Józsa L, Kvist M, Kannus P, Vieno T, Järvinen M, Lehto M
Department of Morphology, National Institute of Traumatology, Budapest, Hungary.
Acta Morphol Hung. 1991;39(4):287-97.
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.
在大鼠的腓肠肌-比目鱼肌-跟腱单元中，研究了慢肌纤维（1型）和快肌纤维（2型）的肌腱结合处（MTJ）的大分子组成和超微结构。在MTJ处可检测到蛋白聚糖和糖胺聚糖、III型胶原蛋白、纤连蛋白和层粘连蛋白。由于膜折叠，在肌腱结合处可见指状突起。然而，1型纤维的突起尺寸更大，由于细分，2型肌纤维的突起比1型纤维具有更大的表面积。1型和2型肌纤维中的大分子组成相似。
