Modlin I M, Oddsdottir M, Adrian T E, Zdon M J, Zucker K A, Goldenring J R
J Surg Res. 1987 Apr;42(4):348-53. doi: 10.1016/0022-4804(87)90168-5.
Histamine-stimulated phosphorylation was studied in isolated rabbit parietal cells. Secretion of acid, as assessed by aminopyrine uptake, was linear at 15 min of stimulation with histamine. By utilizing two dimensional gels, a specific 30,000-Da protein (pp30) was identified whose phosphorylation was prominently stimulated by histamine after 15 min of incubation. The pp30 protein displayed an isoelectric point of 6.0. Furthermore, cAMP-dependent pp30 phosphorylation could also be demonstrated in vitro in a preparation of parietal cell cytosol. The results suggest that pp30 may represent an important histamine-stimulated cAMP-dependent phosphoprotein involved in the initiation or maintenance of parietal cell secretion.
在分离的兔壁细胞中研究了组胺刺激的磷酸化作用。通过氨基比林摄取评估的酸分泌，在用组胺刺激15分钟时呈线性。利用二维凝胶，鉴定出一种特定的30,000道尔顿蛋白质（pp30），其磷酸化在孵育15分钟后受到组胺的显著刺激。pp30蛋白的等电点为6.0。此外，在壁细胞胞质溶胶制剂中也可在体外证明cAMP依赖性的pp30磷酸化。结果表明，pp30可能代表一种重要的组胺刺激的cAMP依赖性磷蛋白，参与壁细胞分泌的起始或维持。
