Vitamin B-6 deficiency alters rat enterocyte calcium homeostasis but not duodenal transport.

Isolated enterocytes were used as differential transporting cells to examine calcium homeostasis in control and vitamin B-6-deficient rats. Kinetic analysis of calcium fluxes, as well as biochemical determinations, indicated that enterocytes from control animals had high concentrations of cytosol ionized calcium (318.5 +/- 22.

Activation of liver cytosol phosphoenolpyruvate carboxykinase by Ca2+ through intracellular redistribution of Mn2+.

Calcium has no known direct effect on phosphoenolpyruvate carboxykinase from rat liver cytosol. However, addition of calcium salts to liver postnuclear supernatant led to an increase in assayable enzyme activity in cytosols. This indicates that mitochondria and microsomes present in postnuclear supernatant can participate in observed enzyme activation.

Inhibition of glutamate dehydrogenase activity in rabbit renal mitochondria by phosphoenolpyruvate.

The effect of phosphoenolpyruvate on glutamate dehydrogenase activity was studied in both intact and Triton X-100-treated rabbit renal mitochondria. The intramitochondrial phosphoenolpyruvate content was modulated by application of both 3-MPA, an inhibitor of phosphoenolpyruvate carboxykinase, and BTCA, which inhibits the tricarboxylate-transporting system. The data indicate that: (i) phosphoenolpyruvate is a potent inhibitor of glutamate dehydrogenase activity; and (ii) its inhibitory effect on the enzyme may be abolished by leucine and ADP, activators of glutamate dehydrogenase.