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Literature summary for 3.4.17.21 extracted from

  • Choi, J.; Kim, J.; Jo, S.
    Acetylation regulates the stability of glutamate carboxypeptidase II protein in human astrocytes (2014), Biochem. Biophys. Res. Commun., 450, 372-377.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Homo sapiens Q04609
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Posttranslational Modification

Posttranslational Modification Comment Organism
acetylation treatment with valproic acid increases the acetylation of glutamate carboxypeptidase II protein at the lysine residues and facilitates a decrease of the poly-ubiquitinated glutamate carboxypeptidase II level. Similarly, M344, a specific histone deacetylase 1/6 inhibitor, also increases the glutamate carboxypeptidase II protein level Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
astrocyte
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Homo sapiens
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U-87MG cell
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Homo sapiens
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Synonyms

Synonyms Comment Organism
GCPII
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Homo sapiens

General Information

General Information Comment Organism
metabolism acute exposure to valproic acid, a drug used for bipolar disorder and epilepsy and a known histone deacetylase inhibitor, for 4-6 h increases the glutamate carboxypeptidase II protein level in human astrocyte U-87MG cells but does not have a similar effect after 12-24 h exposure. Valproic acid does not affect the glutamate carboxypeptidase II mRNA expression, but decrease in glutamate carboxypeptidase II protein level by cycloheximide treatment is blocked by valproic acid. The valproic acid-induced increase of glutamate carboxypeptidase II protein level may be dependent on the ubiquitin/proteasome pathway. Valproic acid increases the acetylation of glutamate carboxypeptidase II protein at the lysine residues and facilitates a decrease of the poly-ubiquitinated glutamate carboxypeptidase II level. Similarly, M344, a specific histone deacetylase 1/6 inhibitor, also increases the glutamate carboxypeptidase II protein level Homo sapiens