rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
1
|
pubmed:dateCreated |
1985-3-20
|
pubmed:abstractText |
beta-Adrenoreceptor stimulation of rat parotid acinar cells increases the activity of several microsomal membrane associated, dolichylmonophosphate (Dol-P) linked glycosyltransferases. The activities of Man-P-Dol synthase and Glc-P-Dol synthase are increased by approximately 50%, and the activity of N-acetylglucosaminyl 1-phosphate transferase plus N-acetylglucosaminyl transferase increased by approximately 60%, after agonist treatment. Increases in enzyme activity are (i) independent of endogenous Dol-P levels and (ii) observed under conditions in which the specific activities of donor sugar nucleotides are kept constant. Activation of these enzymes is specific since comparable levels of NADPH-cytochrome c reductase are found in control and agonist-treated membranes. The data thus provide the initial demonstration of neurotransmitter modulation of enzymes in the dolichol-linked pathway of protein N-glycosylation.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Jan
|
pubmed:issn |
0006-291X
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
16
|
pubmed:volume |
126
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
123-9
|
pubmed:dateRevised |
2003-11-14
|
pubmed:meshHeading |
pubmed-meshheading:2982364-Animals,
pubmed-meshheading:2982364-Dolichol Phosphates,
pubmed-meshheading:2982364-Hexosyltransferases,
pubmed-meshheading:2982364-Isoproterenol,
pubmed-meshheading:2982364-Male,
pubmed-meshheading:2982364-Microsomes,
pubmed-meshheading:2982364-Parotid Gland,
pubmed-meshheading:2982364-Polyisoprenyl Phosphates,
pubmed-meshheading:2982364-Rats,
pubmed-meshheading:2982364-Rats, Inbred Strains,
pubmed-meshheading:2982364-Receptors, Adrenergic, beta,
pubmed-meshheading:2982364-Tunicamycin
|
pubmed:year |
1985
|
pubmed:articleTitle |
beta-Adrenergic activation of glycosyltransferases in the dolichylmonophosphate-linked pathway of protein N-glycosylation.
|
pubmed:publicationType |
Journal Article
|