RGD Reference Report - Modulation of glycogen phosphorylase activity affects 5-phosphoribosyl-1-pyrophosphate availability in rat hepatocyte cultures. - Rat Genome Database

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Modulation of glycogen phosphorylase activity affects 5-phosphoribosyl-1-pyrophosphate availability in rat hepatocyte cultures.

Authors: Boer, P  Sperling, O 
Citation: Boer P and Sperling O, Nucleosides Nucleotides Nucleic Acids. 2004 Oct;23(8-9):1235-9.
RGD ID: 1599376
Pubmed: PMID:15571236   (View Abstract at PubMed)
DOI: DOI:10.1081/NCN-200027496   (Journal Full-text)

The effect of modulation of the rate of glycogenolysis on the availability of 5-phosphoribosyl-1-pyrophosphate (PRPP) was investigated in rat hepatocyte cultures. Dibutyryl cyclic AMP (dbcAMP), forskolin and glucagon, activating glycogen phosphorylase through activation of protein kinase A (PKA), were found to raise PRPP availability by 44%-56%. Arg-vasopressin and phenylephrine, activating glycogen phosphorylase through the phosphoinositide cascade, did not affect PRPP availability. dbcAMP, but not phenylephrine, increased the degradation of pre labeled glycogen by 57%. Caffeine and CP-91149, inhibitors of glycogen phosphorylase, decreased PRPP availability by 33% and 43%, respectively. The finding that induction of glycogenolysis enhances, and inhibition of glycogenolysis decelerates PRPP generation suggests that glycogenolysis is a major contributor to PRPP generation in liver tissue in the basal (postabsorptive) state.



Gene Ontology Annotations    Click to see Annotation Detail View

Biological Process

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
PyglRat5-phosphoribose 1-diphosphate biosynthetic process  IMP  RGD 

Molecular Function

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
PyglRatglycogen phosphorylase activity  IMP  RGD 

Objects Annotated

Genes (Rattus norvegicus)
Pygl  (glycogen phosphorylase L)


Additional Information