scholarly journals Over Expression of Plk1 Does Not Induce Cell Division in Rat Cardiac Myocytes In Vitro

PLoS ONE ◽  
2009 ◽  
Vol 4 (8) ◽  
pp. e6752 ◽  
Author(s):  
Carmen H. Coxon ◽  
Katrina A. Bicknell ◽  
Fleur L. Moseley ◽  
Gavin Brooks
Keyword(s):  
Cell Division ◽  
Cardiac Myocytes ◽  
Over Expression ◽  
Induce Cell Division ◽  
Rat Cardiac Myocytes

scholarly journals Induced cardiac myocytes apoptosis in vitro by microRNA-122 over expression

Heart ◽  
2011 ◽  
Vol 97 (Suppl 3) ◽  
pp. A40-A40
Author(s):  
Yangdeye ◽  
F. Huang ◽  
X. Huang ◽  
X. Shi ◽  
Z.-q. Huang ◽  
...  
Keyword(s):  
Cardiac Myocytes ◽  
Over Expression

scholarly journals Cellular Physiology of Rat Cardiac Myocytes in Cardiac Fibrosis: In Vitro Simulation Using the Cardiac Myocyte/Cardiac Non-Myocyte Co-Culture System

2008 ◽  
Vol 31 (4) ◽  
pp. 693-706 ◽  
Author(s):  
Keiichi Ikeda ◽  
Katsuyoshi Tojo ◽  
Takashi Udagawa ◽  
Chikara Otsubo ◽  
Masahiro Ishikawa ◽  
...  
Keyword(s):  
Cardiac Myocytes ◽  
Culture System ◽  
Cardiac Fibrosis ◽  
Cardiac Myocyte ◽  
Cellular Physiology ◽  
In Vitro Simulation ◽  
Rat Cardiac Myocytes

Cytosolic pH measurements in single cardiac myocytes using carboxy-seminaphthorhodafluor-1

1992 ◽  
Vol 263 (1) ◽  
pp. H276-H284 ◽  
Author(s):  
P. S. Blank ◽  
H. S. Silverman ◽  
O. Y. Chung ◽  
B. A. Hogue ◽  
M. D. Stern ◽  
...  
Keyword(s):  
Cardiac Myocytes ◽  
Spectral Feature ◽  
Ph Measurements ◽  
Dual Emission ◽  
Cytosolic Ph ◽  
Ph Gradients ◽  
In Situ Calibration ◽  
Rat Cardiac Myocytes

This study examines the use of carboxy-seminaphthorhodafluor-1 (C-SNARF-1) as an indicator of cytosolic pH in isolated rat cardiac myocytes. The emission spectrum of C-SNARF-1 when excited at 530 nm contains two well-separated peaks at approximately 590 and 640 nm, corresponding to the acidic and basic forms of the indicator. This spectral feature allows the indicator to be used in the single excitation, dual emission ratio mode. When C-SNARF-1 is loaded into rat cardiac myocytes as the membrane permeant ester derivative, C-SNARF-1/AM, the indicator localizes within the cytosol with virtually no partitioning into the mitochondria. C-SNARF-1 does not load into isolated mitochondria in suspension. There was no evidence for the presence of non-deesterified C-SNARF-1 within the cells. C-SNARF-1 can be calibrated in situ using a technique that abolishes all transsarcolemmal pH gradients. A 0.7-unit shift in the apparent pK (pKapp = pK-log10) between the in vitro calibration and the in situ calibration is consistent with a change in beta (I640 to pH 9/I640 at pH 5) in the cytosolic environment (beta in situ/beta in vitro = 0.21) and not a change in the true pK of the indicator. The contribution of cellular autofluorescence to the total signal can be made negligible. There is no effect of C-SNARF-1 on the contractile properties of rat cardiac myocytes.(ABSTRACT TRUNCATED AT 250 WORDS)

scholarly journals Involvement of Cardiotrophin-1 in Cardiac Myocyte-Nonmyocyte Interactions During Hypertrophy of Rat Cardiac Myocytes In Vitro

Circulation ◽  
1999 ◽  
Vol 100 (10) ◽  
pp. 1116-1124 ◽  
Author(s):  
Koichiro Kuwahara ◽  
Yoshihiko Saito ◽  
Masaki Harada ◽  
Masahiro Ishikawa ◽  
Emiko Ogawa ◽  
...  
Keyword(s):  
Cardiac Myocytes ◽  
Cardiac Myocyte ◽  
Rat Cardiac Myocytes

Gene silencing in adult rat cardiac myocytes in vitro by adenovirus-mediated RNA interference

2006 ◽  
Vol 27 (5-7) ◽  
pp. 413-421 ◽  
Author(s):  
Andreas Rinne ◽  
Christoph Littwitz ◽  
Marie-Cécile Kienitz ◽  
Andreas Gmerek ◽  
Leif I. Bösche ◽  
...  
Keyword(s):  
Rna Interference ◽  
Gene Silencing ◽  
Cardiac Myocytes ◽  
Adult Rat ◽  
Rat Cardiac Myocytes

scholarly journals Expression of myosin isoenzymes in cardiac-muscle cells in culture

1984 ◽  
Vol 221 (1) ◽  
pp. 21-26 ◽  
Author(s):  
A C Nag ◽  
M Cheng
Keyword(s):  
Atpase Activity ◽  
Cardiac Myocytes ◽  
Electrophoretic Pattern ◽  
Adult Type ◽  
Adult Chicken ◽  
Myosin Isoenzyme ◽  
Rat Myocytes ◽  
Rat Cardiac Myocytes

Myosin isoenzyme profiles of rat and chicken embryonic cardiac myocytes were studied during differentiation and growth in vitro by native-gel electrophoresis and assay of Ca2+-activated ATPase. The electrophoretic pattern of myosin extracted from 18-day-embryonic-rat myocytes after 7 days in culture exhibits three isoenzyme bands, V1, V2 and V3, of which the slow-migrating V3 is predominant. This resembles the isoenzyme profiles from 18-20-day-embryonic ventricles in vivo. However, the isoenzyme profile of the 7-day-old culture differs from that of its counterpart in vivo, as well as from that of the young and adult rat ventricles, the last two containing the predominant fast-migrating component, V1. When embryonic cardiac myocytes were grown in vitro for 7 days in a medium containing a physiological concentration of L-thyroxine (T4), myosin isoenzyme profiles of these cells shifted to the adult form, with isoenzyme V1 predominating after day 4 of culture. The 7-day-old intact embryonic-chicken ventricles and isolated myocytes showed a single myosin isoenzyme band after 7 days of culture that resembles the pattern seen for the adult chicken. T4 had no effect on the electrophoretic mobility of this isoenzyme pattern. ATPase activity of isoenzyme V1 in cultured rat myocytes treated with T4 was comparable with that of V1 in the untreated adult heart. This study demonstrates that ATPase activity of the chicken myosin isoenzyme is significantly lower than that of isoenzyme V1, but is comparable with that of rat V3. This study shows that the expression of myosin isoenzyme profiles in cultured rat cardiac myocytes does not fully represent the situation in vivo. Physiological concentrations of T4 can modulate the predominant foetal-type isoenzyme V3 to the adult type V1 in cultured embryonic-rat cardiac myocytes within a brief period.

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