A brain polypeptide termed diazepam-binding inhibitor (DBI) and thought to be chemically and functionally related to the endogenous effector of the benzodiazepine recognition site was purified to homogeneity. This peptide gives a single band of protein on NaDodSO4 and acidic urea gel electrophoresis. A single UV-absorbing peak was obtained by HPLC using three different columns and solvent systems. DBI has a molecular mass of 411,000 daltons. Carboxyl-terminus analysis shows that tyrosine is the only residue while the amino-terminus was blocked. Cyanogen bromide treatment of DBI yields three polypeptide fragments, and the sequences of two of them have been determined for a total of 45 amino acids. DBI is a competitive inhibitor [3H]imipramine binding tested at their respective Kd values. DBI injected intraventricularly at doses of 5-10 nmol completely reversed the anticonflict action of diazepam on unpunished drinking and, similar to the anxiety-inducing 1-carboline derivative FG 7142 (13-carboline-3-carboxylic acid methyl ester), facilitated the shockinduced suppression of drinking by lowering the threshold for this response.

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We report the clinical, laboratory, EEG, and SPECT findings in a 59-year-old euthyroid woman with previously undiagnosed autoimmune thyroiditis, subclinical hypothyroidism, and rapidly progressive dementia. We made a diagnosis of Hashimoto's encephalopathy based on elevated thyrotropin, abnormal EEG, and clinical improvement after thyroid hormone replacement. SPECT demonstrated global hypoperfusion with normalization on clinical recovery, suggesting a possible mechanism for the pathogenesis of Hashimoto's encephalopathy.

This randomized clinical trial evaluates the safety and efficacy of the monoclonal anti-tau antibody semorinemab in individuals with prodromal to mild Alzheimer disease.