| Autor: |
Praissman, Mel, Fox, Robin L., Walden, Mae, Praissman, Laura A., Kromholz, Noah W., Zahra, Tasneem, Abrar, Naim, Feffer, Stephen E., Grant, Margaret |
| Zdroj: |
Biochemical and Biophysical Research Communications; February 1998, Vol. 243 Issue: 3 p779-784, 6p |
| Abstrakt: |
A specific and saturable interaction between125I-gastrin and eosinophils was discovered in autoradiographs of human gastric mucosal tissue and confirmed in isolated and enriched preparations of WBC's. Gastrin displaced125I-gastrin from eosinophils in a dose-dependent manner with a D50= 11 uM. Scatchard analysis of the saturation curve indicated a single binding site of low affinity (Kd= 4.14 uM) and high capacity (Bmax= 430 umoles/mg protein). The gastrin binding protein was localized to the granular core of the eosinophil and found to have a molecular weight of ∼15 kDa following chemical crosslinking of radioligand to granules and SDS/PAGE. Based on its molecular weight and granular location and the charge characteristics of gastrin, the gastrin binding protein in the human eosinophil is most likely major basic protein.In vivothis interaction might act to limit the cytotoxic potential of MBP on tissues and/or attentuate gastrin concentrations thereby helping regulate gastric acid secretion and mucosal growth. |
| Databáze: |
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