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Functional and biochemical modifications in skeletal muscles from malarial mice
Author(s) -
Brotto Marco A. P.,
Marrelli Mauro T.,
Brotto Leticia S.,
JacobsLorena Marcelo,
Nosek Thomas M.
Publication year - 2005
Publication title -
experimental physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.925
H-Index - 101
eISSN - 1469-445X
pISSN - 0958-0670
DOI - 10.1113/expphysiol.2004.028316
Subject(s) - isometric exercise , skeletal muscle , myosin , myofilament , plasmodium berghei , troponin , medicine , biology , contracture , chemistry , muscle contraction , endocrinology , anatomy , biochemistry , malaria , immunology , genetics , myocardial infarction
Although it is well established that patients suffering from malaria experience skeletal muscle problems (contracture, aches, fatigue, weakness), detailed studies have not been performed to investigate changes in the contractile function and biochemical properties of intact and skinned skeletal muscles of mammals infected with malaria. To this end, we investigated such features in the extensor digitorium longus (EDL, fast‐twitch, glyocolytic) and in the soleus (SOL, slow‐twitch, oxidative) muscles from mice infected with Plasmodium berghei . We first studied maximal tetanic force ( T max ) produced by intact control and malaria‐infected muscles before, during and after fatigue. Triton‐skinned muscle fibres were isolated from these muscles and used to determine isometric contractile features as well as a basic biochemical profile as analysed by silver‐enhanced SDS‐PAGE. We found that the T max of intact muscles and the maximal Ca 2+ ‐activated force ( F max ) of Triton‐skinned muscle fibres were reduced by ∼50% in malarial muscles. In addition, the contractile proteins of Triton‐skinned muscle fibres from malarial muscles were significantly less sensitive to Ca 2+ . Biochemical analysis revealed that there was a significant loss of essential contractile proteins (e.g. troponins and myosin) in Triton‐skinned muscle fibres from malarial muscles as compared to controls. The biochemical alterations (i.e., reduction of essential contractile proteins) seem to explain well the functional modifications resolved in both intact muscles and Triton‐skinned muscle fibres and may provide a suitable paradigm for the aetiology of muscle symptoms associated with malaria.