Literature DB >> 11485856

Interaction between sarcomere and mitochondrial length in normoxic and hypoxic rat ventricular papillary muscles.

T Nozaki1, Y Kagaya, N Ishide, S Kitada, M Miura, J Nawata, I Ohno, J Watanabe, K Shirato.   

Abstract

We hypothesized that the mitochondrial length may be altered according to changes in the sarcomere length, and that this relationship may be affected by exposure to hypoxia. Rat ventricular papillary muscles were isolated and immersed in normoxic or hypoxic solutions for 10 min. Sarcomeres of various lengths were obtained by fixing the papillary muscles in a slack or stretched state, or after exposure to a contracture solution containing saponin and CaCl(2). The mitochondrial length measured using electron microscopy significantly correlated to the length of the adjacent sarcomere in both the normoxic (n=767) and hypoxic (n=1145) groups (P<.0001). The slope of the regression line, however, was significantly less steep, and its intercept was significantly larger in the hypoxic group than in the normoxic group (analysis of covariance). When we analyzed the mitochondrial lengths among the three sarcomere-length subgroups (<1.5, 1.5-2.0, and >2.0 microm), the mitochondrial length was significantly shorter in the hypoxic condition than in the normoxic condition at sarcomere lengths greater than 2.0 microm. Staining for desmin, the major muscle-type intermediate filament, the longitudinal system of which connects the mitochondria with the Z bands of sarcomeres, showed a clear cross-striation pattern in both papillary muscles with and without the exposure to hypoxia, suggesting that desmin was preserved after the exposure to hypoxia. These data indicate that the mitochondrial length changes according to changes in the sarcomere length, suggesting the possible role of mitochondria as an internal load against myocyte contraction. It is also suggested that mitochondria exposed to hypoxia may be more resistive to both compression and stretch in a longitudinal direction than those in the normoxic condition.

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Year:  2001        PMID: 11485856     DOI: 10.1016/s1054-8807(01)00071-0

Source DB:  PubMed          Journal:  Cardiovasc Pathol        ISSN: 1054-8807            Impact factor:   2.185


  12 in total

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2.  Studies of mitochondrial respiration in muscle cells in situ: use and misuse of experimental evidence in mathematical modelling.

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3.  Intracellular diffusion of adenosine phosphates is locally restricted in cardiac muscle.

Authors:  Marko Vendelin; Margus Eimre; Evelin Seppet; Nadezda Peet; Tatiana Andrienko; Maris Lemba; Jiiri Engelbrecht; Enn K Seppet; Valdur A Saks
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4.  Fully automated software for quantitative measurements of mitochondrial morphology.

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5.  Structure-function relationships in the regulation of energy transfer between mitochondria and ATPases in cardiac cells.

Authors:  Enn K Seppet; Margus Eimre; Tiia Anmann; Evelin Seppet; Andres Piirsoo; Nadezhda Peet; Kalju Paju; Rita Guzun; Nathalie Beraud; Sophie Pelloux; Yves Tourneur; Andrey V Kuznetsov; Tuuli Käämbre; Peeter Sikk; Valdur A Saks
Journal:  Exp Clin Cardiol       Date:  2006

6.  Intracellular energetic units in healthy and diseased hearts.

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Review 8.  Engineering cardiac microphysiological systems to model pathological extracellular matrix remodeling.

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9.  IgG from patients with liver diseases inhibit mitochondrial respiration in permeabilized oxidative muscle cells: impaired function of intracellular energetic units?

Authors:  Lumme Kadaja; Kai E Kisand; Nadezhda Peet; Urmo Braun; Kaja Metsküla; Kaupo Teesalu; Riina Vibo; Kalle V Kisand; Raivo Uibo; Harald Jockusch; Enn K Seppet
Journal:  Mol Cell Biochem       Date:  2004 Jan-Feb       Impact factor: 3.396

10.  Coordinated behavior of mitochondria in both space and time: a reactive oxygen species-activated wave of mitochondrial depolarization.

Authors:  Nathan R Brady; Steven P Elmore; Johannes J H G M van Beek; Klaas Krab; Pierre J Courtoy; Louis Hue; Hans V Westerhoff
Journal:  Biophys J       Date:  2004-09       Impact factor: 4.033

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