| Autor: |
Robinovitch MR; Department of Oral Biology, School of Dentistry, University of Washington, Seattle 98195., Iversen JM, Izutsu KT |
| Jazyk: |
angličtina |
| Zdroj: |
Archives of oral biology [Arch Oral Biol] 1992 Mar; Vol. 37 (3), pp. 209-14. |
| DOI: |
10.1016/0003-9969(92)90090-u |
| Abstrakt: |
The chondroitin sulphate contained within the secretory granules of the rat parotid gland and its saliva was shown to be in the form of a proteoglycan by using inhibitors of proteoglycan synthesis in a gland slice system. Gland slices were incubated in either p-nitrophenyl-beta-D-xyloside or chlorate in the presence of both [3H]-leucine and [35S]-sulphate. The slices were next homogenized and either the 250 g supernatant fraction (for initial experiments) or secretory granule-containing fractions were isolated. Protein and proteoglycans of these fractions were precipitated in 10% trichloracetic acid (TCA), and glycosaminoglycans in cetylpyridinium chloride. [3H]-leucine and [35S]-sulphate were quantitated in each type of precipitate by scintillation counting. The results showed that 1 mM xyloside had no effect on protein or glycosaminoglycan synthesis but blocked incorporation of radiosulphate into TCA-precipitable material. Sixteen mM chlorate almost totally inhibited incorporation of radiosulphate into glycosaminoglycan and TCA-precipitable material. These findings demonstrate that the rat parotid secretory chondroitin sulphate is indeed a proteoglycan because its synthesis is blocked by the protein-core analogue acceptor, p-nitrophenyl-beta-D-xyloside. This system offers opportunities for exploring the functional role of chondroitin sulphate proteoglycan in this salivary gland. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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