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Regulation of cardiac myofilament me...

Vahebi, Susan.

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Regulation of cardiac myofilament mechano-energetics by G-protein signaling.

Record Type:	Electronic resources : Monograph/item
Title/Author:	Regulation of cardiac myofilament mechano-energetics by G-protein signaling./
Author:	Vahebi, Susan.
Description:	163 p.
Notes:	Source: Dissertation Abstracts International, Volume: 66-07, Section: B, page: 3598.
Contained By:	Dissertation Abstracts International66-07B.
Subject:	Biophysics, Medical. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3183738
ISBN:	0542250470

Regulation of cardiac myofilament mechano-energetics by G-protein signaling.
Vahebi, Susan.

Regulation of cardiac myofilament mechano-energetics by G-protein signaling. - 163 p.

Source: Dissertation Abstracts International, Volume: 66-07, Section: B, page: 3598.

Thesis (Ph.D.)--University of Illinois at Chicago, Health Sciences Center, 2005.

My overall objective is to test the hypothesis that contractile function and myofilament activity in the heart during cardiac hypertrophy and heart failure may be caused by activation of G-protein signaling cascades, which alter myofilament sensitivity to Ca2+. The result of my study addressed the question how activation of G-protein signaling specifically, Rho associate kinase (ROCK-II), p38 mitogen activated protein kinase (p38alpha MAP kinase) and PKCalpha affect myofilament mechano-energetics.

ISBN: 0542250470Subjects--Topical Terms:

1017681
Biophysics, Medical.

Regulation of cardiac myofilament mechano-energetics by G-protein signaling.
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020 $a 0542250470
035 $a (UnM)AAI3183738
035 $a AAI3183738
040 $a UnM $c UnM
100 1 $a Vahebi, Susan. $3 1905130
245 1 0 $a Regulation of cardiac myofilament mechano-energetics by G-protein signaling.
300 $a 163 p.
500 $a Source: Dissertation Abstracts International, Volume: 66-07, Section: B, page: 3598.
500 $a Adviser: R. John Solaro.
502 $a Thesis (Ph.D.)--University of Illinois at Chicago, Health Sciences Center, 2005.
520 $a My overall objective is to test the hypothesis that contractile function and myofilament activity in the heart during cardiac hypertrophy and heart failure may be caused by activation of G-protein signaling cascades, which alter myofilament sensitivity to Ca2+. The result of my study addressed the question how activation of G-protein signaling specifically, Rho associate kinase (ROCK-II), p38 mitogen activated protein kinase (p38alpha MAP kinase) and PKCalpha affect myofilament mechano-energetics.
520 $a Activation of ROCK-II results in depression of maximum ATPase activity and tension development in detergent extracted (skinned) fiber bundles isolated from mouse left ventricular papillary muscles. Employing TG mouse, exchange experiments, and mass spectrometric analysis we determined that mechanism of depression of maximum force and ATPase activity is independent of ROCK-II phosphorylation of TnI, MLC-2, and C-protein. Depression of maximum tension and ATPase activity in ROCK-II dependent phosphorylation is most probably due to phosphorylation of TnT at a novel phosphorylation site.
520 $a The effect of p38alpha MAP kinase on myofilament contractility was determined by employing two TG mouse models: (1) p38 MAP kinase was constitutively active by an upstream activator (MKK6bE); (2) depressed by expression of a dominant negative p38alpha MAP kinase (DN-p38 [alpha] MAPK). Activation of p38 MAP kinase is associated with dephosphorylation of alpha-Tm, which may account for depression of maximum tension and ATPase activity. Western blot analysis indicates no truncation of alpha-actin alpha-actinin or TnT was observed. There was no Tm or TnT isoform switching was observed in TG-MKK6bE.
520 $a Employing a TG mouse, in which we exchanged the 27 terminal amino acids of alpha-Tm for the corresponding region in beta-Tm, induced a depression in myofilament sensitivity to Ca2+. These data together demonstrate that the C-terminal of alpha-Tm is a critical determinant of sarcomere performance and calcium sensitivity in both the whole heart and in isolated myofilaments.
520 $a Over-expression PKCalpha in TG mouse model resulted in depression of maximum tension and ATPase activity and no change in tension cost in skinned fibers. Knockout PKCalpha in TG mouse model resulted in increase in maximum force and ATPase activity with no change in tension cost in skinned fibers.
590 $a School code: 0806.
650 4 $a Biophysics, Medical. $3 1017681
650 4 $a Biology, Animal Physiology. $3 1017835
650 4 $a Biology, Molecular. $3 1017719
690 $a 0760
690 $a 0433
690 $a 0307
710 2 0 $a University of Illinois at Chicago, Health Sciences Center. $3 1021703
773 0 $t Dissertation Abstracts International $g 66-07B.
790 1 0 $a Solaro, R. John, $e advisor
790 $a 0806
791 $a Ph.D.
792 $a 2005
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3183738