Stimulation of fluid secretion of Malpighian tubules of Drosophila melanogaster Meig. by cyclic nucleotides of inosine, cytidine, thymidine and uridine
Ja. Riegel et al., Stimulation of fluid secretion of Malpighian tubules of Drosophila melanogaster Meig. by cyclic nucleotides of inosine, cytidine, thymidine and uridine, J EXP BIOL, 201(24), 1998, pp. 3411-3418
External application of the 3',5'-cyclic monophosphates of inosine, cytidin
e, uridine and thymidine stimulated the fluid secretion rate (FSR) of Malpi
ghian tubules isolated from Drosophila melanogaster. The evidence suggested
that the cyclic nucleotides acted intracellularly in some capacity. Recept
ors of the 'purinergic' type appeared not to be major contributors to fluid
secretion; of three purinergic agonists tried, adenosine, adenosine 5'-mon
ophosphate (AMP) and adenosine 5'-triphosphate (ATP), only adenosine had an
effect, but this was not observed consistently. None of the purinergic ago
nists interfered with the stimulation of the FSR by adenosine 3',5'-cyclic
monophosphate (cAMP), The maximum stimulation of the fluid-secretion rate b
y any cyclic nucleotide was approximately double the unstimulated (control)
rate. Tubules stimulated to less than maximal FSR by one cyclic nucleotide
could be stimulated maximally by an appropriate concentration of another c
yclic nucleotide. Malpighian tubules bathed in solutions that contained eit
her [H-3]cAMP or [H-3]cGMP accumulated radioactivity to a level many times
that in the medium. Accumulation of radioactivity by tubules bathed in 430n
moll(-1) [H-3]cAMP was suppressed by 1mmoll(-1) non-radioactive cyclic nucl
eotides in the order cAMP much greater than cGMP>cIMP>cCMP; neither cTMP no
r cUMP suppressed the accumulation of [H-3]cAMP. Approximately 35 % of the
[H-3]cAMP and 80 % of the [H-3]cGMP that entered the Malpighian tubule cell
s was metabolised to compounds that were not identified. It was concluded t
hat cyclic nucleotides enter the Malpighian tubule cells by at least one tr
ansport mechanism which is particularly sensitive to purine-based nucleotid
es.