RGD Reference Report - Phosphorylation of the alpha subunit of initiation factor 2 correlates with the inhibition of translation following transient cerebral ischaemia in the rat. - Rat Genome Database

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Phosphorylation of the alpha subunit of initiation factor 2 correlates with the inhibition of translation following transient cerebral ischaemia in the rat.

Authors: Burda, J  Martin, ME  Garcia, A  Alcazar, A  Fando, JL  Salinas, M 
Citation: Burda J, etal., Biochem J. 1994 Sep 1;302 ( Pt 2):335-8.
RGD ID: 10395352
Pubmed: PMID:8092984   (View Abstract at PubMed)
PMCID: PMC1137233   (View Article at PubMed Central)

Rats were subjected to the standard four-vessel occlusion model of cerebral transient ischaemia (vertebral and carotid arteries) for 15 and 30 min. After a 30 min recirculation period, protein synthesis rate, initiation factor 2 (eIF-2) and guanine nucleotide exchange factor (GEF) activities, and the level of phosphorylation of the alpha subunit of eIF-2 (eIF-2 alpha) were determined in the neocortex region of the brain from sham-operated controls and ischaemic animals. Following reversible cerebral ischaemia, the protein synthesis rate, as measured in a cell-free system, was significantly inhibited (70%) in the ischaemic animals. eIF-2 activity, as measured by its ability to form a ternary complex, also decrease parallel to the decrease in protein synthesis. As eIF-2 activity was assayed in the presence of Mg2+ and GTP-regenerating capacity, the decrease in ternary-complex formation indicated the possible impairment of GEF activity. Since phosphorylated eIF-2 [eIF-2(alpha P)] is a powerful inhibitor of GEF, the levels of phosphorylated eIF-2 alpha were determined, and an increase from 7% phosphorylation in sham control rats to 20% phosphorylation in 15 min and 29% phosphorylation in 30 min in ischaemic rats was observed, providing evidence for a tight correlation of phosphorylation of eIF-2 alpha and inhibition of protein synthesis. Moreover, GEF activity measured in the GDP-exchange assay was in fact inhibited in the ischaemic animals, proving that protein synthesis is impaired by the presence of eIF-2(alpha P), which blocks eIF-2 recycling.



RGD Manual Disease Annotations    Click to see Annotation Detail View

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
EIF2S1HumanBrain Hypoxia-Ischemia  ISOEif2s1 (Rattus norvegicus) RGD 
Eif2s1RatBrain Hypoxia-Ischemia  IDA  RGD 
Eif2s1MouseBrain Hypoxia-Ischemia  ISOEif2s1 (Rattus norvegicus) RGD 

Objects Annotated

Genes (Rattus norvegicus)
Eif2s1  (eukaryotic translation initiation factor 2 subunit alpha)

Genes (Mus musculus)
Eif2s1  (eukaryotic translation initiation factor 2, subunit 1 alpha)

Genes (Homo sapiens)
EIF2S1  (eukaryotic translation initiation factor 2 subunit alpha)


Additional Information