Fine structure of the myotendinous junction and "terminal coupling" in the skeletal muscle of the lamprey, Lampetra japonica.

The myotendinous junction in the skeletal muscle of adult lamprey Lampetra japonica was studied with an electron microscope. Numerous finger-like sarcolemmal invaginations were present at the ends of muscle fibers to form the myotendinous junction. Parietal fibers of each muscle unit showed more closely distributed sarcolemmal invaginations than central fibers. Features of the myotendinous junction generally conform to the accounts in the literature. The sarcolemmal invagination was covered on its sarcoplasmic aspect by the connecting filament layer and the dense amorphous attachment layer, and on the extracellular aspect by the intermediary layer and the external lamina with collagen fibrils arising from the myosepta. Sarcolemmal invaginations were sometimes seen to consist of a pair of sarcolemmas of adjacent muscle fibers within a muscle unit, which is characteristic to the myotendinous junction of lamprey. It is noteworthy that the connecting filament layer is much thinner than that, e. g., in the tadpole tail muscles (Nakao, '74). Furthermore, it is much thicker in the parietal fibers than in the central fibers. The sarcolemma of the terminal segment of the invagination frequently showed specific coupling with cisterns of the sarcoplasmic reticulum (terminal coupling). The external lamina is partially or completely deficient in the terminal segment of sarcolemmal invaginations which form terminal couplings so that collagen fibrils contained in the invagination appear to be in direct contact with the sarcolemma; however, definite relationships of collagen fibrils with the sarcolemma and the external lamina in the terminal segment of invagination still remain obscure. This type of coupling is considered to play a role in the coupling of excitation to contraction of muscle fibers as triads and diads.     

Macromolecular composition of the myotendinous junction.

The macromolecular composition of the myotendinous junction of the rat Achilles tendon was investigated. Heparan sulphate, chondroitin sulphate, and/or dermatan sulphate could be detected in the terminal processes of the muscle cells, but neither heparin nor keratan sulphate was present. The presence of hyaluronic acid was also questionable. High concentrations of sulphate containing glycosaminoglycans could be demonstrated both in the sarcolemma membranes and extracellular region. The main collagenous component in the myotendinous junction was type I collagen. Also small amounts of type III collagen was found at the myotendinous interface. In addition, high concentrations of fibronectin was present on the muscle cell surfaces of the junction. These results showed that myotendinous junction is histochemically and immunohistochemically a highly specified area rich in various polysaccharides. The high concentration of the polysaccharides in the myotendinous interface may increase the adhesive force between the muscle cell membrane and tendineal collagen fibrils and, by this way, it may be important in improving the elastic buffer capacity of the junction against loading.     

Ultrastructure of myotendinous junctions in Myxine and rat specializations between the plasma membrane and the lamina densa

Summary Myotendinous junctions in the parietal muscle of the Atlantic hagfish (Myxine glutinosa, L.) and in the diaphragm of rat were studied with the electron microscope.The ends of muscle fibers posses deep tube-like invaginations and also finger-like processes. Terminal I-filaments of the myofibrils attach to the plasma membrane of the invaginations. Collagen fibrils of the tendon attach to the external aspect of the lamina densa. The lamina densa and also collagen fibrils continue into the invaginations.Specializations are present in the zone between the plasma membrane and the lamina densa of the invaginations, being most conspicuous in Myxine. These consist of 60 Å wide spine-like or thread-like profiles 150 Å apart, connecting with both the outer leaflet of the plasma membrane and the lamina densa. Spatially, they form parallel circular ridges oriented transversely in stacks along the invaginations. Similar spine-like profiles are also discernible in the invaginations of rat muscle fibers. In rat, however, their spatial arrangement (ridges or fibrils) remains unknown.These specializations may serve to attach the lamina densa to the plasma membrane, and may be important for the transmission of force from muscle fibers to tendon.The author is indebted to Dr. Finn Walvig, Biological Station, University of Oslo, Drøbak, for supply of hagfishes, and to Mrs. Jorunn Line Vaaland for technical assistance.     

The human muscle-tendon junction

Summary The myotendon junction of human paravertebral skeletal muscle was studied by light and electron microscopy. Transverse and longitudinal sections of myotendinous regions of normal multifidus muscles were examined at three chronological stages from birth to maturity. Variations in the appearance of surface extensions at the terminal ends of muscle fibers consisted of brush-like evaginations at birth and villous-like projections in the adult. Regardless of age, they were invariably covered by a prominent external lamina, and mutually interdigitated with connectivetissue elements in the adjacent tendon. Various stages of myofibrillar assembly and sarcomere alignment were evident in the muscle fiber terminus at birth. With advancing age, splitting of terminal sarcomeres at Z bands commonly gave rise to diverging myofilament bundles that attached to electron-dense patches under the sarcolemma. In these regions, leptomeric organelles were also encountered in neonatal and adolescent myotendons. At all stages, the ends of muscle fibers possessed cytological features consistent with active synthesis and secretion. Densely-packed sarcoplasmic organelles including multiple Golgi complexes, clusters of ribosomes, mitochondria, cytoplasmic vesicles, and elements of rough- and smooth-surfaced endoplasmic reticulum were prevalent. Peripheral and centrally-placed heterochromatic nuclei with prominent nucleoli were arranged singly or in groups at the ends of muscle fibers. Satellite cell profiles and unmyelinated axons in the subjacent tendon were also identified at these sites in the adult. Fibroblasts in growing tendon were plentiful, and at all stages, possessed morphological features indicative of high metabolic and secretory activities.     

Sensory terminals on extrafusal muscle fibres in myotendinous regions of developing rat muscles

Summary Axon terminals were observed to form neuromuscular contacts with extrafusal muscle fibres in myotendinous regions of developing rat muscles up to 5 days after birth. These neuromuscular contacts are found in fascicles of muscle fibres connected with differentiating Golgi tendon organs. Axon terminals establishing these contacts are obviously sensory, since they do not degenerate after de-efferentation performed in neonatal rats. The terminals contain mainly clear and dense core vesicles and form neuromuscular connections resembling developing motor endplates, with a cleft about 60 nm wide and basal lamina interposed between the axolemma and the sarcolemma. Each terminal, however, also forms a close contact in a restricted region where the basal lamina is missing; there the cleft is reduced to 20 nm and the axolemmal and sarcolemmal membranes are linked by desmosome-like attachment plaques. After the fifth postnatal day, axon terminals become detached from muscle fibres and are only found among collagen bundles of the tendon organ. The functional significance of these temporary neuromuscular contacts is not clear.     

Type VI collagen in mouse masseter tendon,from osseous attachment to myotendinous junction

Background and Methods: The association of masseter tendon type VI collagen with other extracellular matrix (ECM) components was examined from osseous attachment to myotendinous junction by immunohistochemistry and transmission electron microscopy with ATP treatment and enzyme digestion. Results: In the tendon proper, fibrocytes extended their processes among bundles of striated collagen fibrils and associated with adjacent cells through amorphous materials, thus forming a three-dimensional network. The amorphous or filamentous material was observed around the fibrocyte cell body and along the cell processes, where the localization of type VI collagen was confirmed by immunohistochemistry using anti-type VI collagen antibody. After treatment with 20 mM adenosine 5′-triphosphate (ATP), 100 nm periodic fibrils, an aggregated form of type VI collagen, were formed in the place where amorphous or filamentous material was present before the treatment. In myotendinous junction, the ATP-aggregated periodic fibrils were observed to associate with the external lamina of the muscle cells as well as among junctional tendon collagen fibrils. In the tendonbone boundary, ATP-aggregated periodic fibrils were observed around fibrocartilage-like cells in the uncalcifying area but not in the calcification front. Prolonged ATP treatment or hyaluronidase predigestion caused the formation of type VI collagen periodic fibrils in the area near the calcified matrix. Conclusions: The distribution of type VI collagen in mouse masseter tendon is different in different anatomical position. This may reflect the different functional demand for this collagen. © 1995 Wiley-Liss, Inc.     

The effect of immobilization on myotendinous junction: an ultrastructural, histochemical and immunohistochemical study.

The effect of immobilization on the myotendinous junction of the calf muscles in the rat was studied histochemically, immunohistochemically and morphometrically with a transmission electron microscope. After 3 weeks of immobilization, the contact area between the muscle cells and tendineal collagen fibres was reduced by almost 50% in both type I (slow-twitch) and type II (fast-twitch) muscle fibres. The terminal finger-like processes of the muscle cells became shallow and cylindrical or were completely atrophied. Their basal membranes were slightly thickened. Histochemically, the most remarkable alteration in the myotendinous junction was the marked decrease in the sulphate containing glycosaminoglycans. In the basal lamina of the muscle fibres, the glycosaminoglycan and proteoglycan content was also reduced. Immunohistochemical analyses revealed that the amount of type III collagen was markedly increased on the myotendinous interface, but the amount and distribution of type I collagen was not affected by immobilization. These findings suggest that immobilization causes degenerative changes at the myotendinous junction, which, in turn, most likely decrease its tensile strength and may predispose it to rupture during activity.     

Assembly of transverse tubule architecture in the middle and myotendinous junctional regions in developing rat skeletal muscle fibers

The transverse (t)-tubule is responsible for the rapid inward spread of excitation from the sarcolemma to the inside of the muscle fiber, and the compartments of the t-tubule become highly and regularly organized during development. Although it is known that skeletal muscle fibers lengthen by adding sarcomeres at the myotendinous junction (MTJ) during development, no specific model exists for the assembly of new t-tubule architecture at the MTJ. We performed an electron-microscopic examination of the assembly of t-tubule architecture at the MTJ in developing rat skeletal muscle fibers. Although the longitudinally oriented t-tubule elements represent only a small fraction of the total t-tubule system in adult muscle fibers, they were observed at both A-band and I-band regions of middle and MTJ regions in early developmental stages, and gradually disappeared in the middle regions of muscle fibers during development; however, they remained in the MTJ even in adult muscle fibers. The frequency of pentads and heptads (two or three t-tubule elements with three or four elements of terminal cisternae, closely aligned with terminal cisternae of the sarcoplasmic reticulum) decreased during development, with sudden decrease between 7 and 10 weeks of age in the middle regions. Interestingly, although the frequency of decrease appeared to be higher in the middle region than in the MTJ regions in early (3- to 7-week) development, this pattern reversed, and the frequency of decrease was higher in the MTJ in later development (after 10 weeks of age). The MTJ maintained the features of immature membrane systems involved in e-c coupling much longer than the middle region of the fiber during development. The assembly of t-tubule architecture during postnatal development thus follows different processes in the middle and MTJ regions of skeletal muscle fibers.     

An electron microscope study of differentiation of the molting muscles of Rhodnius prolixus

The abdominal intersegmental molting muscles of Rhodnius prolixus undergo a repeated differentiation and dedifferentiation correlated with the molting cycle of the insect. In the dedifferentiated phase, the muscle fibers lack myofibrils but contain a few bundles of 50–60Å filaments associated with amorphous dense plaques on the sarcolemma. Differentiation of the muscle fibers begins when a starved Rhodnius nymph takes a blood meal. The first morphological signs of differentiation at ten hours after feeding are a dispersal of ribosomes from the nuclear envelopes and a formation of polysomes in the sarcoplasm. The initial myofilaments appear within 10 to 15 hours after the blood meal and are preferentially deposited in the cortices of the muscle fibers in association with the 50–60Å filament bundles and the dense plaques on the sarcolemma. Striated myofibrils are present after five days of differentiation. Developmental continuity between Z-band segments and sarcolemmal dense plaques is suggested. The formation of cross-bridges between thick and thin myofilaments appears to be the primary mechanism of myofibril organization. Disruption of microtubules with colchicine does not significantly alter myofilament deposition and organization during early stages of differentiation. Dyads, consisting of smooth sarcoplasmic reticulum and invaginations of the sarcolemma, are present in the dedifferentiated muscle fiber, and increase in number as differentiation proceeds.     

Myonecrosis Induced by Rattlesnake Venom: An Electron Microscopic Study

The myonecrotic effect of rattlesnake (Crotalus viridis viridis) venom on mouse skeletal muscle was studied. The biceps femoris muscle was examined with the electron microscope after one-fourth the LD₅₀ of the crude venom was injected into the gracilis and semimembranosus muscles. Focal areas of myonecrosis were abundant. Injured fibers contained dilated sarcoplasmic reticulum, disoriented, coagulated myofilamentous components and condensed, rounded and enlarged mitochondria. The external lamina and sarcolemma remained intact in many fibers. Hemorrhage was apparent in the endomysial connective tissue, and hemolysis was discernible. In areas where the erythrocytes were tightly packed between the muscle fibers, there was disruption of the external lamina and sarcolemma. Degeneration of the fibers in these areas was pronounced. These findings correlate well with the breakdown of muscle fibers by various methods described in the literature. Myonecrosis induced by snake venom may serve as a useful model for studying muscle necrosis because of its rapid onset and relative ease of induction.     

Chicken gizzard

Summary The fine structure and the organization of muscle and connective tissue in the middle portion of the chicken gizzard (muscular stomach) has been studied by light and electron microscopy. The musculature is divided into long, well-defined bundles arranged circularly and concentrically and extending between the two tendons (tendinous aponeurosis). The muscle bundles are inserted onto the inner sufface of the tendon at an angle of about 45°. In addition to muscle cells (which are ultrastructurally similar to those of the small intestine) the musculature contains fibroblasts and interstitial cells and a small number of nerve bundles and capillaries. The gizzard tendons are very compact, made of parallel fascicles of collagen fibrils with interposed stellate tendon cells; ultrastructurally they are very similar to the tendon of skeletal muscles of this and other species. Their collagen fibrils range in size from 30 to 160 nm. The muscle cells that approach the tendon develop longitudinal invaginations of the cell membrane and then break into finger-like terminal processes heavily encrusted with dense bands. The membrane of the invaginations and the terminal processes are surrounded by a basal lamina material which embeds a conspicuous web of small collagen fibrils. The boundary between tendon and muscle is sharp, without interpenetration of the two tissues. A novel type of cell is found at the interface of muscle and tendon (junctional cells), filled with intermediate filaments and some rough endoplsmic reticulum and displaying a trace of a basal lamina.     

Ultrastructural comparison of slack and stretched myotendinous junctions,based on a three-dimensional model of the connecting domain

Summary The vertebrate myotendinous junction contains junctional microfibrils, located in the lamina lucida of the basement membrane. The junctional microfibrils are thought to transmit muscular force across the junctional lamina lucida, also called the connecting domain. If true, deformation of the terminal muscle cell processes and connecting domain during force transmission would be detected as a change in spacing and/or orientation of the junctional microfibrils. This study compared connecting domain morphology in frog semitendinosus muscles fixed in two extremes of resting tension, to elucidate the mechanical properties of the myotendinous junction. An initial study of connecting domain ultrastructure revealed that junctional microfibrils are punctate or spinelike in shape, and that they are distributed in a linear, helically-oriented array on the muscle cell surface. The rows in the surface lattice are 10–15 nm in thickness, have a centre-to-centre distance between rows of approximately 24 nm, and are oriented at approximately 41^o with respect of the long axis of the muscle fibre. Comparison of slack and highly stretched myotendinous junctions shows no significant changes in spacing or orientation of either individual junctional microfibrils or rows in the helical surface lattice. Thus, both the connecting domain and terminal cell processes at the myotendinous junction are essentially inextensible under the loading conditions used in this study.     

The effect of immobilization on myotendinous junction: an ultrastructural,histochemical and immunohistochemical study

Kannus , P., Jozsa , L., Kvist , M., Lehto , M. & Järvinen , M. 1992. The effect of immobilization on myotendinous junction: an ultrastructural, histochemical and immunohistochemical study. Acta Physiol Scand 144 , 387–394. Received 28 April 1 991 , accepted 13 October 1991. ISSN 0001–6772. Tampere Research Station of Sports Medicine, UKK-Institute, and Department of Surgery, Tampere University Central Hospital, Tampere, Finland; Department of Morphology, National Institute of Traumatology, Budapest, Hungary; and Sports Medical Research Unit, Paavo Nurmi Center, University of Turku, Turku, Finland. The effect of immobilization on the myotendinous junction of the calf muscles in the rat was studied histochemically, immunohistochemically and morphometrically with a transmission electron microscope. After 3 weeks of immobilization, the contact area between the muscle cells and tendineal collagen fibres was reduced by almost 50% in both type I (slow-twitch) and type II (fast-twitch) muscle fibres. The terminal finger-like processes of the muscle cells became shallow and cylindrical or were completely atrophied. Their basal membranes were slightly thickened. Histochemically, the most remarkable alteration in the myotendinous junction was the marked decrease in the sulphate containing glyco-saminoglycans. In the basal lamina of the muscle fibres, the glycosaminoglycan and proteoglycan content was also reduced. Immunohistochemical analyses revealed that the amount of type III collagen was markedly increased on the myotendinous interface, but the amount and distribution of type I collagen was not affected by immobilization. These findings suggest that immobilization causes degenerative changes at the myotendinous junction, which, in turn, most likely decrease its tensile strength and may predispose it to rupture during activity.     

Some observations on the fine structure of the epidermal-dermal junction in the skin of the frog tadpole,Rana rugosa

Special lamellated bodies, 400 to 700 Å in diameter, are observed in the adepidermal space at the epidermal-dermal junction of the skin of the frog tadpole, Rana rugosa. Each stained lamella is about 20 Å thick and separated from adjacent lamellae by spacings of 20 to 30 Å. The lamellated bodies are demonstrated in specimens prepared with phosphotungstic acid (PTA)-containing fixatives, but are not revealed in specimens fixed with ordinary aldehyde fixatives which lack PTA. They are sometimes observed within the cytoplasm of basal epidermal cells, suggesting their epidermal origin. Far less frequently, comparable structures are present outside the sarcolemma of skeletal muscle fibers. Three kinds of anchoring structures are observed at the epidermal-dermal junction: anchoring filaments, anchoring fibrils, and anchoring fibers. The anchoring filaments are observed in the adepidermal space connecting hemidesmosomes to the basal lamina. They are 200 to 230 Å in diameter and have no banding pattern. Anchoring fibrils, 210 to 250 Å thick and unbanded, are present in the upper one-third of the collagenous lamellae. Fibrils do not have a banding pattern. Direct continuity between anchoring fibrils and anchoring filaments is suggested. Anchoring fibers, about 170 mμ, thick, occur less frequently. They are composed of laterally aggregated finer fibrils which show no clear bandings. Their distal ends join with the basal lamina and they extend proximally deep into the collagenous lamellae.     

The occurrence, structure and innervation of slow and twitch muscle fibres in the tensor tympani and stapedius of the cat

1. The muscle fibres of the tensor tympani and stapedius of the cat have been examined in the light microscope in teased preparations after cholinesterase staining and in the electron microscope.2. In both muscles, two kinds of fibre have been found: those with an individual end-plate and those with multiple nerve terminals.3. The stapedius fibres with an end-plate have fibrils regularly separated from each other by sarcoplasmic reticulum, a straight Z line, transverse tubular T system elements regularly occurring at the junction of A and I bands, an M line, an extensive sole plate area, and numerous post-junctional sarcolemmal infoldings under the nerve terminal. This type of muscle fibre in the tensor tympani has all of these features except that the fibrils are not well separated from each other, T system elements are absent in some sarcomeres, and a typical M line is absent.4. Compared to the individually innervated fibres, the fibres with multiple endings have fibrils poorly separated from each other by sarcoplasmic reticulum, a jagged Z line, very few T system elements, a less extensive sole plate area, and essentially no folds under the nerve terminal. These fibres in both muscles have M lines.5. Muscle fibres have thus been found in both the tensor tympani and stapedius of the cat which conform in their innervation, the structure of their motor nerve endings, and their internal structure to many of the morphological characteristics which are exhibited by slow muscle fibres elsewhere.     

Tendon and myo-tendinous junction in an overloaded skeletal muscle of the rat

Summary Overloading of rat plantaris muscles was produced by aseptic ablation of the synergists. The morphological changes occurring after 1 or 2 weeks were investigated at the light and electron microscopical level in the distal tendon of the plantaris and at the myotendinous junction. Sham-operated rats were prepared as controls. In the tendon, quiescent fibrocytes were replaced by activated fibroblasts displaying a vesicular nucleus with prominent nucleoli and an outstanding increase in cytomembranes, particularly the rough endoplasmic reticulum and the Golgi complex. The plasmalemma of the fibroblasts was modified by the presence of caveolae and the surbsurface cytoplasm contained many membrane-bound vacuoles. In the tendon, the collagen bundles were disrupted, resulting in the formation of empty longitudinally oriented spaces; in these spaces, as in the pericapillary areas, no inflammatory cells were observed. At the myotendinous junction, fibroblast activation was consistently observed in both control and overloaded specimens. At this level, the sarcolemma of the finger-like projections of muscle fibres presented many caveolae close to clusters of large subsurface vacuoles. These observations indicate that, at the beginning of the compensatory hypertrophy, the adaptative changes to overloading include a non-inflammatory reaction of the tendon characterized by enhanced collagen synthesis and intensive membrane renewal and recycling. From the mechanical point of view this reaction can impair the tendon resistance to stretch. At the myotendinous junction the increased membrane turnover of the sarcolemma and the fibroblast activation can be considered permanent phenomena consequent to the increased stress exerted upon the interface connecting the contractile apparatus to the stroma.     

Intramembrane aspects of myotendinous and myomuscular junctions: a freeze-fracture study of the gill sac-muscle of the Atlantic hagfish, Myxine glutinosa

The intramembrane organization of the sarcolemma at the sites of myotendinous and myomuscular junctions was studied in the gill sac-muscle of the Atlantic hagfish, Myxine glutinosa, by using freeze-fracture replicas. At these sites rows of irregularly shaped particles (diameter approximately 6 nm) and short fibrils are present on the P face and a complementary pattern of grooves is present on the E face of the split plasma membrane. The center-to-center distance between adjacent rows of particles and grooves ranges from 12 to 20 nm. Rodlike projections being in register with the rows of particles and grooves, respectively, extend from the plasma membrane toward the extracellular space. These rodlike projections are also recognizable in thin sections, where they appear as spinelike projections (cross sections) or linear arrays (grazing sections) located in the lamina lucida of the basal lamina. The intramembrane particles are considered to be integral membrane proteins and to represent transmembrane links in a series of molecules by which intracellular actin filaments and extracellular collagen fibrils are connected across the plasma membrane. The rodlike projections are probably peripheral membrane proteins possibly connecting the plasma membrane with structural components of the basal lamina.     

Ultrastructural distinction between reticular and collagenous fibers with an ammoniacal silver stain

Reticular and collagenous fibers stain differently when subjected to ammoniacal silver reduction. A variety of tissues were subjected to such a “reticulin” technique and the association of reaction product with intercellular connective tissue elements was studied with the electron microscope. The reaction with reticular fibers was primarily associated with the interfibrillar matrix, and was globular in form having a wide variety of particle sizes. Conversely, in dermal collagen the unit fibrils were stained rather than the interfibrillar matrix. The precipitate was punctate in form and was associated with the cross striations of unit collagen fibrils. Large microfibrils also reacted positively with the stain, imparting a faint periodicity. Basement membranes were stained uniquely. The underlying plasmalemma and the lamina densa were heavily stained with silver while the lamina lucida was relatively unstained. The unit fibrils of the lamina reticularis stained in the same manner as dermal unit collagen while the ground substance remained unstained. This represents a clear distinction between the argentophilic characteristics of collagenous fibers, reticular fibers, and basement membranes.     

Divalent cation-dependent adhesion at the myotendinous junction: ultrastructure and mechanics of failure

Summary Junctional microfibrils, which span the lamina lucida of the vertebrate myotendinous junction, are thought to function in force transmission at the junction. This hypothesis has been tested by disrupting junctional microfibrils through elimination of extracellular divalent cations, and determining the effects of this treatment on the ultrastructure and mechanics of whole frog skeletal muscles passively stretched to failure. Muscles incubated in divalent cation-free solution failed exclusively in the lamina lucida of the myotendinous junction, while control muscles all failed within the muscle fibres, several millimetres away from the junction. Failure sites from divalent cation-free muscles incubated with antibodies against collagen type IV, laminin, and tenascin showed no labelling of the avulsed ends of the muscle fibres, indicating that remnants of junctional microfibrils observed on the cell surface are not composed of any of these extracellular proteins. All three proteins were present on the tendon side of the failure site, confirming that the lamina densa remains attached to the tendon. Breaking stress for control muscles was 3.47×10⁵ N m^-2, and for divalent cation-free muscles, 1.84×10⁵ N m^-2, or approximately half the control value. Breaking strain averaged 1.17 for divalent cation-free muscles and 1.39 for controls, although the difference was not significant. We conclude that junctional microfibrils are components of a divalent cation-dependent adhesion mechanism at the myotendinous junction. In addition, ultrastructural analysis of divalent cation-free fibres stretched just short of failure suggests that a second, divalent cation-independent mechanism persists along the non-junctional cell surface, and can transmit substantial passive tension from myofibrils laterally to the extracellular matrix, bypassing the failed myotendinous junction.     

Morphological analysis of the acute effects of overdistension on the extracellular matrix of the rat urinary bladder wall.

PURPOSE: To investigate the morphological effects of acute overdistension in the structure of the extracellular matrix of the bladder wall in rats. MATERIALS AND METHODS: The bladders of a group of 6 male Wistar rats were transurethrally overdistended for 3 hours. Another identical group (the control group) was only submitted to a sham operation. Specimens from the bladder dome were analyzed with light microscopy (LM), transmission electron microscopy (TEM) and scanning electron microscopy (SEM). RESULTS: LM--The control group bladders had a 4 to 5 layer urothelium, a lamina propria, and a smooth muscle layer with longitudinal and transversal fibers. The overdistended bladders presented an intense interstitial infiltrate in the lamina propria, and a less intense infiltrate among the smooth muscle fibers. TEM--The cells of the overdistended bladders had a significant amount of vacuoles, unlike the control bladders, where such vacuoles were scarce or absent. SEM--A delicate three-dimensional mesh of collagen fibrils was observed in the lamina propria of the bladder walls from the control group. Whilst for the control group this mesh consisted of distinct geometric structures, with mostly circular cellular spaces surrounded by the fibrils, the overdistended group showed evidence of distortion of the mesh, with flattened and elongated cellular spaces. CONCLUSIONS: Acute bladder overdistension induces structural modifications, altering the arrangement and interaction of collagen fibrils, as well as incipient tissue damage as edema in the lamina propria and smooth muscle layers.