Structure and macromolecular composition of the myotendineal junction. Histochemical, immunohistochemical and electron microscopic study of the rat calf muscles.
L Józsa, M Kvist, P Kannus, T Vieno, M Järvinen, M Lehto
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引用次数: 0
Abstract
The macromolecular composition and ultrastructure of the myotendineal junction (MTJ) of slow-twitch (type 1) and fast-twitch (type 2) muscle fibers were studied in the gastrocnemius-soleus-Achilles unit of the rat. Both proteoglycans and glycosaminoglycans, type III collagen, fibronectin and laminin could be detected at the MTJ. Due to membrane folding, finger-like processes were seen at the myotendineal junction. The processes of the type 1 fibers are greater in size, however, due to subdivisions, the processes of type 2 muscle fibers had a greater surface than type 1 fibers. The macromolecular composition is similar in both type 1 and type 2 muscle fibers.
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