Increased compliance in diaphragm muscle of the cardiomyopathic Syrian hamster

Author:

Coirault Catherine1,Samuel Jane-Lyse2,Chemla Denis3,Pourny Jean-Claude1,Lambert Francine1,Marotte Françoise2,Lecarpentier Yves3

Affiliation:

1. Laboratoire d’Optique Appliquée-Ecole Polytechnique, Institut National de la Santé et de la Recherche MédicaleU451, 91125 Palaiseau cedex;

2. Hôpital Lariboisière, Institut National de la Santé et de la Recherche Médicale U127, 75010 Paris; and

3. Service d’Explorations Fonctionnelles, Centre Hospitalier et Universitaire de Bicêtre, 94275 Le Kremlin-Bicêtre, France

Abstract

We investigated the hypothesis that diaphragm compliance was abnormal in cardiomyopathic Syrian hamsters (CSH), an experimental model of myopathy. The passive elastic properties of isolated diaphragm muscles were analyzed at both the muscle and sarcomere levels. We used the following passive exponential relationship between stress (ς) and strain (ε): ς = (Eo/β) ( e βε − 1), where Eo is the initial elastic modulus and β is the stiffness constant. Immunocytochemistry procedures were used to analyze the distribution of two key elastic components of muscle, extracellular collagen and intracellular titin elastic components, as well as the extracellular matrix glycoprotein laminin. Muscle and sarcomere values of β were nearly twofold lower in CSH (8.7 ± 1.9 and 8.3 ± 1.4, respectively) than in control animals (19.7 ± 1.7 and 16.8 ± 2.1, respectively) ( P < 0.01 for each). Compared with controls, Eo was higher in CSH. Sarcomere slack length was significantly longer in CSH than in control animals (2.1 ± 0.1 vs. 1.9 ± 0.1 μm, P < 0.05). The surface area of collagen I was significantly larger in CSH (17.4 ± 1.8%) than in control animals (12.4 ± 0.7%, P< 0.05). There was no change in the distribution of titin or laminin labelings between the groups. These results demonstrate increased diaphragm compliance in cardiomyopathic hamsters. The increase in CSH diaphragm compliance was observed despite an increase in the surface area of collagen and was not associated with an abnormal distribution of titin or laminin.

Publisher

American Physiological Society

Subject

Physiology (medical),Physiology

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