet aggregation in agglucetin/fibrinogen-pretreated platelets. Importantly, Syk may function as a major regulator for the response from GPIbα-initiated agglutination to integrin αIIbβ3-dependent aggregation in human platelets.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 443, Issue 2, 10 January 2014, Pages 580-585
Journal: Biochemical and Biophysical Research Communications - Volume 443, Issue 2, 10 January 2014, Pages 580-585
نویسندگان
Chun-Ho Shih, Tin-Bin Chiang, Wen-Jeng Wang,