Effect of monensin on the levels of tachykinins and their processing enzyme activity in rat dorsal root ganglia.
Th effect of monensin, which inhibits trans-Golgi function, on the levels of tachykinins and their processing enzyme activity was examined in organ-cultured rat dorsal root ganglia (DRG). Using an enzyme immunoassay method, we measured neurokinin A and substance P immunoreactivity in the DRG cultured for 72 h with and without 0.1 microM monensin. Both tachykinins were reduced in the DRG treated with monensin. Treatment with monensin also reduced the activity of carboxypeptidase E, which is one of the proteolytic processing enzymes of neuropeptides. These data suggest that proteolytic processing enzymes may in part modulate the biological activity of neuropeptides within a trans-Golgi apparatus.
Chikuma
Toshiyuki
T
Department of Hygienic Chemistry, Showa Pharmaceutical University, Machida 194-8543, Japan.
Inomata
Yuji
Y
Tsuchida
Ken
K
Hojo
Hiroshi
H
Kato
Takeshi
T
D000818:Animals; D043423:Carboxypeptidase H; D002268:Carboxypeptidases / Q000037:antagonists & inhibitors*; D005727:Ganglia, Spinal / Q000187:drug effects* / Q000378:metabolism*; D007476:Ionophores / Q000494:pharmacology*; D008297:Male; D008985:Monensin / Q000494:pharmacology*; D015288:Neurokinin A / Q000037:antagonists & inhibitors*; D009924:Organ Culture Techniques; D051381:Rats; D017208:Rats, Wistar; D013373:Substance P / Q000037:antagonists & inhibitors*
D007476:Ionophores; D013373:Substance P; D015288:Neurokinin A; D008985:Monensin; D002268:Carboxypeptidases; D043423:Carboxypeptidase H