The metabolic fate of intravenously injected peptide-bound chondroitin sulphate in the rat.
نویسندگان
چکیده
The degradation of intravenously administered chondroitin sulphate-peptide, obtained by trypsin digestion of rat cartilage preparations labelled in vitro with 35S (and, in some cases, with 3H), was studied in rats. As with free chains of chondroitin sulphate, the major site of accumulation and degradation in the body was the liver, although peptide-linked chains were taken up more rapidly than free chains. In the first 2h after intravenous injection of a chondroitin sulphate-peptide fraction, labelled macromolecular components were excreted in the urine. These were shown to be chondroitin sulphate-peptide of the same degree of sulphation but of smaller average size than the injected material. A similar observation was made when free chains of chondroitin sulphate from the same source were administered intravenously. An isolated perfused rat kidney failed to de-sulphate circulating chondroitin sulphate-peptide, but a component of lower average molecular weight was excreted in the urine. When a chondroitin sulphate-peptide fraction of relatively larger hydrodynamic volume was administered, very little chondroitin sulphate appeared in the urine in the first 2h. It was concluded that, depending on size and/or peptide content, the chondroitin sulphate-peptide released from connective tissues into the circulation would probably be subjected to one of two alternative fates. The smaller fragments are more likely to be excreted in the urine, whereas the larger ones are taken up by the liver and there degraded to inorganic sulphate and undefined carbohydrate components.
منابع مشابه
The metabolic fate of chondroitin (35S)sulphate proteoglycan in the rat.
Revell & Muir (1972) have studied the metabolism of 35S-labelled proteoglycan from porcine cartilage after injection into guinea pigs. They concluded that the polymeric material excreted in the urine was the result of proteolytic degradation of the injected proteoglycan to single chains of chondroitin sulphate. These results are particularly interesting with respect to the site(s) and mechanism...
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ورودعنوان ژورنال:
- The Biochemical journal
دوره 158 1 شماره
صفحات -
تاریخ انتشار 1976