Download Molecular Parameters Indicating Adaptation to Mechanical by Stefan Milz, Michael Benjamin, Reinhard Putz PDF

By Stefan Milz, Michael Benjamin, Reinhard Putz

The connective and supportive tissues represent a large amount of the biomass in human and animal organisms. the purpose of this publication is to give a contribution to the certainty of the mutual courting among the mechanical state of affairs of tendons and ligaments and their internal constitution.

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Read or Download Molecular Parameters Indicating Adaptation to Mechanical Stress in Fibrous Connective Tissue (Advances in Anatomy, Embryology and Cell Biology) PDF

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Additional info for Molecular Parameters Indicating Adaptation to Mechanical Stress in Fibrous Connective Tissue (Advances in Anatomy, Embryology and Cell Biology)

Sample text

Labeling for versican and tenascin is present in all parts of the tendon and in all of the trochleae. In certain cases, where cells with distinctly cartilaginous morphology are present in the center of the trochlea, labeling for versican and keratan sulfate is absent in both the territorial and the interterritorial matrices. Aggrecan and link protein can also be detected in all parts of the tendon and in the trochlea (Fig. 15) Labeling is distributed homogeneously throughout the tendon’s ECM. However, labeling in the trochlea is predominantly pericellular and tends to be more pronounced toward the central region.

From Milz et al. 1998, with permission of Wiley-Liss) The Transverse Ligament of the Atlas 31 Labeling for aggrecan is detectable in the sesamoid fibrocartilages of all extensor tendons (Fig. 9) and sometimes extends into the adjacent proximal and distal portions of the tendon. In a few cases, positive labeling for aggrecan occurred in regions of the tendons that do not label for chondroitin 6 sulfate (in neighboring sections). The intensity of labeling differs considerably between tendons: the strongest and most extensive labeling is seen in the extensor tendon of an index finger, the weakest in that of a thumb.

Bray et al. (1993) are of the opinion that type VI collagen serves as an anchoring structure between chondroitin sulfate/hyaluronic acid complexes, on the one hand, and type I collagen fibrils, on the other. This arrangement would surround the collagen fibrils with a strongly hydrated layer that would make easier the transportation of fluids between the fibrils. According to Burgeson and Nimni (1992), type VI collagen favorably influences the attachment of fibroblasts to the collagenous network. The distribution of labeling for type VI collagen observed here could well be correlated with such a model.

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