RGD Reference Report - Activation of dolichol-phosphate mannosyltransferase by dibutryl cyclic AMP in rat liver. - Rat Genome Database

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Activation of dolichol-phosphate mannosyltransferase by dibutryl cyclic AMP in rat liver.

Authors: Sharma, C  Radhakrishnamurthy, B  Berenson, GS 
Citation: Sharma C, etal., Biochem Biophys Res Commun. 1988 Sep 15;155(2):615-21.
RGD ID: 1601442
Pubmed: (View Article at PubMed) PMID:2844175

Radiolabeled mannose incorporation into secretory glycoproteins and immunoprecipitable fibronectin in the incubation media significantly increased (105 and 32 percent respectively) with a corresponding increase in the levels of dolichol-phosphate mannose, dolichol-diphosphate oligosaccharides and dolichol-phosphate mannosyltransferase activity in the rat liver slices when incubated with dibutryl cAMP and ATP. Dibutryl cAMP activated maximally this enzyme in the presence of ATP in the incubation medium. The activation of the enzyme resulted in a two fold increase in Vmax with no apparent change in the Km for GDP mannose. Phosphorylation the rat liver microsomes with catalytic subunit of cAMP dependent protein kinase, resulted in the activation of dolichol-phosphate mannosyltransferase. These results suggest that cAMP modulates protein glycosylation by activating dolicholphosphate mannosyltransferase activity. The activation of this enzyme could be through phosphorylation/dephosphorylation mechanism involving a cAMP dependent protein kinase.

Annotation

Gene Ontology Annotations    

Biological Process

Cellular Component

Molecular Function

Objects Annotated

Genes (Rattus norvegicus)
Dpm1  (dolichyl-phosphate mannosyltransferase subunit 1, catalytic)


Additional Information