[Lactate dehydrogenase isoenzymes in sympathetic neurons and satellite glial cells in normal animals and after nicotinic acetylcholine receptor blockade].

Using the method of integral cytophotometry, lactate dehydrogenase (LDH) N- and M-isoform activity was determined in neurons and satellite glial cells in tissue sections of rabbit cervical cranial sympathetic ganglion under normal conditions and after experimentally induced total and partial pharmacological blockade of nicotinic acetylcholine receptors (N-CR). In normal animals, activity of N- and M-isoforms was demonstrated in both cellular types, however, their LDH isoenzyme profile was different: N-isoforms prevailed in neurons, while M-isoforms were more active in glial cells. After partial and total blockade, activity of LDH, N- and M-isoforms was significantly reduced in neurons in proportion to the number of N-CR blocked. In satellite glial cells, the increase of blockade intensity was accompanied by the reduction of only M-isoform activity, while that of N-isoforms remained unchanged. After partial N-CR blockade, satellite glial cell LDH isoenzyme profile was shifted in the direction of a neuronal one, and after total blockade became indistinguishable from LDH isoenzyme profile of intact neurons. It is suggested that lactate formation in satellite glial cells is induced by N-cholinergic synapse activity, which directly mediates the neuron-glial interaction and participates in control of LDH enzyme system activity in sympathetic neurons.