Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1992-4-17
pubmed:abstractText
Mutants of Chinese hamster ovary cells have been found that no longer produce heparan sulfate. Characterization of one of the mutants, pgsD-677, showed that it lacks both N-acetylglucosaminyl- and glucuronosyltransferase, enzymes required for the polymerization of heparan sulfate chains. pgsD-677 also accumulates 3- to 4-fold more chondroitin sulfate than the wild type. Cell hybrids derived from pgsD-677 and wild type regained both transferase activities and the capacity to synthesize heparan sulfate. Two segregants from one of the hybrids reexpressed the dual enzyme deficiency, the lack of heparan sulfate synthesis, and the enhanced accumulation of chondroitin sulfate, suggesting that all of the traits were genetically linked. These findings indicate that the pgsD locus may represent a gene involved in the coordinate control of glycosaminoglycan formation.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/1532254-1028164, http://linkedlifedata.com/resource/pubmed/commentcorrection/1532254-107165, http://linkedlifedata.com/resource/pubmed/commentcorrection/1532254-14294058, http://linkedlifedata.com/resource/pubmed/commentcorrection/1532254-14907713, http://linkedlifedata.com/resource/pubmed/commentcorrection/1532254-1847668, http://linkedlifedata.com/resource/pubmed/commentcorrection/1532254-1883201, http://linkedlifedata.com/resource/pubmed/commentcorrection/1532254-1931081, http://linkedlifedata.com/resource/pubmed/commentcorrection/1532254-2016281, http://linkedlifedata.com/resource/pubmed/commentcorrection/1532254-2022632, http://linkedlifedata.com/resource/pubmed/commentcorrection/1532254-2061321, http://linkedlifedata.com/resource/pubmed/commentcorrection/1532254-2522106, http://linkedlifedata.com/resource/pubmed/commentcorrection/1532254-2524477, http://linkedlifedata.com/resource/pubmed/commentcorrection/1532254-2524478, http://linkedlifedata.com/resource/pubmed/commentcorrection/1532254-2545696, http://linkedlifedata.com/resource/pubmed/commentcorrection/1532254-2691858, http://linkedlifedata.com/resource/pubmed/commentcorrection/1532254-2957376, http://linkedlifedata.com/resource/pubmed/commentcorrection/1532254-3129423, http://linkedlifedata.com/resource/pubmed/commentcorrection/1532254-3137658, http://linkedlifedata.com/resource/pubmed/commentcorrection/1532254-3346331, http://linkedlifedata.com/resource/pubmed/commentcorrection/1532254-3782085, http://linkedlifedata.com/resource/pubmed/commentcorrection/1532254-3858816, http://linkedlifedata.com/resource/pubmed/commentcorrection/1532254-4260846, http://linkedlifedata.com/resource/pubmed/commentcorrection/1532254-6454688, http://linkedlifedata.com/resource/pubmed/commentcorrection/1532254-7018909, http://linkedlifedata.com/resource/pubmed/commentcorrection/1532254-9127
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0027-8424
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
89
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2267-71
pubmed:dateRevised
2010-9-7
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
A single mutation affects both N-acetylglucosaminyltransferase and glucuronosyltransferase activities in a Chinese hamster ovary cell mutant defective in heparan sulfate biosynthesis.
pubmed:affiliation
Department of Biochemistry, School of Medicine, University of Alabama, Birmingham 35294.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't