Fine structure of the myotendinous junction of lathyritic rat muscle with special reference to connectin, a muscle elastic protein.
The fine structure of the myotendinous junction of the skeletal muscle of lathyritic rats caused by beta-aminopropionitrile was investigated. In the junction there are finger-like processes of muscle fibers, in which thin filaments were extended from the last Z lines of myofibrils and attached to the sarcolemma of the processes. By the heavy meromyosin decoration technique, these thin filaments were identified as actin filaments. In the lathyritic muscle, the thin filaments were markedly fewer in number and distributed sparsely in the sarcoplasm. The content of connectin, an elastic protein, which is localized in myofibrils and also in sarcolemma was significantly decreased in the lathyritic muscle. A possible relationship between the changes in the fine structure of the myotendinous junction and in the connectin contents is discussed.
D000629:Aminopropionitrile; D000818:Animals; D003094:Collagen; D007842:Lathyrism / Q000139:chemically induced / Q000473:pathology*; D009124:Muscle Proteins / Q000032:analysis*; D009132:Muscles / Q000032:analysis / Q000648:ultrastructure*; D009210:Myofibrils / Q000648:ultrastructure; D051381:Rats; D012508:Sarcolemma / Q000648:ultrastructure; D012519:Sarcoplasmic Reticulum / Q000648:ultrastructure; D013710:Tendons
D009124:Muscle Proteins; D000629:Aminopropionitrile; D003094:Collagen