Analysis of the Acid Phosphatases of Rat Sensory Gangli by Isoelectric Focussing on Polyacrylamide Gels

Abstract

The acid phosphatases of rat spinal and trigeminal ganglia were separated by isoelectric focusing on polyacrylamide gels into 2 main classes with pI [isoelectric point] of 7.1 and 5.4. A low-pI acid phosphatase is also present in the mouse but not in the guinea pig. Evidence is presented that in the rat, the pI 5.4 enzyme represents the nonlysosomal acid phosphatase that was identified histochemically in one population of sensory neurons. This pI 5.4 acid phosphatase is partly membrane-bound and is selectively depleted by capsaicin administration. In lumbar dorsal root ganglia, the enzyme is selectively depleted by sectioning the sciatic nerve and undergoes rapid axonal transport, a greater amount being transported peripherally than centrally. The results are discussed with reference to the possible function of this nonlysosomal acid phosphatase.