RESUMO
Background: The injury repair process in tendons and ligaments includes different phases such as inflammation, neovascularization, fibroblast proliferation and fibrosis. Collagen type and tissue characteristics of tendon and ligament repair are described such as type collagen differentiation and properties of the scars tissue. The degeneration of articular cartilage when, characterized by loss of the articular layers associated of the decreased of proteoglycans. The aim of this study is to describe by histochemistry techniques the characteristics of tissue scar, collagen type in the repair process of tendons and ligaments, as well as articular cartilage degeneration.Materials, Methods & Results: Tissue samples of equine tendons, ligaments and articular cartilage of the metacarpophalangeal joint region were evaluated by ultrasonography, macroscopically and prepared for routine histopathology (H&E staining). The inclusion criterion of the samples in this study was based on the presence of lesions characterized in H&E stain as fibroplasia, neovascularization, collagenolysis, chondroid metaplasia in tendons and ligaments and fibrillation and cartilaginous eburnation lesions in the articular cartilage samples. The Massons trichrome, Picrosirius red and Alcian blue staining techniques were also performed in addition to H&E. Pathologic findings in the tendons and ligaments included fibroplasia, collagenolysis, chondroid metaplasia and lymphohistioplasmacytic inflammation. Tendons and ligaments scars were composed of type III collagen but there was also some type I collagen. Fiber alignment of tendons and ligaments in the reorganization tissue was not flawless and the fiber appearance was characterized by a lack of the fiber crimp and parallelism. The fibroplasia was characterized by endotendinous tickening areas associated with the presence of loose connective tissue.[...](AU)
Assuntos
Animais , Cavalos , Tendões/anatomia & histologia , Tendões/química , Ligamentos/anatomia & histologia , Ligamentos/química , Cartilagem Articular/anatomia & histologia , Cartilagem Articular/química , Técnicas Histológicas/métodosRESUMO
Background: The injury repair process in tendons and ligaments includes different phases such as inflammation, neovascularization, fibroblast proliferation and fibrosis. Collagen type and tissue characteristics of tendon and ligament repair are described such as type collagen differentiation and properties of the scars tissue. The degeneration of articular cartilage when, characterized by loss of the articular layers associated of the decreased of proteoglycans. The aim of this study is to describe by histochemistry techniques the characteristics of tissue scar, collagen type in the repair process of tendons and ligaments, as well as articular cartilage degeneration.Materials, Methods & Results: Tissue samples of equine tendons, ligaments and articular cartilage of the metacarpophalangeal joint region were evaluated by ultrasonography, macroscopically and prepared for routine histopathology (H&E staining). The inclusion criterion of the samples in this study was based on the presence of lesions characterized in H&E stain as fibroplasia, neovascularization, collagenolysis, chondroid metaplasia in tendons and ligaments and fibrillation and cartilaginous eburnation lesions in the articular cartilage samples. The Massons trichrome, Picrosirius red and Alcian blue staining techniques were also performed in addition to H&E. Pathologic findings in the tendons and ligaments included fibroplasia, collagenolysis, chondroid metaplasia and lymphohistioplasmacytic inflammation. Tendons and ligaments scars were composed of type III collagen but there was also some type I collagen. Fiber alignment of tendons and ligaments in the reorganization tissue was not flawless and the fiber appearance was characterized by a lack of the fiber crimp and parallelism. The fibroplasia was characterized by endotendinous tickening areas associated with the presence of loose connective tissue.[...]
Assuntos
Animais , Cartilagem Articular/anatomia & histologia , Cartilagem Articular/química , Cavalos , Ligamentos/anatomia & histologia , Ligamentos/química , Tendões/anatomia & histologia , Tendões/química , Técnicas Histológicas/métodosRESUMO
The region in tendons that surrounds bone extremities adapts to compression forces, developing a fibrocartilaginous structure. During maturation, changes occur in the amount and organization of macromolecules of the extracellular matrix of tendons, changing the tissue morphology. To study the effect of maturation on tendons, Pedrês chickens were sacrificed at 1, 5, and 8 months old and had the calcaneal tendon (CT) divided into proximal region, submitted to tension/compression forces (p), and distal region submitted to tension force (d). Morphological analysis of the p region showed the presence of fibrocartilage in all ages. In the central part of the fibrocartilage, near a diminishment of the metachromasy, there was also a development of a probable fat pad that increased with the maturation. The activity of MMP-2 and MMP-9 was higher at 5 and 8 months old, in both regions, compared with 1-month-old animals. In SDS-PAGE analysis, components with electrophoretic migration similar to decorin and fibromodulin increased with maturation, particularly in the d region. The Western blotting confirmed the increased amount of fibromodulin with maturation. In conclusion, our results show that process of maturation leads to the appearance of a probable fat pad in the center of the fibrocartilage of CT, with a reduced amount of glycosaminoglycans and an increased activity of MMPs.
Assuntos
Galinhas/crescimento & desenvolvimento , Matriz Extracelular/química , Tendões/química , Tendões/crescimento & desenvolvimento , Animais , Western Blotting , Eletroforese em Gel de Poliacrilamida , Histocitoquímica , MicroscopiaRESUMO
The plantaris longus tendon (PLT) in bullfrog develops a fibrocartilage-like tissue in the area that is functionally subject to compressive forces. The aim of this study was to analyze the modifications of the pressure-bearing region in bullfrog PLT with different ages (7, 180, and 1,080 days after the end of metamorphosis) using histomorphometric, ultrastructural and biochemical methods. Weak basophilia and cells with a fibroblastic phenotype were observed in the compression region at 7 days of age. On the other hand, a large area of intense tissue basophilia associated with a chondroblast-like cell population was noted at the other ages. Collagen fibers exhibited a three-dimensional network-like arrangement at all ages. The number of connective tissue cells increased between 7 and 180 days of age and was reduced in older animals. The 180-day-old animals presented a well-developed pericellular matrix rich in proteoglycans. The mean diameter of collagen fibrils increased from 7 to 180 days and was the same at 1,080 days. Glycosaminoglycan content was higher in 7-day-old animals. A higher amount of hydroxyproline was observed at 180 and 1,080 days. The swelling test showed a significant increase of wet weight in 7-day-old animals. In conclusion, the alterations that occur in the pressure-bearing of bullfrog PLT are the result of physiological alterations of the animal with the maturation and aging.
Assuntos
Envelhecimento/fisiologia , Rana catesbeiana/fisiologia , Tendões/ultraestrutura , Animais , Glicosaminoglicanos/análise , Hidroxiprolina/análise , Microscopia , Microscopia Eletrônica de Transmissão , Rana catesbeiana/anatomia & histologia , Tendões/química , Tendões/fisiologia , Suporte de Carga/fisiologiaRESUMO
Tendons are formed by dense connective tissue composed of an abundant extracellular matrix (ECM) that is constituted mainly of collagen molecules, which are organized into fibrils, fibers, fiber bundles and fascicles helicoidally arranged along the largest axis of the tendon. The biomechanical properties of tendons are directly related to the organization of the collagen molecules that aggregate to become a super-twisted cord. In addition to collagen, the ECM of tendons is composed of non-fibrillar components, such as proteoglycans and non-collagenous glycoproteins. The capacity of tendons to resist mechanical stress is directly related to the structural organization of the ECM. Collagen is a biopolymer and presents optical anisotropies, such as birefringence and linear dichroism, that are important optical properties in the characterization of the supramolecular organization of the fibers. The objective of this study was to present a review of the composition and organization of the ECM of tendons and to highlight the importance of the anisotropic optical properties in the study of alterations in the ECM.
Assuntos
Matriz Extracelular/química , Matriz Extracelular/ultraestrutura , Tendões/química , Tendões/ultraestrutura , Animais , Anisotropia , Humanos , Fenômenos MecânicosRESUMO
I review here form, or textural, birefringence (Δ(F)) in the context of advances in the field, as well as with regard to findings and applications in the physics of photonic devices, fibers maintaining polarization, photonic crystal fibers, and in biopolymers present in extracellular matrices and the myelin sheath. Some advantages of applying knowledge of Δ(F) to biological fields involving biopolymers, especially collagen fibers, are considered in more detail. Tendon and cartilage collagen fibers have been regarded as a model of dense, highly aggregated biopolymers with preferential orientations. Owing to their supramolecular organization, such materials may be used to study molecular order by using anisotropic optical properties, especially Δ(F). Differences between collagen type I- and collagen type II-rich structures, and similarities between collagen crimp and second harmonic generation images are reported. Based on data reported here, it is possible to deduce that collagen type I supramolecular organization has nonlinear optical properties and that tendon segments can conduct red laser light. With respect to nerve fibers, the detection and measurements of Δ(F) have allowed the myelin sheath to be considered a smectic liquid crystal.
Assuntos
Birrefringência , Animais , Anisotropia , Cartilagem Articular/química , Bovinos , Galinhas , Colágeno Tipo I/química , Colágeno Tipo II/química , Matriz Extracelular/química , Microscopia de Polarização , Bainha de Mielina/química , Ratos , Cauda/química , Tendões/químicaRESUMO
Obesity is currently considered to be a world epidemic and one of the major public health problems in many countries, whose incidence is increasing at alarming rates. Genetically obese Zucker rats are used as a model of obesity and were employed in the present study. Tendons transmit contractile force from muscles to bone, thus permitting articular movement. The objective of our study was to analyze the ultrastructural, biochemical, and biomechanical alterations that occur in the deep digital flexor tendon of obese Zucker rats compared to lean animals. Ultrastructural analysis showed differences in collagen fibril diameter distribution and mass-average diameter between obese and lean animals. Regarding mechanical parameters, there was a significant difference in maximum displacement and strain. Hydroxyproline content was higher in obese animals. In view of the excess weight and peculiar conditions to which the tendon of obese animals is submitted, we concluded that obesity provokes alterations in the composition and organization of tendon extracellular matrix components. These alterations might be related to organizational and structural modifications in the collagen bundles, influencing the mechanical properties of the tendon and the progression to a pathological state.
Assuntos
Colágeno/ultraestrutura , Obesidade/patologia , Ratos Zucker/fisiologia , Tendões/ultraestrutura , Animais , Colágeno/fisiologia , Matriz Extracelular/química , Matriz Extracelular/metabolismo , Membro Anterior , Hidroxiprolina/análise , Hidroxiprolina/metabolismo , Técnicas Imunoenzimáticas , Masculino , Obesidade/genética , Ratos , Estresse Mecânico , Tendões/química , Tendões/metabolismo , Resistência à TraçãoRESUMO
The role of physical activity in affecting the composition of extracellular matrix and mechanical properties of tendons has been well studied, but little is known about the role of passive stretching. The purpose of this study was to test the hypothesis that stimulation by passive stretching may change the composition and mechanical properties of tendons. Three-month-old Wistar rats were divided into three groups: the control, animals were not submitted to stretching procedures; groups that had their calcaneal tendons manually stretched three or five times a week, for 21 days. Afterward, the calcaneal tendons were removed and assayed for hydroxyproline content and biomechanical test. The hydroxyproline content in the stretched groups was higher, suggesting that more collagen was present in the tendons of these groups. These tendons also showed higher values of maximum stress and modulus of elasticity or Young's modulus. These results indicate that stretching leads to alterations in the synthesis of the extracellular matrix components and in the mechanical properties of tendons.
Assuntos
Calcâneo/química , Calcâneo/fisiologia , Colágeno/metabolismo , Matriz Extracelular/metabolismo , Tendões/química , Tendões/fisiologia , Resistência à Tração/fisiologia , Adaptação Fisiológica/fisiologia , Animais , Fenômenos Biomecânicos , Calcâneo/anatomia & histologia , Elasticidade/fisiologia , Fibroblastos/metabolismo , Hidroxiprolina/análise , Hidroxiprolina/metabolismo , Locomoção/fisiologia , Masculino , Movimento/fisiologia , Contração Muscular/fisiologia , Ratos , Estresse Mecânico , Tendões/anatomia & histologia , Regulação para Cima/fisiologiaRESUMO
Biochemical and morphological aspects of fibrocartilages of calcaneal and deep digital flexor tendons in rats aged 30, 180 and 730 days were analyzed. In both tendons a stronger staining with Alcian blue, indicating the presence of proteoglycans, was detected in rats of 30 and 180 days. In animals 730 days old, it was restricted to the pericellular area. Ultrastructural analysis showed a more prominent pericellular matrix in calcaneal tendon compared to the deep digital flexor tendon. The biochemical analysis showed higher levels of proteins and glycosaminoglycans in the calcaneal tendon of 30-day-old rats compared to older rats. In the deep digital flexor tendon, no significant differences were observed between ages. The small proteoglycan, fibromodulin, was detected in both tendons of all ages, but in young rats it appeared to be running as a 210 kDa component, probably due to the association with collagen chains or self-association.
Assuntos
Envelhecimento/fisiologia , Fibrocartilagem/química , Fibrocartilagem/citologia , Tendões/química , Tendões/citologia , Animais , Calcâneo/citologia , Calcâneo/ultraestrutura , Eletroforese em Gel de Poliacrilamida , Fibrocartilagem/ultraestrutura , Glicosaminoglicanos/análise , Masculino , Proteínas/análise , Ratos , Ratos Wistar , Ácidos Urônicos/análiseRESUMO
Tendon composition changes according to differentiation, mechanical load, and aging. In this study, we attempted to identify, localize, and quantify type VI collagen in bovine tendons. Type VI collagen was identified by the electrophoretic behavior of the alpha chains and Western blotting, and by rotary shadowing. Type VI collagen was extracted from powdered tendon with three sequential 24-h extractions with 4 M guanidine-HCl. The amount of type VI collagen was determined by enzyme-linked immunosorbent assay for purely tensional areas and for the compressive fibrocartilage regions of the deep flexor tendon of the digits, for the corresponding fetal and calf tendons, and for the extensor digital tendon. The distal fibrocartilaginous region of the adult tendon was richer in type VI collagen than the tensional area, reaching as much as 3.3 mg/g (0.33%) of the wet weight. Calf tendons showed an accumulation of type VI at the fibrocartilage site. Immunocytochemistry demonstrated that type VI collagen was evenly distributed in the tensional areas of tendons but was highly concentrated around the fibrochondrocytes in the fibrocartilages. The results demonstrate that tendons are variable with regard to the presence and distribution of type VI collagen. The early accumulation of type VI collagen in the region of calf tendon that will become fibrocartilage in the adult suggests that it is a good marker of fibrocartilage differentiation. Furthermore, the distribution of type VI collagen in tendon fibrocartilage indicates that it organizes the pericellular environment and may represent a survival factor for these cells.