PubMed1985
An investigation was carried out on the sheaths which envelop rat tail tendons. The samples were processed for observation by light and electron microscopy. In the case of electron microscopy, thin sections of specimens embedded in epoxy resin and replicas of freeze etched samples were used. On the basis of histological and ultrastructural observations, four distinct connective tissue sheaths have been detected. The paratendineum is a thick fibrous sheath that covers externally the four groups of tendons arranged around the vertebrae of the tail; the epitendineum is a distinct fibrous sheath surrounding each tendon group; the peritendineum is composed of concentric cellular laminae enveloping each tendon; lastly, the endotendineum is made up of one cellular lamella which adheres to the fibres of the tendon, projecting trabeculae between the individual tendon fascicles. In the para- and epitendineum, thick bundles of collagen fibrils, running parallel to the fibres of the tendon, were visible. The collagen fibrils had a wide variability of diameters (from 35 to 220 nm) and, when examined in replica, their microfibrillar arrangement appeared to be straight. In the peri- and endotendineum, thin bundles of collagen fibrils were visible between the cellular laminae, parallel to the main axis of the tendon. Among these collagen bundles, elastic fibres and numerous glycoproteins containing microfibril-like filaments were visible. The collagen fibrils were small and of uniform diameter (50 nm) and, when observed on replica, showed a helicoidal microfibrillar arrangement. The cell layers of the peri- and endotendineum were made up of flattened fibroblasts which were connected by specialised junctions and which contained numerous micropinocytotic vesicles. A thin layer of granular electron-dense material, with ultrastructural characteristics similar to those of a basement membrane, was visible on the surface of the most external cellular layer of the peritendineum and on the outer surface of the cellular lamella of the endotendineum. Due to their morphological characteristics it is supposed that the four tendon sheaths are involved in different and special functions. Moreover, collagen Type I and collagen Type III, demonstrated by means of immunofluorescence techniques in previous investigations, show respectively a close similarity in distribution to the thick collagen fibrils, with a straight microfibrillar arrangement, of the two external sheaths, and to the thin collagen fibrils, with a helicoidal microfibrillar arrangement, of the two internal sheaths.