Järvinen M, Jozsa L, Kvist M, Lehto M, Vieno T, Isola J, Kannus P
Department of Surgery, University of Tampere, Finland.
Acta Anat (Basel). 1992;145(3):216-9. doi: 10.1159/000147369.
The collagen composition and ultrastructural organization of the myo-fascial junction was studied using immunohistochemical techniques and electron microscopy. At the myo-fascial junction, a small amount of type-III collagen was found; however, the major collagen component was the type-I collagen. On the longitudinal sites of muscle cells, there were deep recesses and, within these, finger-like structures containing sarcomeres. In these recesses and in the finger-like structures of the myo-fascial junction, the sarcolemma was thickened (three times) in a similar way to the basal lamina at the myotendinous junction. Thin collagen fibers were closely associated with the thickened sarcolemma of the finger-like structures.
采用免疫组织化学技术和电子显微镜对肌筋膜连接部的胶原成分和超微结构组织进行了研究。在肌筋膜连接部，发现了少量的III型胶原；然而，主要的胶原成分是I型胶原。在肌细胞的纵切面上，有深陷凹，在这些凹内有含肌节的指状结构。在这些凹以及肌筋膜连接部的指状结构中，肌膜增厚（三倍），其方式与肌腱连接部的基膜相似。细胶原纤维与指状结构增厚的肌膜紧密相连。
