Sarcoplasmic reticulum of human skeletal muscle: age‐related changes and effect of trainirig

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Abstract
The effect of ageing on human skeletal muscle was investigated using needle biopsies from young and aged subjects and from aged subjects trained with different activity patterns. Histochemical staining for myofibrillar ATPase of ageing m. vastus lateralis demonstrated an unchanged fibre type distribution but a selective atrophy of type IIa and type IIb fibres. Analysis of myosin heavy chain (MHC) composition showed that type I MHC increased with ageing (P<0.05). The relative content of the MHC isoforms correlated with the relative area of the respective fibre types. Sarcoplasmic reticulum (SR) proteins were investigated in muscle extracts by electrophoretic and immunoblotting techniques. When compared to a young control group (28 0.1 years old,n =7) blots of post‐myofibrillar supernatant proteins probed with polyclonal antibodies to the rabbit fast SR Ca‐ATPase, a marker of extrajunctional SR, showed that the content of Ca‐ATPase was significantly lower (P< 0.05) in the old control group (68 ± 0.5 years old,n= 8). On the other hand the content of calsequestrin (CS), the major intraluminal protein of SR terminal cisternae (TC), and of the 350‐kDa ryanodine‐binding protein, which is localized in the junctional regions of TC, did not show a concomitant decrease. These results suggest that ageing differentially affects extrajunctional and junctional SR of human skeletal muscle. These age‐related changes were not observed within a group of old strength‐trained subjects.