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dc.contributor.authorSteward, William P
dc.contributor.authorChristmas, Stephen E
dc.contributor.authorLyon, Malcolm
dc.contributor.authorGallagher, John T
dc.date.accessioned2010-08-17T13:39:23Z
dc.date.available2010-08-17T13:39:23Z
dc.date.issued1990-05-22
dc.identifier.citationThe synthesis of proteoglycans by human T lymphocytes. 1990, 1052 (3):416-25 Biochim. Biophys. Actaen
dc.identifier.issn0006-3002
dc.identifier.pmid2354207
dc.identifier.doi10.1016/0167-4889(90)90151-3
dc.identifier.urihttp://hdl.handle.net/10541/109769
dc.description.abstractWe have examined the proteoglycans produced by highly-purified cultures of human T-lymphocytes. The proteoglycans were metabolically labelled with [35S]sulphate and analysed in cellular and medium fractions using DEAE-cellulose chromatography, gel filtration and specific enzymatic and chemical degradations. The results showed that the T cells synthesized a relatively homogeneous, proteinase-resistant chondroitin 4-sulphate proteoglycan that accumulated in the culture medium during a 48 h incubation period. The cellular fraction contained a significant amount of free chondroitin sulphate chains that were not secreted into the medium. These polysaccharides were formed by intracellular degradation of proteoglycan in a chloroquine-sensitive process, indicating a requirement for an acidic environment. In contrast to chondroitin sulphate derived from proteoglycan, chondroitin sulphates synthesized on the exogenous primer, beta-D-xyloside, were mainly secreted by the cells. beta-D-Xylosides caused an 8-fold stimulation in the synthesis of chondroitin sulphate, but decreased the synthesis of proteoglycan by about 50%. These proteoglycans contained shorter chondroitin sulphate chains than their normal counterparts. The results indicate that although proteoglycans are mainly secretory components in human T-cell cultures, a specific metabolic step leads to the intracellular accumulation of free glycosaminoglycans. Separate functions are likely to be associated with the intracellular and secretory pools of chondroitin sulphate.
dc.language.isoenen
dc.subject.meshCells, Cultured
dc.subject.meshChloroquine
dc.subject.meshGlycosaminoglycans
dc.subject.meshGlycosides
dc.subject.meshHumans
dc.subject.meshProteoglycans
dc.subject.meshT-Lymphocytes
dc.titleThe synthesis of proteoglycans by human T lymphocytes.en
dc.typeArticleen
dc.contributor.departmentCRC Dept. Medical Oncology, Christie Hospital, Manchester, U.K.en
dc.identifier.journalBiochimica et Biophysica Actaen
html.description.abstractWe have examined the proteoglycans produced by highly-purified cultures of human T-lymphocytes. The proteoglycans were metabolically labelled with [35S]sulphate and analysed in cellular and medium fractions using DEAE-cellulose chromatography, gel filtration and specific enzymatic and chemical degradations. The results showed that the T cells synthesized a relatively homogeneous, proteinase-resistant chondroitin 4-sulphate proteoglycan that accumulated in the culture medium during a 48 h incubation period. The cellular fraction contained a significant amount of free chondroitin sulphate chains that were not secreted into the medium. These polysaccharides were formed by intracellular degradation of proteoglycan in a chloroquine-sensitive process, indicating a requirement for an acidic environment. In contrast to chondroitin sulphate derived from proteoglycan, chondroitin sulphates synthesized on the exogenous primer, beta-D-xyloside, were mainly secreted by the cells. beta-D-Xylosides caused an 8-fold stimulation in the synthesis of chondroitin sulphate, but decreased the synthesis of proteoglycan by about 50%. These proteoglycans contained shorter chondroitin sulphate chains than their normal counterparts. The results indicate that although proteoglycans are mainly secretory components in human T-cell cultures, a specific metabolic step leads to the intracellular accumulation of free glycosaminoglycans. Separate functions are likely to be associated with the intracellular and secretory pools of chondroitin sulphate.


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