title: Contraction parameters, myosin composition and metabolic enzymes of the skeletal muscles of the etruscan shrew Suncus etruscus and of the common European white-toothed shrew Crocidura russula (Insectivora: soricidae).
abstract: In the Etruscan shrew, the isometric twitch contraction times of extensor digitorum longus (EDL) and soleus muscles are shorter than in any other mammal, allowing these muscles to contract at outstandingly high contraction frequencies. This species has the highest mass-specific metabolic rate of all mammals and requires fast skeletal muscles not only for locomotion but also for effective heat production and for an extremely high ventilation rate. No differences could be detected in the fibre type pattern, the myosin heavy and light chain composition, or in the activity of the metabolic enzymes lactate dehydrogenase and citrate synthase of the two limb muscles, the EDL and the soleus, which in larger mammalian species exhibit distinct differences in contractile proteins and metabolic enzymes. All properties determined in EDL and soleus muscles of Suncus etruscus, as well as in the larger Crocidura russula, are typical for fast-oxidative fibres, and the same holds for several other skeletal muscles including the diaphragm muscle of S. etruscus. Nevertheless, the EDL and soleus muscles showed different mechanical properties in the two shrew species. Relaxation times and, in C. russula, time to peak force are shorter in the EDL than in the soleus muscle. This is in accordance with the time course of the Ca(2+) transients in these muscles. Such a result could be due to different parvalbumin concentrations, to a different volume fraction of the sarcoplasmic reticulum in the two muscles or to different Ca(2+)-ATPase activities. Alternatively, the lower content of cytosolic creatine kinase (CK) in the soleus compared with the EDL muscle could indicate that the observed difference in contraction times between these shrew muscles is due to the CK-controlled activity of their sarcoplasmic reticulum Ca(2+)-ATPase.
authors.affiliation: Zentrum Physiologie, Medizinische Hochschule, D 30623 Hannover, Germany.
authors.forename: T
authors.initials: T
authors.lastname: Peters
authors.forename: H P
authors.initials: HP
authors.lastname: Kubis
authors.forename: P
authors.initials: P
authors.lastname: Wetzel
authors.forename: S
authors.initials: S
authors.lastname: Sender
authors.forename: G
authors.initials: G
authors.lastname: Asmussen
authors.forename: R
authors.initials: R
authors.lastname: Fons
authors.forename: K D
authors.initials: KD
authors.lastname: Jürgens
mesh_terms: D000818:Animals; D001481:Basal Metabolism; D001696:Biomechanical Phenomena; D001833:Body Temperature Regulation; D002118:Calcium / Q000378:metabolism; D000252:Calcium-Transporting ATPases / Q000378:metabolism; D002950:Citrate (si)-Synthase / Q000378:metabolism*; D003593:Cytoplasm / Q000378:metabolism; D003964:Diaphragm / Q000201:enzymology; D007700:Kinetics; D007770:L-Lactate Dehydrogenase / Q000378:metabolism*; D009119:Muscle Contraction; D018485:Muscle Fibers, Skeletal / Q000145:classification / Q000201:enzymology; D009124:Muscle Proteins / Q000378:metabolism; D018482:Muscle, Skeletal / Q000737:chemistry / Q000502:physiology*; D009218:Myosins / Q000032:analysis*; D012788:Shrews
chemical_list: D009124:Muscle Proteins; D007770:L-Lactate Dehydrogenase; D002950:Citrate (si)-Synthase; D009218:Myosins; D000252:Calcium-Transporting ATPases; D002118:Calcium