Myofibrillar-protein isoforms and sarcoplasmic-reticulum Ca2+-transport activity of single human muscle fibres.
In this study the polymorphism of myofibrillar proteins and the Ca2+-uptake activity of sarcoplasmic reticulum were analysed in single fibres from human skeletal muscles. Two populations of histochemically identified type-I fibres were found differing in the number of light-chain isoforms of the constituent myosin, whereas the pattern of light chains of fast myosin of type-IIA and type-IIB fibres was indistinguishable. Regulatory proteins, troponin and tropomyosin, and other myofibrillar proteins, such as M- and C-proteins, showed specific isoforms in type-I and type-II fibres. Furthermore, tropomyosin presented different stoichiometries of the alpha- and beta-subunits between the two types of fibres. Sarcoplasmic-reticulum volume, as indicated by the maximum capacity for calcium oxalate accumulation, was almost identical in type-I and type-II fibres, whereas the rate of Ca2+ transport was twice as high in type-II as compared with type-I fibres. It is concluded that, in normal human muscle fibres, there is a tight segregation of fast and slow isoforms of myofibrillar proteins that is very well co-ordinated with the relaxing activity of the sarcoplasmic reticulum. These findings may thus represent a molecular correlation with the differences of the twitch-contraction time between fast and slow human motor units. This tight segregation is partially lost in the muscle fibres of elderly individuals.
D000367:Age Factors; D001692:Biological Transport; D002118:Calcium / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D006801:Humans; D009124:Muscle Proteins / Q000235:genetics / Q000378:metabolism*; D009132:Muscles / Q000378:metabolism*; D009210:Myofibrils / Q000378:metabolism*; D009218:Myosins / Q000378:metabolism; D011110:Polymorphism, Genetic; D012519:Sarcoplasmic Reticulum / Q000378:metabolism*
D009124:Muscle Proteins; D009218:Myosins; D002118:Calcium