Yukari Ikeda

Autoimmune Regulator (AIRE) Gene Is Expressed in Human Activated CD4 T-Cells and Regulated by Mitogen-Activated Protein Kinase Pathway

The autoimmune regulator (AIRE) gene is a gene responsible for autoimmune polyendocrinopathy‐candidiasis‐ectodermal dystrophy. Here we show that AIRE is expressed in human peripheral CD4‐positive T‐cells, and most highly in antigen‐ and interleukin 2‐stimulated T (IL‐2T) cells. Mitogen‐activated protein kinases (MAPKs), including MAPK kinase (MEK) 1/2 and p38 MAPK, were phosphorylated in IL‐2T cells and the expression of the AIRE gene was inhibited by a specific p38 MAPK inhibitor (SB203580), thereby indicating that AIRE gene expression is controlled by the MAPK pathway in IL‐2T cells. These data suggested the possible significance of the AIRE gene in the peripheral immune system.

Synthesis of Methyl 2-Cyano-(1,2-dimethylcyclohepta[b]pyrrol-6-ylidene)acetate. A Steric Effect to Accelerate the Geometrical Isomerism of the Exocyclic C=C Bond of Heterocycle-fused Heptafulvenes

The rotational barriers of the exocyclic C = C bonds of heptafulvenes condensed with furan, pyrrole, and thiophene rings were largely dependent on the steric repulsion around the exocyclic C = C bonds; newly synthesized methyl 2-cyano-(1,2-dimethylcyclohepta[b]pyrrol-6-ylidene)acetate and its furanylidene analogue revealed higher energy barriers than the corresponding methyl 2-cyano-(1,2-dimethylcyclohepta[b]pyrrol-8-ylidene)acetate and the furan derivative

Chemical Reactivity of Oxidation Products of the Dithiolanylidenemalonate Fungicide, Isoprothiolane

Diisopropyl dithiolanylidenemalonate (isoprothiolane) was oxidized with m-chloroperbenzoic acid to give a monosulfoxide, disulfoxide, and disulfone. The monosulfoxide was subjected to addition reactions with such nucleophiles as methanol, thiols, and amines at the thioacetal carbon to open the dithiolane ring, affording a thiosulfinate, sulfinate and disulfide. The presence of a small amount of sodium carbonate accelerated the reactions and, moreover, reformed isoprothiolane from the ring-opened addition products. The further oxidation products were transformed into dithianes by reacting with nucleophiles. Isoprothiolane monosulfoxide inhibited alcohol dehydrogenase, an SH enzyme.