These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


PUBMED FOR HANDHELDS

Search MEDLINE/PubMed


  • Title: Complex pattern of inhibition by Mg2+ of exocytosis from permeabilised eosinophils.
    Author: Larbi KY, Gomperts BD.
    Journal: Cell Calcium; 1997 Mar; 21(3):213-9. PubMed ID: 9105730.
    Abstract:
    Inhibition by Mg2+ ions of exocytotic secretion from permeabilised eosinophils, stimulated by Ca2+ and GTP gamma S, and in the presence and absence of ATP, has been examined. While Mg2+ inhibits release of aryl sulphatase, hexosaminidase and peroxidase, we found no evidence that this occurs by competition at a Ca(2+)-binding site. On the other hand, the IC50 for Mg2+ approximates a simple inverse relationship to EC50 for GTP gamma S over a wide range of concentrations, indicative of a possible competition with events directly controlled by a GTP-binding protein. However, for secretion stimulated by GTP gamma S in the absence of Ca2+ (which necessitates provision of ATP), the effect of Mg2+ becomes biphasic. Initially, secretion is dependent on the presence of Mg2+ as a component of the complex ligand Mg.ATP. At high concentrations, Mg2+ inhibits secretion and the IC50 was found to be fixed at a concentration of about 8 mM regardless of the strength of the stimulus. The presence of ATP appears to divert the site of inhibition due to Mg2+.
    [Abstract] [Full Text] [Related] [New Search]