Abstract
The affinity of four distinct types of folate binding sites and of two membrane-bound folate degrading enzymes for 15 folic acid derivatives was monitored. Apart from two types (A H and A L of binding sites, all binding classes or enzymes show different affinity patterns. This strongly suggests the observed binding sites to be nonidentical to the membrane-bound folate deaminase or folate C 9-N 10 cleaving enzyme. The analog specificity of the chemotactic response towards folates shows a strong resemblance to the specificity of binding to one of the binding classes: ‘B-sites’ ( p < 0.01%). Less or no correlation was observed between the other classes or the enzymes and the chemotactic response. This may indicate that the B-sites are involved in the transduction of an extracellular signal to chemotactic cell movement. Folates elicit secretion of cAMP. Recently, the activity of several folate derivatives to evoke a cAMP response was studied (Devreotes, P.N. (1983) Dev. Biol. 95, 154–162). Comparison of this activity and the specificity of the binding sites in this study, suggests that the ‘A-sites’ are involved in the cAMP response.
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