胃酸分泌酵素の構造と細胞特異的転写

概要

論文の詳細を見る
Progress in molecular biological studies on the H^+/K^+-ATPase (gastric proton pump) now enables us to discuss not only its subunit protein structures and catalysis but also the organizations of its subunit genes and their cell-specific transcription. The primary structures of the catalytic α and glycosylated β subunits and their transmembrane topology are similar to those of the corresponding subunits of Na^+/K^+-ATPase. The exon/intron organizations of the genes for the H^+/K^+-ATPase α and β subunits are closely similar to those of the corresponding subunits of Na^+/K^+-ATPase, suggesting that the α and β subunit genes of the two ATPases were respectively derived from common ancestors. In contrast to ubiquitous Na^+/K^+-ATPase, the H^+/K^+-ATPase is expressed specifically in gastric parietal cells. Consistent with this fact, we found novel zinc finger proteins which are present in the gastric parietal cells and recognize a gastric sequence motif in the 5'-upstream regions of the H^+/K^+-ATPase α and β subunit genes. The proteins are likely to play important roles in the transcriptional regulation of the parietal cell specific genes.
公益社団法人日本薬学会の論文
1995-01-25