title: Increased compliance in diaphragm muscle of the cardiomyopathic Syrian hamster.
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 (sigma) and strain (epsilon): sigma = (Eo/beta) (ebetaepsilon - 1), where Eo is the initial elastic modulus and beta 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 beta 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 micrometer, 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.
authors.affiliation: Laboratoire d'Optique Appliquée-Ecole Polytechnique, Institut National de la Santé et de la Recherche MédicaleU451, 91125 Palaiseau cedex, France. coirault@enstay.ensta.fr
authors.forename: C
authors.initials: C
authors.lastname: Coirault
authors.forename: J L
authors.initials: JL
authors.lastname: Samuel
authors.forename: D
authors.initials: D
authors.lastname: Chemla
authors.forename: J C
authors.initials: JC
authors.lastname: Pourny
authors.forename: F
authors.initials: F
authors.lastname: Lambert
authors.forename: F
authors.initials: F
authors.lastname: Marotte
authors.forename: Y
authors.initials: Y
authors.lastname: Lecarpentier
mesh_terms: D000818:Animals; D002311:Cardiomyopathy, Dilated / Q000473:pathology / Q000503:physiopathology*; D003094:Collagen / Q000378:metabolism; D003187:Compliance; D064211:Connectin; D006224:Cricetinae; D003964:Diaphragm / Q000473:pathology / Q000503:physiopathology* / Q000648:ultrastructure; D007150:Immunohistochemistry; D066298:In Vitro Techniques; D007797:Laminin / Q000378:metabolism; D008297:Male; D008565:Membrane Proteins / Q000378:metabolism; D008647:Mesocricetus; D018485:Muscle Fibers, Skeletal / Q000502:physiology / Q000648:ultrastructure; D009124:Muscle Proteins / Q000378:metabolism; D011494:Protein Kinases / Q000378:metabolism; D012518:Sarcomeres / Q000502:physiology / Q000648:ultrastructure
chemical_list: D064211:Connectin; D007797:Laminin; D008565:Membrane Proteins; D009124:Muscle Proteins; D003094:Collagen; D011494:Protein Kinases