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Phosphorylation of brain (NA + ,K + )‐ATPase alpha catalytic subimits in normal and epileptic cerebral cortex: II. Partial seizures in human epilepsy
Author(s) -
Guillaume Daniel,
Grisar T.,
DelgadoEscueta A. V.,
Laschet J.,
BureauHeeren M.
Publication year - 1991
Publication title -
journal of neuroscience research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.72
H-Index - 160
eISSN - 1097-4547
pISSN - 0360-4012
DOI - 10.1002/jnr.490290212
Subject(s) - epilepsy , cerebral cortex , human brain , atpase , ictal , dephosphorylation , cortex (anatomy) , chemistry , alpha (finance) , phenytoin , phosphorylation , endocrinology , medicine , enzyme , microbiology and biotechnology , neuroscience , biology , biochemistry , phosphatase , construct validity , nursing , patient satisfaction
We examined the activity and phosphorylation level of (Na + , K + )‐ATPase (E.C. 3.6.1.3) partially puri fied from normal and epileptic human cortices. Con trol patients (n = 11) were operated on for a non‐ epileptogenic deep brain lesion, while epileptic patients (n = 10) were operated on for temporal or frontal originating partial seizures, resistant to med ications or secondary to evolutive brain tumors. No differences in the specific activity of microsomal (Na + , K + )‐ATPase were observed between the two groups of patients. After partial purification of the enzyme followed by SDS‐polyacrylaniide, gel. electrophoresis, (Na + , K + )‐ATPase catalytic subunit had a decreased affinity for K + in human epileptic cortex and lost its sensitivity to phenytoin dephosphorylation. Indirect evidence suggests that those abnormalities of (Na + , K + )‐ATPase in human epileptic cortex hold preferentially true for the alpha(–) enzymatic subunit. Those result indicate that, in human epileptic cortex, (Na + , K + ) glial subtype is altered in its K + regulation and phenytoin sensitivity and could be responsible for ictal transformation and seizure spread.