Language dominance in mesial temporal lobe epilepsy: a functional transcranial Doppler sonography study of brain plasticity.

Functional transcranial Doppler sonography was used to study hemispheric language dominance (HLD) in 24 right-handed patients with left temporal lobe epilepsy (TLE) and a structural lesion in the left temporal lobe and in 69 healthy controls. Twenty-five percent of the patients and 4% of controls showed atypical (right or bilateral) HLD. Degree of HLD was not correlated with age, Full Scale IQ, Verbal IQ, spike frequency, seizure frequency, age at seizure onset, or duration of TLE.

Inhibition by adenosine A(2A) receptors of NMDA but not AMPA currents in rat neostriatal neurons.

Whole-cell patch clamp experiments were used to investigate the transduction mechanism of adenosine A(2A) receptors in modulating N-methyl-D-aspartate (NMDA)-induced currents in rat striatal brain slices. The A(2A) receptor agonist 2-p-(2-carboxyethyl)phenethylamino-5'-N-ethylcarboxamidoadenosine (CGS 21680) inhibited the NMDA, but not the (S)-alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) current in a subset of striatal neurons. Lucifer yellow-filled pipettes in combination with immunostaining of A(2A) receptors were used to identify CGS 21680-sensitive cells as typical medium spiny striatal neurons.

Adenosine A2A receptors inhibit the conductance of NMDA receptor channels in rat neostriatal neurons.

Whole-cell patch clamp experiments were carried out in rat striatal brain slices. In a subset of striatal neurons (70-80%), NMDA-induced inward currents were inhibited by the adenosine A2A receptor selective agonist CGS 21680. The non-selective adenosine receptor antagonist 8-(p-sulphophenyl)-theophylline and the A2A receptor selective antagonist 8-(3-chlorostyryl)caffeine abolished the inhibitory action of CGS 21680.

Mutants with substitutions for Glu171 in the catabolite activator protein (CAP) of Escherichia coli activate transcription from the lac promoter.

Single amino acid substitutions for residue Glu171 in helix E of the catabolite gene activator protein (CAP) of Escherichia coli have been reported to abolish activation of transcription without impairing binding to the CAP site of the lac promoter. The negative charge of Glu171 was proposed to transmit the activating signal from CAP to RNA polymerase. However, this idea has been challenged by later work.