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  • About
  • The Global ETD Search service is a free service for researchers to find electronic theses and dissertations. This service is provided by the Networked Digital Library of Theses and Dissertations.
    Our metadata is collected from universities around the world. If you manage a university/consortium/country archive and want to be added, details can be found on the NDLTD website.
91

EXPRESSION OF THE EXTRACELLULAR NUCLEOTIDE DIPHOSPHOHYDROLASE, NTPDASE2, IS DOWN-REGULATED IN PRIMARY CHOLANGIOPATHIES

Toure, Joahd 01 July 2003 (has links)
Portal fibroblasts are newly discovered liver cells that may be of particular importance in biliary fibrosis. Recent data indicate that portal fibroblasts express NTPDase2, an ecto-nucleoside triphosphate diphosphohydrolase. Portal fibroblasts exist within the peri-portal regions of rat livers and express NTPDase2 adjacent to the basolateral side of intrahepatic bile ducts. Because extracellular nucleotides regulate secretion via activation of P2Y purinergic receptors, extracellular nucleotide hydrolysis via NTPDase2 makes NTPDase2 a potential regulator of bile ductular secretion. We propose that NTPDase2 expression may be altered in biliary fibrosis, especially in conditions in which bile duct epithelia are the target of disease. To test this hypothesis we have contrasted the distribution of NTPDase2 in normal and diseased liver states. Using confocal immunofluorescence, we assessed differences in expression of NTPDase2 in liver biopsy specimens from normal liver, primary biliary cirrhosis (PBC), and hepatitis C (HepC). We found that NTPDase2 was down regulated in the peri-portal regions of patients with PBC when compared to normal patients. Hepatitis C, however, showed NTPDase2 staining equal to or nearly equal to that of normal liver. The intermediate filament vimentin was down regulated in both PBC and Hep C when compared to normal liver. We conclude that NTPDase2 expression is down regulated in PBC but not Hep C, while vimentin is down regulated in both disease states when compared to normal liver.
92

Nde1-mediated inhibition of ciliogenesis controls cell cycle re-entry

Kim, Sehyun. January 2009 (has links) (PDF)
Thesis (Ph. D.)--University of Oklahoma. / Bibliography: leaves 118-130.
93

Seawater survival and osmoregulation of Atlantic salmon (Salmo salar) parr-smolts exposed to four different pesticides

Hauta, Christopher Carl 24 February 2014 (has links)
Atlantic salmon (Salmo salar) parr-smolts were exposed to sublethal concentrations of cypermethrin, chlorothalonil, quintozene or atrazine to determine if they affected osmoregulation. After 96 h of exposure to a pesticide, Na+K+-ATPase, hematocrit, liver somatic index (LSI), plasma sodium, chloride, and cortisol concentrations were determined. There were no mortalities observed following a 24-h seawater challenge. No effects were seen with cypermethrin exposure. Chlorothalonil exposure resulted in increases in plasma Na+ concentrations following the seawater challenge in the 0.18 and 3.6 μg/L groups. For quintozene, decreases in LSI was seen at each concentration, and decreases in Na+K+-ATPase activity was seen at 0.55 μg/L as well as a decrease in Na+ concentrations at the highest exposure concentration. Atrazine exposure increased Na+K+-ATPase activity in the 1 and 100 μg/L groups, and plasma cortisol concentrations at100 μg/L. Overall, the pesticides examined had minimal effects on fish osmoregulation and stress at the concentrations tested.
94

Expanding the Role of Electron Cryomicroscopy in Structural Analysis of Asymmetrical Protein Complexes

Keating, Shawn 18 March 2013 (has links)
Single particle electron cryomicroscopy (cryo-EM) is a rapidly developing structural biology technique for the study of macromolecular protein complexes. Presently, cryo-EM fills an important niche by facilitating acquisition of 3-D structures of protein complexes not amenable to structure determination by other techniques. Expansion of cryo-EM beyond this niche requires continued improvement in the types of specimens that can be studied as well as the final resolutions achieved. Two studies were undertaken to address these issues. The first examined resolution limitations by quantifying the effect of beam-induced motion in images of beam-sensitive paraffin crystals. The second explored the possibility of using cryo-EM to study the interaction of small effector proteins with a large multi-protein complex, V-ATPase. The results of these studies exposed the fact that fundamental aspects of the imaging and specimen preparation processes remain poorly understood and must be addressed to facilitate future improvements in cryo-EM structure determination.
95

Novel aspects of Na⁺,K⁺-ATPase /

Aizman, Oleg, January 2002 (has links)
Diss. (sammanfattning) Stockholm : Karol. inst., 2002. / Härtill 6 uppsatser.
96

Imaging studies of cell physiology with particular reference to Na,K-ATPase function /

Andersson, Ronnie M., January 2003 (has links)
Diss. (sammanfattning) Stockholm : Karol. inst., 2003. / Härtill 6 uppsatser.
97

Digoxin and exercise effects on Na+, K+-ATPase isoform gene and protein expression in human skeletal muscle

Gong, Xiaofei. January 2006 (has links)
Thesis (M. App. Sc.)--Victoria University (Melbourne, Vic.), 2006. / Includes bibliographical references.
98

Membrane lipid composition and its effect on sodium pump molecular activity a comparative study /

Turner, Nigel. January 2003 (has links)
Thesis (Ph.D.)--University of Wollongong, 2003. / Typescript. Includes bibliographical references: leaf 168-188.
99

Cryo-electron microscopy of Ca²⁺-ATPase from sarcoplasmic reticulum /

Zhang, Peijun. January 1998 (has links)
Thesis (Ph. D.)--University of Virginia, 1998. / Spine title: Cryo-EM of Ca²⁺-ATPase from SR. Includes bibliographical references (p. 149-159). Also available online through Digital Dissertations.
100

Temporal and steric analysis of ionic permeation and binding in Na+, K+-ATPase via molecular dynamic simulations

Fonseca, James Ernest. January 2008 (has links)
Thesis (Ph.D.)--Ohio University, June, 2008. / Title from PDF t.p. Includes bibliographical references.

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