The components of the cartilagenous intercellular matrix - proteoglycans, hyaluronic acid, collagen and structural glycoproteins - are degraded during inflammation and following trauma by enzymes of varied origin (Table 1) . The loss of the matrix as long as it is not completely compensated for by a new synthesis, leads to advanced degeneration of the cartilage.
Even today it is not certain to what extent cartilage specific enzymes (that is, the enzymes produced by the chondrocytes) are responsible for the degradation of the intercellular matrix.
There exist numerous biochemical indications that proteases (for example, cathepsin D. elastase) as well as glucuronidase are present in articular cartilage. It is assumed that these enzymes are intracellularly produced by the rough endoplasmatic reticulum (er) and then stored in an inactive form in the lysosomes of the cells. It is a matter for speculation as to how these enzymes reach the intercellular space and in which form they are present.
According to Thyberg and Friberg (1970, 1972), the enzymes are presumably present in the matrix even under physiological conditions, partially in vesicles, which are similar to primary lysosomes. The authors could show, by electron microscopy that acidic phosphatase, the key lysosomal enzyme, is present in the“matrix dense bodies”originate through an in toto excretion from the chondrocytes.
In order to study the meaning of cartilage specific enzymes after blunt trauma of the articular cartilage, we produced cartilage contusions in animal experiments and investigated electron microscopically the time dependent activity of the lysosomal enzymes in the matrix.
Since a morphological representation of the specific enzymes which degrade the matrix (above all, the proteases) is not directly feasible because these enzymes or their respective reaction products could not be coupled on an electron dense substance, we therefore used the acid phosphatase as the lysosomal key enzyme and the arylsulfatase for the electron microscopic investigations.
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