Studies on Avian Erythrocyte Metabolism. XII. The Synthesis and Degradation of Inositol Pentakis (Dihydrogen Phosphate)

Abstract

The pathway(s) of synthesis and degradation of inositol 1, 3, 4, 5, 6 pentakis (dihydrogen phosphate) (inositol-P5), found predominantly in the avian erythrocyte, are unknown. Myo-inositol (inositol), D-glucose, inosine, and phosphate have been studied as potential precursors of inositol-P5 synthsis in chicken erythrocytes. Whole blood from chickens at several ages has been incubated for prolonged periods and the concentration of inositol-P5 measured to determine the ability of the avian erythrocyte to catabolize inositol-P5.Incubation of erythrocyte suspensions from 5-day chicks with [U-14C] myo-inositol (inositol) for 17 hr lead to the appearance of 19.8% of the radioactivity in the aqueous acid-soluble extract of the erythrocytes (RBC). Fractionation of this extract on an anion exchange column yielded five major radioactive peaks, three of which represent 1) free myo-inositol, accounting for 63.5% of the radioactivity; 2) myo-inositol monokis (dihydrogen phosphate) (inositol-P), representing 1.6% of the radioactivity; and 3) inositol 1, 3, 4, 5, 6 pentakis (dihydrogen phosphate) (inositol-P5), representing 27.0% of the label in the erythrocyte. Sodium fluoride did not inhibit the incorporation of [U-14 C] myo-inositol into inositol-P5. Similar incubations with D-[U-14 Cl -glucose and [U-14 C]-inosine yielded no incorporation of radioactivity into inositol-P5. These data are consistent with the interpretation that inositol is the major precursor for synthesis of inositol-P5 in chick red cells.Incubation of whole blood from 1-, 5-, and 42-day chicks and mature birds at 40 C for as long as 72 hr resulted in increases in RBC inorganic phosphate (Pi) thought due primarily to depletion of adenosine triphosphate (ATP). Inositol-P5 content of RBC of 5- and 42-day birds decreased 28 and 20%, respectively, after 72 hr, but no change was noted in inositol-P5 levels of RBC from mature birds. The red cells of the mature bird appear to be unable to catabolize inositol-P5 at significant rates.The apparent inability of the chicken erythrocyte to alter readily its concentration of inositol-P5 suggests that the hemoglobin oxygen delivery system of birds may be less adaptable to changing oxygen requirements by regulating the concentration of hemoglobin modulator than is that of the mammals.