rdf:type |
|
lifeskim:mentions |
umls-concept:C0010453,
umls-concept:C0016030,
umls-concept:C0017968,
umls-concept:C0030685,
umls-concept:C0086418,
umls-concept:C0220781,
umls-concept:C0391871,
umls-concept:C0680255,
umls-concept:C1123023,
umls-concept:C1283071,
umls-concept:C1963578
|
pubmed:issue |
1
|
pubmed:dateCreated |
1978-2-18
|
pubmed:abstractText |
1. Confluent human skin fibroblasts maintained in a chemically defined medium incorporate l-[1-(3)H]fucose in a linear manner with time into non-diffusible macromolecules for up to 48h. Chromatographic analysis demonstrated that virtually all the macromolecule-associated (3)H was present as [(3)H]fucose. 2. Equilibrium CsCl-density-gradient centrifugation established that [(3)H]fucose-labelled macromolecules released into the medium were predominantly glycoproteins. Confirmation of this finding was provided by molecular-size analyses of the [(3)H]fucose-labelled material before and after trypsin digestion. 3. The [(3)H]fucose-labelled glycoproteins released into fibroblast culture medium were analysed by gel-filtration chromatography and sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. These techniques demonstrated that the major fucosylated glycoprotein had an apparent mol.wt. of 230000-250000; several minor labelled species were also detected. 4. Dual-labelling experiments with [(3)H]fucose and (14)C-labelled amino acids indicated that the major fucosylated glycoprotein was synthesized de novo by cultured fibroblasts. The non-collagenous nature of this glycoprotein was established by three independent methods. 5. Gel-filtration analysis before and after reduction with dithiothreitol showed that the major glycoprotein occurs as a disulphide-bonded dimer when analysed under denaturing conditions. Further experiments demonstrated that this glycoprotein was the predominant labelled species released into the medium when fibroblasts were incubated with [(35)S]cysteine. 6. The relationship between the major fucosylated glycoprotein and a glycoprotein, or group of glycoproteins, variously known as fibronectin, LETS protein, cell-surface protein etc., is discussed.
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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
|
pubmed:status |
MEDLINE
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pubmed:month |
Oct
|
pubmed:issn |
0264-6021
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pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
15
|
pubmed:volume |
168
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pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
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pubmed:pagination |
91-103
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:202258-Humans,
pubmed-meshheading:202258-Ascorbic Acid,
pubmed-meshheading:202258-Skin,
pubmed-meshheading:202258-Cysteine,
pubmed-meshheading:202258-Fucose,
pubmed-meshheading:202258-Molecular Weight,
pubmed-meshheading:202258-Glycoproteins,
pubmed-meshheading:202258-Fibroblasts,
pubmed-meshheading:202258-Cells, Cultured,
pubmed-meshheading:202258-Macromolecular Substances,
pubmed-meshheading:202258-Microbial Collagenase
|