keratan-sulfate and Cadaver

Ideally, cartilage regenerative cell therapy should produce a tissue which closely matches the microstructure of native cartilage. Benchmark reference information is necessary to assess the quality of engineered cartilage. Our goal was to examine the variation in glycosaminoglycans (GAGs) in cartilage zones within human knee joints of different ages.. Osteochondral biopsies were removed from the medial femoral condyles of deceased persons aged 20-50 years. Fluorophore-Assisted Carbohydrate Electrophoresis (FACE) was used to profile GAGs through the superficial, middle and deep zones of the articular cartilage. Differences were identified by statistical analysis.. Cartilage from the younger biopsies had 4-fold more hyaluronan in the middle zone than cartilage from the older biopsies. The proportion of hyaluronan decreased with increasing age. Cartilage from the middle and deep zones of younger biopsies had significantly more chondroitin sulphate and keratan sulphate than the cartilage from older biopsies. This would suggest that chondrocytes synthesise more sulphated GAGs when deeper in the tissue and therefore in conditions of hypoxia. With increasing age, there was significantly more chondroitin-6 sulphate than chondroitin-4 sulphate. For the first time, unsulphated chondroitin was detected in the superficial zone.. As an outcome measure, FACE offers the potential of a complete, detailed assessment of all GAGs and offers more information that the widely used 1,9-dimethylmethylene blue (DMMB) dye assay. FACE could be very useful in the evolving cartilage regeneration field.

Topics: Adult; Age Factors; Cadaver; Cartilage, Articular; Cell- and Tissue-Based Therapy; Chondroitin; Chondroitin Sulfates; Electrophoresis; Glycosaminoglycans; Guided Tissue Regeneration; Humans; Hyaluronic Acid; Keratan Sulfate; Knee Joint; Middle Aged; Outcome Assessment, Health Care; Reference Values; Tissue Engineering; Young Adult

The most common site of rupture of the posterior tibial tendon is the retromalleolar region where the tendon changes its direction of pull. The aim of this study was to characterize the tissue of the gliding zone of the tibialis posterior tendon to gain further knowledge about possible structural causes for spontaneous tendon rupture.. Light microscopy, transmission electron microscopy and immunohistochemical methods were used to describe the structure of the human tibialis posterior tendon.. In the region where the tendon wraps around the medial malleolus, the structure of the tissue changes from the typical structure of a traction tendon. The superficial zone which was directed towards the pulley tissue had the structure of fibrocartilage with a specific three-dimensional collagen fibril texture. Transmission electron microscopy showed chondrocytes with a felt-like pericellular matrix that increased in size towards the gliding surface. The extracellular matrix of the fibrocartilage was rich in acid glycosaminoglycans and stained intensively with alcian blue at pH 1. Immunohistochemical staining of cartilage-specific extracellular matrix components such as type II collagen, chondroitin-4-sulphate, chondroitin-6-sulphate, keratan sulphate and aggrecan was positive.. The location of the fibrocartilage corresponds to the region where the tibialis posterior tendon wraps around the medial malleolus, which serves as a pulley. According to the theory of 'causal histogenesis', the stimulus for the development of fibrocartilage within dense connective tissue is intermittent compressive and shear stress. The fibrocartilaginous region is the region where most spontaneous ruptures of the tibialis posterior tendon occur. Due to its structure, the fibrocartilaginous region may be more vulnerable to repetitive tensile microtrauma; degeneration may occur due to the poor repair response of the avascular fibrocartilaginous tissue.

Topics: Adult; Aged; Aggrecans; Ankle Joint; Cadaver; Cartilage, Articular; Chondrocytes; Chondroitin Sulfate Proteoglycans; Chondroitin Sulfates; Extracellular Matrix; Extracellular Matrix Proteins; Female; Fibrillar Collagens; Glycosaminoglycans; Humans; Immunohistochemistry; Keratan Sulfate; Lectins, C-Type; Male; Microscopy; Middle Aged; Proteoglycans; Tendons

The human intervertebral discs which were obtained by cadavers and anterior discectomy are investigated histochemically. Chondroitin-4S, chondroitin-6S, dermatan sulfate, hyaluronic acid and keratan sulfate were detected in the human intervertebral disc by various histochemical methods. pH2.5, pH1.1 toluidin blue metachromasia and 0.4M MgCl2 alcianophilia became weaker with increasing age, and the herniated disc were weaker than controlled discs in the same age group. Chondroitin-4S and chondroitin-6S were distributed throughout the discs. There was no clear localization of the various glycosaminoglycans in the human intervertebral disc, with the exception of keratan sulfate. There was no histologically and histochemically observable difference in the cervical and lumbar discs.

Topics: Adult; Cadaver; Cartilage; Chondroitin Sulfates; Dermatan Sulfate; Histocytochemistry; Humans; Hyaluronic Acid; Intervertebral Disc; Intervertebral Disc Displacement; Keratan Sulfate