Xylosyl transfer to the core protein precursor of the rat chondrosarcoma proteoglycan

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Fältnamn	Indikatorer	Metadata
000		03682naa a2200289 4500
001		oai:lup.lub.lu.se:52f6a2c0-7074-42f4-ae84-0c0dbf6711b3
003		SwePub
008		160504s1989 \| \|\|\|\|\|\|\|\|\|\|\|000 \|\|eng\|
024	7	a https://lup.lub.lu.se/record/52f6a2c0-7074-42f4-ae84-0c0dbf6711b32 URI
040		a (SwePub)lu
041		a engb eng
042		9 SwePub
072	7	a art2 swepub-publicationtype
072	7	a ref2 swepub-contenttype
100	1	a Lohmander, Stefanu Lund University,Lunds universitet,Ortopedi, Lund,Sektion III,Institutionen för kliniska vetenskaper, Lund,Medicinska fakulteten,Lund OsteoArthritis Division - Nedbrytning av ledbrosk: en biologisk process som leder till artros,Forskargrupper vid Lunds universitet,Orthopaedics (Lund),Section III,Department of Clinical Sciences, Lund,Faculty of Medicine,Lund OsteoArthritis Division - Molecular marker research group,Lund University Research Groups4 aut0 (Swepub:lu)ort-slo
245	1 0	a Xylosyl transfer to the core protein precursor of the rat chondrosarcoma proteoglycan
264	1	c 1989
300		a 6 s.
520		a Rat chondrosarcoma chondrocytes were labeled with [3H]serine or [3H]mannose as a precursor. Intracellular proteoglycan core protein precursor was purified from cell lysates by immunoprecipitation with polyclonal antibodies against the hyaluronic acid-binding region, followed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The core precursor was eluted from the gels and treated with alkaline borohydride in order to convert serine residues substituted with xylose or N-acetylgalactosamine to alanine (or with alkaline sulfite to convert them to cysteic acid). After acid hydrolysis, the proportions of labeled serine and alanine (or cysteic acid) were determined by high performance liquid chromatography, and the results were compared with those obtained for the completed proteoglycan molecules isolated from the same cultures. In the completed proteoglycans, about 55% of the serine residues were substituted with xylose or N-acetylgalactosamine, while the corresponding figure for the intracellular precursor molecules was less than 5%. These results indicate, in agreement with our previous kinetic data, that the major part of the xylosyl transfer to the chondrosarcoma proteoglycan core protein precursor must occur late in the processing sequence, i.e. after about 85% of its intracellular lifetime and no more than 7 min before the addition of the rest of the chondroitin sulfate chain. The ratio of [3H]mannose to [3H]fucose in the core precursor was about 19, while that for the complete proteoglycan was about 2. This indicates the presence of high mannose, N-linked oligosaccharides on the core protein precursor which are converted to the complex forms on the completed proteoglycan. These data provide further support that the core precursor resides mainly in the pre-Golgi compartment and that xylosylation occurs mainly in a Golgi compartment.
650	7	a MEDICIN OCH HÄLSOVETENSKAPx Medicinska och farmaceutiska grundvetenskaperx Cell- och molekylärbiologi0 (SwePub)301082 hsv//swe
650	7	a MEDICAL AND HEALTH SCIENCESx Basic Medicinex Cell and Molecular Biology0 (SwePub)301082 hsv//eng
700	1	a Shinomura, T.u Rush University Medical Center Chicago4 aut
700	1	a Hascall, V. C.u National Institutes of Health, United States4 aut
700	1	a Kimura, J. H.u Rush University Medical Center Chicago4 aut
710	2	a Ortopedi, Lundb Sektion III4 org
773	0	t Journal of Biological Chemistryg 264:31, s. 18775-18780q 264:31<18775-18780x 0021-9258
856	4 8	u https://lup.lub.lu.se/record/52f6a2c0-7074-42f4-ae84-0c0dbf6711b3

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Av författaren/redakt...: Lohmander, Stefa ...; Shinomura, T.; Hascall, V. C.; Kimura, J. H.

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