دورية أكاديمية
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Circulating but not immobilized N-deglycosylated von Willebrand factor increases platelet adhesion under flow conditions.

التفاصيل البيبلوغرافية
العنوان: Circulating but not immobilized N-deglycosylated von Willebrand factor increases platelet adhesion under flow conditions.
المؤلفون: Fallah MA; University of Augsburg, Chair of Experimental Physics I, 86159 Augsburg, Germany ; Department of Biophysical Chemistry, University of Konstanz, 78457 Konstanz, Germany., Huck V; Heidelberg University, Medical Faculty Mannheim, Experimental Dermatology, 68167 Mannheim, Germany., Niemeyer V; Heidelberg University, Medical Faculty Mannheim, Experimental Dermatology, 68167 Mannheim, Germany., Desch A; Heidelberg University, Medical Faculty Mannheim, Experimental Dermatology, 68167 Mannheim, Germany., Angerer JI; University of Augsburg, Chair of Experimental Physics I, 86159 Augsburg, Germany., McKinnon TA; Imperial College London, Hammersmith Hospital Campus, Department of Medicine, London W12 0NN, United Kingdom., Wixforth A; University of Augsburg, Chair of Experimental Physics I, 86159 Augsburg, Germany., Schneider SW; Heidelberg University, Medical Faculty Mannheim, Experimental Dermatology, 68167 Mannheim, Germany., Schneider MF; Department of Mechanical Engineering, Boston University, Boston, Massachusetts 02215, USA.
المصدر: Biomicrofluidics [Biomicrofluidics] 2013 Aug 26; Vol. 7 (4), pp. 44124. Date of Electronic Publication: 2013 Aug 26 (Print Publication: 2013).
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: American Institute of Physics Country of Publication: United States NLM ID: 101293825 Publication Model: eCollection Cited Medium: Print ISSN: 1932-1058 (Print) Linking ISSN: 19321058 NLM ISO Abbreviation: Biomicrofluidics Subsets: PubMed not MEDLINE
أسماء مطبوعة: Original Publication: Melville, NY : American Institute of Physics, 2007-
مستخلص: The role of von Willebrand factor (VWF) as a shear stress activated platelet adhesive has been related to a coiled-elongated shape conformation. The forces dominating this transition have been suggested to be controlled by the proteins polymeric architecture. However, the fact that 20% of VWF molecular weight originates from glycan moieties has so far been neglected in these calculations. In this study, we present a systematic experimental investigation on the role of N-glycosylation for VWF mediated platelet adhesion under flow. A microfluidic flow chamber with a stenotic compartment that allows one to mimic various physiological flow conditions was designed for the efficient analysis of the adhesion spectrum. Surprisingly, we found an increase in platelet adhesion with elevated shear rate, both qualitatively and quantitatively fully conserved when N-deglycosylated VWF (N-deg-VWF) instead of VWF was immobilized in the microfluidic channel. This has been demonstrated consistently over four orders of magnitude in shear rate. In contrast, when N-deg-VWF was added to the supernatant, an increase in adhesion rate by a factor of two was detected compared to the addition of wild-type VWF. It appears that once immobilized, the role of glycans is at least modified if not-as found here for the case of adhesion-negated. These findings strengthen the physical impact of the circulating polymer on shear dependent platelet adhesion events. At present, there is no theoretical explanation for an increase in platelet adhesion to VWF in the absence of its N-glycans. However, our data indicate that the effective solubility of the protein and hence its shape or conformation may be altered by the degree of glycosylation and is therefore a good candidate for modifying the forces required to uncoil this biopolymer.
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تواريخ الأحداث: Date Created: 20140110 Date Completed: 20140109 Latest Revision: 20211021
رمز التحديث: 20221213
مُعرف محوري في PubMed: PMC3772935
DOI: 10.1063/1.4819746
PMID: 24404057
قاعدة البيانات: MEDLINE
الوصف
تدمد:1932-1058
DOI:10.1063/1.4819746