Genetic variation in the carbonic anhydrase isozymes of macaque monkeys : III. Biosynthesis of carbonic anhydrases in bone marrow erythroid cells and peripheral blood reticulocytes of Macaco nemestrina

Abstract

The carbonic anhydrase isozymes (CA I and CA II) of the pig-tailed macaque, Macaca nemestrina, have been chosen to study the regulation of enzyme levels in red blood cells. Two quantitative variants of CA I that are ideal for studies of enzyme regulation exist in this species. One variant is one of four known electrophoretic types of CA I, designated CA Ia, which is present at levels about 30% of those of the other electrophoretic types. The other is a deficiency variant of CA I which, in homozygotes, reduces the product of the CA I locus about 5000-fold and reduces the product of the CA II locus by about 60%. -[14C]Serine was used to study the biosynthesis of CA I and CA II isozymes in the reticulocytes of animals carrying these CA I variants. Specific radioactivity and total incorporation data from bone marrow erythroid cells, and peripheral blood reticulocytes indicate that the reduced CA Ia concentration is probably the result of degradation. This degradation appears to occur for only a short time before the reticulocytes enter the peripheral blood. It was not possible to determine whether the 5000-fold reduction of CA I in the CA I-deficient animals is due to reduced transcription, reduced translation, or degradation. The effect of the CA I-deficiency mutation on the synthesis of CA II was also studied. For each dose of CA I-deficiency gene, there appears to be a 30% reduction in the rate of -[14C]serine incorporation into CA II, thereby accounting for the reduced CA II concentration in CA I-deficient animals.