Skip to navigation Skip to content
  • Woodruff
  • Business
  • Health Sciences
  • Law
  • MARBL
  • 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
    • Works by Dept
    • Faculty by Dept
  • For Authors
    • How to Submit
    • Deposit Advice
    • Author Rights
    • Publishing Your Data
    • 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:

Year

  • 2011 (1)
  • 2012 (1)
  • 2014 (1)
  • 2016 (1)
  • 2020 (1)

Author

  • Brenet, Marianne (1)
  • Burridge, Keith (1)
  • Cardenas, Areli (1)
  • Chen, Guangping (1)
  • Chen, Y. Eugene (1)
  • Chu, Miensheng (1)
  • Diaz, Jorge (1)
  • Farjah, Mariam (1)
  • Garcia-Barrio, Minerva (1)
  • Garcia-Mata, Rafael (1)
  • Geenen, David L. (1)
  • Goldspink, Paul H. (1)
  • Griendling, Kathy (1)
  • Hitomi, Hirofumi (1)
  • Huang, Bo (1)
  • Kalmanson, Olivia (1)
  • Kang, Ting (1)
  • Kim, Taehoon (1)
  • Kong, Milene (1)
  • Koshman, Yevgeniya E. (1)
  • Kumar, Mohit (1)
  • Lassegue, Bernard P (1)
  • Lewis, William (1)
  • Leyton, Lisette (1)
  • Lin, Yiming (1)
  • Liu, Dong (1)
  • Maldonado, Horacio (1)
  • Matthews, Roland (1)
  • Mehta, Puja K. (1)
  • Olatinwo, Moshood (1)
  • Qian, Xiaoqian (1)
  • Quest, Andrew F. G. (1)
  • Samarel, Allen M. (1)
  • San Martin Almeyda, Alejandra (1)
  • San Martin, Alejandra (1)
  • Sands, Jeff (1)
  • Schneider, Pascal (1)
  • Seidel-Rogol, Bonnie (1)
  • Solaro, R. John (1)
  • Song, Xiang (1)
  • Taniyama, Yoshihiro (1)
  • Thompson, Winston E. (1)
  • Valdivia, Alejandra (1)
  • Xu, Wei (1)
  • de Tombe, Pieter (1)

Subject

  • Health Sciences, Oncology (2)
  • Biology, Genetics (1)
  • Biology, Microbiology (1)
  • Health Sciences, Medicine and Surgery (1)
  • Health Sciences, Obstetrics and Gynecology (1)

Journal

  • American Journal of Physiology - Cell Physiology (1)
  • Cell Communication and Signaling (1)
  • Journal of Molecular and Cellular Cardiology (1)
  • PLoS ONE (1)
  • Pflügers Archiv European Journal of Physiology (1)

Keyword

  • kinas (4)
  • protein (4)
  • scienc (4)
  • technolog (4)
  • activ (3)
  • biomedicin (3)
  • cell (3)
  • life (3)
  • phosphoryl (3)
  • 2 (2)
  • adhes (2)
  • biolog (2)
  • express (2)
  • focal (2)
  • gene (2)
  • membran (2)
  • 1 (1)
  • 3 (1)
  • accumul (1)
  • adipocyt (1)
  • adipos (1)
  • atp (1)
  • atpas (1)
  • b (1)
  • ca (1)
  • cancer (1)
  • cardiac (1)
  • cardiolog (1)
  • cardiovascular (1)
  • cjun (1)
  • cmyc (1)
  • collect (1)
  • concentr (1)
  • contractil (1)
  • crista (1)
  • cytoplasm (1)
  • cytoskeleton (1)
  • defect (1)
  • degrad (1)
  • depend (1)
  • differenti (1)
  • dna (1)
  • duct (1)
  • dysfunct (1)
  • echocardiographi (1)
  • endo (1)
  • exchang (1)
  • factor (1)
  • failur (1)
  • function (1)
  • geneexpress (1)
  • glycosyl (1)
  • heal (1)
  • heart (1)
  • heartfailur (1)
  • improv (1)
  • insulin (1)
  • integrin (1)
  • jun (1)
  • lack (1)
  • local (1)
  • mesenchym (1)
  • mice (1)
  • migrat (1)
  • morphogenesi (1)
  • multidisciplinari (1)
  • myc (1)
  • nh (1)
  • nucleoid (1)
  • other (1)
  • par (1)
  • physiolog (1)
  • plasmic (1)
  • polar (1)
  • proteinkinasec (1)
  • receptor (1)
  • releas (1)
  • reticulum (1)
  • sarco (1)
  • sarcoendoplasm (1)
  • serca (1)
  • serin (1)
  • sialyl (1)
  • sialyltransferas (1)
  • signal (1)
  • substrat (1)
  • system (1)
  • termin (1)
  • tissu (1)
  • topic (1)
  • transport (1)
  • turnov (1)
  • tyrosin (1)
  • urea (1)
  • ut (1)
  • utb (1)
  • wound (1)

Author department

  • Medicine: Cardiology (2)
  • Global Health (1)
  • Medicine: Admin (1)
  • Medicine: Nephrology (1)
  • Pathology: Admin (1)
  • Physiology: Admin (1)

Search Results for all work with filters:

  • Biology, Cell
  • Biology, Physiology
  • c

Work 1-5 of 5

Sorted by relevance

Article

Mitochondrial Dysfunction and Adipogenic Reduction by Prohibitin Silencing in 3T3-L1 Cells

by Dong Liu; Yiming Lin; Ting Kang; Bo Huang; Wei Xu; Minerva Garcia-Barrio; Moshood Olatinwo; Roland Matthews; Y. Eugene Chen; Winston E. Thompson

2012

Subjects
  • Biology, Genetics
  • Health Sciences, Oncology
  • Biology, Cell
  • Biology, Physiology
  • Health Sciences, Obstetrics and Gynecology
  • File Download
  • View Abstract

Abstract:Close

Increase in mitochondrial biogenesis has been shown to accompany brown and white adipose cell differentiation. Prohibitins (PHBs), comprised of two evolutionarily conserved proteins, prohibitin-1 (PHB1) and prohibitin-2 (PHB2), are present in a high molecular-weight complex in the inner membrane of mitochondria. However, little is known about the effect of mitochondrial PHBs in adipogenesis. In the present study, we demonstrate that the levels of both PHB1 and PHB2 are significantly increased during adipogenesis of 3T3-L1 preadipocytes, especially in mitochondria. Knockdown of PHB1 or PHB2 by oligonucleotide siRNA significantly reduced the expression of adipogenic markers, the accumulation of lipids and the phosphorylation of extracellular signal-regulated kinases. In addition, fragmentation of mitochondrial reticulum, loss of mitochondrial cristae, reduction of mitochondrial content, impairment of mitochondrial complex I activity and excessive production of ROS were observed upon PHB-silencing in 3T3-L1 cells. Our results suggest that PHBs are critical mediators in promoting 3T3-L1 adipocyte differentiation and may be the potential targets for obesity therapies.

Article

Syndecan-4/PAR-3 signaling regulates focal adhesion dynamics in mesenchymal cells

by Alejandra Valdivia; Areli Cardenas; Marianne Brenet; Horacio Maldonado; Milene Kong; Jorge Diaz; Keith Burridge; Pascal Schneider; Alejandra San Martin; Rafael Garcia-Mata; Andrew F. G. Quest; Lisette Leyton

2020

Subjects
  • Biology, Cell
  • Biology, Microbiology
  • Health Sciences, Oncology
  • Biology, Physiology
  • File Download
  • View Abstract

Abstract:Close

Background Syndecans regulate cell migration thus having key roles in scarring and wound healing processes. Our previous results have shown that Thy-1/CD90 can engage both αvβ3 integrin and Syndecan-4 expressed on the surface of astrocytes to induce cell migration. Despite a well-described role of Syndecan-4 during cell movement, information is scarce regarding specific Syndecan-4 partners involved in Thy-1/CD90-stimulated cell migration. Methods Mass spectrometry (MS) analysis of complexes precipitated with the Syndecan-4 cytoplasmic tail peptide was used to identify potential Syndecan-4-binding partners. The interactions found by MS were validated by immunoprecipitation and proximity ligation assays. The conducted research employed an array of genetic, biochemical and pharmacological approaches, including: PAR-3, Syndecan-4 and Tiam1 silencing, active Rac1 GEFs affinity precipitation, and video microscopy. Results We identified PAR-3 as a Syndecan-4-binding protein. Its interaction depended on the carboxy-terminal EFYA sequence present on Syndecan-4. In astrocytes where PAR-3 expression was reduced, Thy-1-induced cell migration and focal adhesion disassembly was impaired. This effect was associated with a sustained Focal Adhesion Kinase activation in the siRNA-PAR-3 treated cells. Our data also show that Thy-1/CD90 activates Tiam1, a PAR-3 effector. Additionally, we found that after Syndecan-4 silencing, Tiam1 activation was decreased and it was no longer recruited to the membrane. Syndecan-4/PAR-3 interaction and the alteration in focal adhesion dynamics were validated in mouse embryonic fibroblast (MEF) cells, thereby identifying this novel Syndecan-4/PAR-3 signaling complex as a general mechanism for mesenchymal cell migration involved in Thy-1/CD90 stimulation. Conclusions The newly identified Syndecan-4/PAR-3 signaling complex participates in Thy-1/CD90-induced focal adhesion disassembly in mesenchymal cells. The mechanism involves focal adhesion kinase dephosphorylation and Tiam1 activation downstream of Syndecan-4/PAR-3 signaling complex formation. Additionally, PAR-3 is defined here as a novel adhesome-associated component with an essential role in focal adhesion disassembly during polarized cell migration. These novel findings uncover signaling mechanisms regulating cell migration, thereby opening up new avenues for future research on Syndecan-4/PAR-3 signaling in processes such as wound healing and scarring.

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

Vascular smooth muscle insulin resistance, but not hypertrophic signaling, is independent of angiotensin II-induced IRS-1 phosphorylation by JNK

by Hirofumi Hitomi; Puja K. Mehta; Yoshihiro Taniyama; Bernard P Lassegue; Bonnie Seidel-Rogol; Alejandra San Martin Almeyda; Kathy Griendling

2011

Subjects
  • Biology, Cell
  • Biology, Physiology
  • View on PubMed Central
  • View Abstract

Abstract:Close

Angiotensin II (ANG II) has been implicated in the pathogenesis of diabetic micro- and macrovascular disease. In vascular smooth muscle cells (VSMCs), ANG II phosphorylates and degrades insulin receptor substrate-1 (IRS-1). While the pathway responsible for IRS-1 degradation in this system is unknown, c-Jun NH2-terminal kinase (JNK) has been linked with serine phosphorylation of IRS-1 and insulin resistance. We investigated the role of JNK in ANG II-induced IRS-1 phosphorylation, degradation, Akt activation, glucose uptake, and hypertrophic signaling, focusing on three IRS-1 phosphorylation sites: Ser302, Ser307, and Ser632. Maximal IRS-1 phosphorylation on Ser632 occurred at 5 min, on Ser307 at 30 min, and on Ser302 at 60 min. The JNK inhibitor SP600125 reduced ANG II-induced IRS-1 Ser307 phosphorylation (by 80%), IRS-1 Ser302 phosphorylation (by 70%), and IRS-1 Ser632 phosphorylation (by 50%). However, JNK inhibition had no effect on ANG II-mediated IRS-1 degradation, nor did it reverse the ANG II-induced decrease in Akt phosphorylation or glucose uptake. Transfection of VSMCs with mutants S307A, S302A, or S632A of IRS-1 did not block ANG II-mediated IRS-1 degradation. In contrast, JNK inhibition attenuated insulin-induced upregulation of collagen and smooth muscle α-actin in ANG II-pretreated cells. We conclude that phosphorylation of Ser307, Ser302, and Ser632 of IRS-1 is not involved in ANG II-mediated IRS-1 degradation, and that JNK alone does not mediate ANG II-stimulated IRS-1 degradation, but rather is responsible for the hypertrophic effects of insulin on smooth muscle.

Article

Cardiomyocyte-specific expression of CRNK, the C-terminal domain of PYK2, maintains ventricular function and slows ventricular remodeling in a mouse model of dilated cardiomyopathy

by Yevgeniya E. Koshman; Miensheng Chu; Taehoon Kim; Olivia Kalmanson; Mariam Farjah; Mohit Kumar; William Lewis; David L. Geenen; Pieter de Tombe; Paul H. Goldspink; R. John Solaro; Allen M. Samarel

2014

Subjects
  • Health Sciences, Medicine and Surgery
  • Biology, Physiology
  • Biology, Cell
  • File Download
  • View Abstract

Abstract:Close

Up-regulation and activation of PYK2, a member of the FAK family of protein tyrosine kinases, is involved in the pathogenesis of left ventricular (LV) remodeling and heart failure (HF). PYK2 activation can be prevented by CRNK, the C-terminal domain of PYK2. We previously demonstrated that adenoviral-mediated CRNK gene transfer improved survival and LV function, and slowed LV remodeling in a rat model of coronary artery ligation-induced HF. We now interrogate whether cardiomyocyte-specific, transgenic CRNK expression prevents LV remodeling and HF in a mouse model of dilated cardiomyopathy (DCM) caused by constitutively active Protein Kinase Cε (caPKCε). Transgenic (TG; FVB/N background) mice were engineered to express rat CRNK under control of the α-myosin heavy chain promoter, and crossed with FVB/N mice with cardiomyocyte-specific expression of caPKCε to create double TG mice. LV structure, function, and gene expression were evaluated in all 4 groups (nonTG FVB/N; caPKCε(+/-); CRNK(+/-); and caPKCε×CRNK (PXC) double TG mice) at 1, 3, 6, 9 and 12mo of age. CRNK expression followed a Mendelian distribution, and CRNK mice developed and survived normally through 12mo. Cardiac structure, function and selected gene expression of CRNK mice were similar to nonTG littermates. CRNK had no effect on caPKCε expression and vice versa. PYK2 was up-regulated ~6-fold in caPKCε mice, who developed a non-hypertrophic, progressive DCM with reduced systolic (Contractility Index=151±5 vs. 90±4s-1) and diastolic (Tau=7.5±0.5 vs. 14.7±1.3ms) function, and LV dilatation (LV Remodeling Index (LVRI)=4.2±0.1 vs. 6.0±0.3 for FVB/N vs. caPKCε mice, respectively; P<0.05 for each at 12mo). In double TG PXC mice, CRNK expression significantly prolonged survival, improved contractile function (Contractile Index=115±8s-1; Tau=9.5±1.0ms), and reduced LV remodeling (LVRI=4.9±0.1). Cardiomyocyte-specific expression of CRNK improves contractile function and slows LV remodeling in a mouse model of DCM.
Site Statistics
  • 28,340
  • Total Works
  • 7,480,631
  • Downloads
  • 97,570
  • Downloads This Year
  • 6,807
  • Faculty Profiles

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 Recent and Popular Items
Download now