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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
1987-1-27
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pubmed:abstractText |
Hyaluronate synthase activity is localized exclusively in plasma-membrane fractions of cultured human skin fibroblasts. The enzyme activity of plasma membranes prepared from exponential-growth-phase cells was about 6.5 times that of stationary-growth-phase cells. Hyaluronate synthase from exponential-growth-phase cells exhibited lower Km and higher Vmax. values for both UDP-N-acetylglucosamine and UDP-glucuronic acid and higher rate of elongation of hyaluronate chains compared with the enzyme from stationary-growth-phase cells. Hyaluronate synthase exhibited an extremely short half-life, 2.2 h and 3.8 h respectively when cells were treated with cycloheximide and actinomycin D. The cell-growth-phase-dependent variations in hyaluronate synthase activity appear to be due to its high turnover rate as well as due to some post-translational modification of the enzyme protein as cells progress from early exponential to stationary growth phase. The isolated plasma membranes contained a protein (Mr approx. 450,000) that was selectively autophosphorylated from [gamma-32P]ATP in vitro in the presence of hyaluronate precursors in the reaction mixture and that also exhibited some hyaluronate-synthesis-related properties. The 32P-labelled protein isolated from plasma membranes of exponentially growing cells expressed an efficient UDP-[14C]glucuronic acid- and UDP-N-acetyl[3H]glucosamine-binding activity and was able to synthesize oligosaccharides (Mr 5000) of [14C]glucuronic acid and N-acetyl[3H]glucosamine residues. The corresponding protein of stationary-growth-phase cells, which expressed much higher nucleotide-sugar-precursor-binding activity, appeared to have lost its oligosaccharide-synthesizing activity.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/3099751-10976232,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3099751-11111,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3099751-13269385,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3099751-14025352,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3099751-14025353,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3099751-14340064,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3099751-14363113,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3099751-14907713,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3099751-166607,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3099751-175072,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3099751-189763,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3099751-194579,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3099751-194893,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3099751-293721,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3099751-3099752,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3099751-36172,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3099751-4178822,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3099751-4356572,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3099751-4652271,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3099751-500705,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3099751-5012760,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3099751-5644126,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3099751-5773295,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3099751-6248180,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3099751-6380494,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3099751-6743290,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3099751-6776108,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3099751-6870820,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3099751-7250300,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3099751-7358171,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3099751-809451,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3099751-9310
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0264-6021
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
237
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
333-42
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:3099751-Adenosine Triphosphate,
pubmed-meshheading:3099751-Cell Division,
pubmed-meshheading:3099751-Cell Line,
pubmed-meshheading:3099751-Cell Membrane,
pubmed-meshheading:3099751-Fibroblasts,
pubmed-meshheading:3099751-Glucuronosyltransferase,
pubmed-meshheading:3099751-Glycosyltransferases,
pubmed-meshheading:3099751-Humans,
pubmed-meshheading:3099751-Hyaluronic Acid,
pubmed-meshheading:3099751-Membrane Proteins,
pubmed-meshheading:3099751-Molecular Weight,
pubmed-meshheading:3099751-Peptide Chain Initiation, Translational,
pubmed-meshheading:3099751-Peptide Chain Termination, Translational,
pubmed-meshheading:3099751-Phosphorylation,
pubmed-meshheading:3099751-Transferases,
pubmed-meshheading:3099751-Xenopus Proteins
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pubmed:year |
1986
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pubmed:articleTitle |
Analysis of cell-growth-phase-related variations in hyaluronate synthase activity of isolated plasma-membrane fractions of cultured human skin fibroblasts.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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