In Vivo Clearance of Alpha-1 Acid Glycoprotein Is Influenced by the Extent of Its N-Linked Glycosylation and by Its Interaction with the Vessel Wall
المؤلفون المشاركون
Eltringham-Smith, Louise J.
Gataiance, Sharon
Bhakta, Varsha
Sheffield, William P.
Fox-Robichaud, Alison E.
McCurdy, Teresa R.
المصدر
Journal of Biomedicine and Biotechnology
العدد
المجلد 2012، العدد 2012 (31 ديسمبر/كانون الأول 2012)، ص ص. 1-11، 11ص.
الناشر
Hindawi Publishing Corporation
تاريخ النشر
2012-04-01
دولة النشر
مصر
عدد الصفحات
11
التخصصات الرئيسية
الملخص EN
Alpha-1 acid glycoprotein (AGP) is a highly glycosylated plasma protein that exerts vasoprotective effects.
We hypothesized that AGP’s N-linked glycans govern its rate of clearance from the circulation, and followed the disappearance of different forms of radiolabeled human AGP from the plasma of rabbits and mice.
Enzymatic deglycosylation of human plasma-derived AGP (pdAGP) by Peptide: N-Glycosidase F yielded a mixture of differentially deglycosylated forms (PNGase-AGP), while the introduction of five Asn to Gln mutations in recombinant Pichia pastoris-derived AGP (rAGP-N(5)Q) eliminated N-linked glycosylation.
PNGase-AGP was cleared from the rabbit circulation 9-fold, and rAGP-N(5)Q, 46-fold more rapidly than pdAGP, primarily via a renal route.
Pichia pastoris-derived wild-type rAGP differed from pdAGP in expressing mannose-terminated glycans, and, like neuraminidase-treated pdAGP, was more rapidly removed from the rabbit circulation than rAGP-N(5)Q.
Systemic hyaluronidase treatment of mice transiently decreased pdAGP clearance.
AGP administration to mice reduced vascular binding of hyaluronic acid binding protein in the liver microcirculation and increased its plasma levels.
Our results support a critical role of N-linked glycosylation of AGP in regulating its in vivo clearance and an influence of a hyaluronidase-sensitive component of the vessel wall on its transendothelial passage.
نمط استشهاد جمعية علماء النفس الأمريكية (APA)
McCurdy, Teresa R.& Bhakta, Varsha& Eltringham-Smith, Louise J.& Gataiance, Sharon& Fox-Robichaud, Alison E.& Sheffield, William P.. 2012. In Vivo Clearance of Alpha-1 Acid Glycoprotein Is Influenced by the Extent of Its N-Linked Glycosylation and by Its Interaction with the Vessel Wall. Journal of Biomedicine and Biotechnology،Vol. 2012, no. 2012, pp.1-11.
https://search.emarefa.net/detail/BIM-460987
نمط استشهاد الجمعية الأمريكية للغات الحديثة (MLA)
McCurdy, Teresa R.…[et al.]. In Vivo Clearance of Alpha-1 Acid Glycoprotein Is Influenced by the Extent of Its N-Linked Glycosylation and by Its Interaction with the Vessel Wall. Journal of Biomedicine and Biotechnology No. 2012 (2012), pp.1-11.
https://search.emarefa.net/detail/BIM-460987
نمط استشهاد الجمعية الطبية الأمريكية (AMA)
McCurdy, Teresa R.& Bhakta, Varsha& Eltringham-Smith, Louise J.& Gataiance, Sharon& Fox-Robichaud, Alison E.& Sheffield, William P.. In Vivo Clearance of Alpha-1 Acid Glycoprotein Is Influenced by the Extent of Its N-Linked Glycosylation and by Its Interaction with the Vessel Wall. Journal of Biomedicine and Biotechnology. 2012. Vol. 2012, no. 2012, pp.1-11.
https://search.emarefa.net/detail/BIM-460987
نوع البيانات
مقالات
لغة النص
الإنجليزية
الملاحظات
Includes bibliographical references
رقم السجل
BIM-460987
قاعدة معامل التأثير والاستشهادات المرجعية العربي "ارسيف Arcif"
أضخم قاعدة بيانات عربية للاستشهادات المرجعية للمجلات العلمية المحكمة الصادرة في العالم العربي
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