Skip to navigation Skip to content
  • Woodruff
  • Business
  • Health Sciences
  • Law
  • Rose
  • Oxford College
  • Theology
  • Schools
    • Undergraduate

      • Emory College
      • Oxford College
      • Business School
      • School of Nursing

      Community

      • Emory College
      • Oxford College
      • Business School
      • School of Nursing
    • Graduate

      • Business School
      • Graduate School
      • School of Law
      • School of Medicine
      • School of Nursing
      • School of Public Health
      • School of Theology
  • Libraries
    • Libraries

      • Robert W. Woodruff
      • Business
      • Chemistry
      • Health Sciences
      • Law
      • MARBL
      • Music & Media
      • Oxford College
      • Theology
    • Library Tools

      • Course Reserves
      • Databases
      • Digital Scholarship (ECDS)
      • discoverE
      • eJournals
      • Electronic Dissertations
      • EmoryFindingAids
      • EUCLID
      • ILLiad
      • OpenEmory
      • Research Guides
  • Resources
    • Resources

      • Administrative Offices
      • Emory Healthcare
      • Academic Calendars
      • Bookstore
      • Campus Maps
      • Shuttles and Parking
      • Athletics: Emory Eagles
      • Arts at Emory
      • Michael C. Carlos Museum
      • Emory News Center
      • Emory Report
    • Resources

      • Emergency Contacts
      • Information Technology (IT)
      • Outlook Web Access
      • Office 365
      • Blackboard
      • OPUS
      • PeopleSoft Financials: Compass
      • Careers
      • Human Resources
      • Emory Alumni Association
  • Browse
    • Works by Author
    • Works by Journal
    • Works by Subject
  • For Authors
    • How to Submit
    • Deposit Advice
    • Deposit Instructions
    • Author Rights
    • FAQ
    • Emory Open Access Policy
    • Open Access Fund
  • About OpenEmory
    • About OpenEmory
    • About Us
    • Citing Articles
    • Contact Us
    • Privacy Policy
    • Terms of Use
 
Contact Us

Filter Results:

Author

  • Chen, Guangping (1)
  • Druey, Kirk M. (1)
  • Hensch, Nicole R. (1)
  • Karim, Zubair A. (1)
  • Khasawneh, Fadi T. (1)
  • Qian, Xiaoqian (1)
  • Sands, Jeff (1)
  • Song, Xiang (1)
  • Tansey, MariadeLourdes (1)

Subject

  • Biology, Cell (1)
  • Biology, Physiology (1)
  • Health Sciences, General (1)
  • Health Sciences, Pharmacy (1)

Journal

  • PLoS ONE (1)
  • Pflügers Archiv European Journal of Physiology (1)

Keyword

  • b (2)
  • protein (2)
  • scienc (2)
  • technolog (2)
  • accumul (1)
  • agonist (1)
  • biomedicin (1)
  • c (1)
  • collect (1)
  • complex (1)
  • concentr (1)
  • coupl (1)
  • defect (1)
  • duct (1)
  • format (1)
  • glycosyl (1)
  • in (1)
  • injuri (1)
  • kappa (1)
  • kappab (1)
  • kinas (1)
  • lack (1)
  • life (1)
  • membran (1)
  • mice (1)
  • multidisciplinari (1)
  • neuron (1)
  • other (1)
  • outsid (1)
  • outsidein (1)
  • physiolog (1)
  • proteincoupl (1)
  • receptor (1)
  • secret (1)
  • sialyl (1)
  • sialyltransferas (1)
  • thrombus (1)
  • topic (1)
  • transport (1)
  • urea (1)
  • ut (1)
  • utb (1)
  • vascular (1)

Author department

  • Medicine: Nephrology (1)

Search Results for all work with filters:

  • 2016
  • phosphoryl
  • Physiology: Admin

Work 1-2 of 2

Sorted by relevance

Article

Modulation of kidney urea transporter UT-A3 activity by alpha2,6-sialylation

by Xiaoqian Qian; Jeff Sands; Xiang Song; Guangping Chen

2016

Subjects
  • Biology, Physiology
  • Biology, Cell
  • File Download
  • View Abstract

Abstract:Close

Two urea transporters, UT-A1 and UT-A3, are expressed in the kidney terminal inner medullary collecting duct (IMCD) and are important for the production of concentrated urine. UT-A1, as the largest isoform of all UT-A urea transporters, has gained much attention and been extensively studied; however, the role and the regulation of UT-A3 are less explored. In this study, we investigated UT-A3 regulation by glycosylation modification. A site-directed mutagenesis verified a single glycosylation site in UT-A3 at Asn279. Loss of the glycosylation reduced forskolin-stimulated UT-A3 cell membrane expression and urea transport activity. UT-A3 has two glycosylation forms, 45 and 65 kDa. Using sugar-specific binding lectins, the UT-A3 glycosylation profile was examined. The 45-kDa form was pulled down by lectin concanavalin A (Con A) and Galant husnivalis lectin (GNL), indicating an immature glycan with a high amount of mannose (Man), whereas the 65-kDa form is a mature glycan composed of acetylglucosamine (GlcNAc) and poly-N-acetyllactosame (poly-LacNAc) that was pulled down by wheat germ agglutinin (WGA) and tomato lectin, respectively. Interestingly, the mature form of UT-A3 glycan contains significant amounts of sialic acid. We explored the enzymes responsible for directing UT-A3 sialylation. Sialyltransferase ST6GalI, but not ST3GalIV, catabolizes UT-A3 α2,6-sialylation. Activation of protein kinase C (PKC) by PDB treatment promoted UT-A3 glycan sialylation and membrane surface expression. The PKC inhibitor chelerythrine blocks ST6GalI-induced UT-A3 sialylation. Increased sialylation by ST6GalI increased UT-A3 protein stability and urea transport activity. Collectively, our study reveals a novel mechanism of UT-A3 regulation by ST6GalI-mediated sialylation modification that may play an important role in kidney urea reabsorption and the urinary concentrating mechanism.

Article

RGS10 Negatively Regulates Platelet Activation and Thrombogenesis

by Nicole R. Hensch; Zubair A. Karim; Kirk M. Druey; MariadeLourdes Tansey; Fadi T. Khasawneh

2016

Subjects
  • Health Sciences, Pharmacy
  • Health Sciences, General
  • File Download
  • View Abstract

Abstract:Close

Regulators of G protein signaling (RGS) proteins act as GTPase activating proteins to negatively regulate G protein-coupled receptor (GPCR) signaling. Although several RGS proteins including RGS2, RGS16, RGS10, and RGS18 are expressed in human and mouse platelets, the respective unique function(s) of each have not been fully delineated. RGS10 is a member of the D/R12 subfamily of RGS proteins and is expressed in microglia, macrophages, megakaryocytes, and platelets. We used a genetic approach to examine the role (s) of RGS10 in platelet activation in vitro and hemostasis and thrombosis in vivo. GPCR-induced aggregation, secretion, and integrin activation was much more pronounced in platelets from Rgs10-/- mice relative to wild type (WT). Accordingly, these mice had markedly reduced bleeding times and were more susceptible to vascular injury-associated thrombus formation than control mice. These findings suggest a unique, non-redundant role of RGS10 in modulating the hemostatic and thrombotic functions of platelets in mice. RGS10 thus represents a potential therapeutic target to control platelet activity and/or hypercoagulable states.
Site Statistics
  • 33,717
  • Total Works
  • 7,945,870
  • Downloads
  • 562,809
  • Downloads This Year

Copyright © 2016 Emory University - All Rights Reserved
540 Asbury Circle, Atlanta, GA 30322-2870
(404) 727-6861
Privacy Policy | Terms & Conditions

v2.2.8-dev

Contact Us
Download now