K+ transport in Malpighian tubules of Tenebrio molitor L.: is a KATP channel involved?

Author:

Wiehart U. I. M.1,Klein G.2,Steels P.2,Nicolson S. W.1,Van Kerkhove E.2

Affiliation:

1. Department of Zoology and Entomology, University of Pretoria, Pretoria 0002, South Africa

2. Laboratory of Physiology, Biomed CMK, Limburgs Universitair Centrum, B3590 Diepenbeek, Belgium

Abstract

SUMMARY The presence of ATP-regulated K+ (KATP) channels in Tenebrio molitor Malpighian tubules was investigated by examining the effect of glibenclamide on both fluid secretion and basolateral membrane potentials (Vbl). Glibenclamide, a KATP channel blocker, slowed fluid secretion of Tenebrio tubules. In low bath K+ concentration (5 mmol l-1), glibenclamide either hyperpolarized or depolarized Vbl, resembling the effect seen with Ba2+. Subsequent addition of 6 mmol l-1Ba2+ caused a further hyper- or depolarization of Vbl. In control Ringer (50 mmol l-1 KCl, 90 mmol l-1 NaCl), glibenclamide had no visible effect on Vbl. The effect of ouabain was investigated in low bath[K+] in the presence of Ba2+. Vblresponded by a small but significant hyperpolarization from -51±4 mV to-56±4 mV (n=16, P<0.001) in response to 1 mmol l-1 ouabain. Repeating the experiments in the presence of both glibenclamide and Ba2+ resulted in a depolarization of Vbl when ouabain was added. In low bath [K+](high Na+), the Na+/K+-ATPase is expected to function at a high rate. In the presence of Ba2+, replacing Na+ by K+ rapidly depolarized Vbl,but this was followed by a repolarization. Repeating the experiments in the presence of glibenclamide markedly reduced the depolarizing effect and abolished the repolarization, with a gradual decrease in the sensitivity of Vbl to the surrounding [K+]. These results suggest the presence of KATP channels in the basolateral membrane. Glibenclamide had no visible effect on Vbl in high K+ or in the absence of Ba2+, indicating that other highly conductive K+ channels may mask the effect on KATP channels. This is the first demonstration of the presence of KATP channels in an insect epithelium.

Publisher

The Company of Biologists

Subject

Insect Science,Molecular Biology,Animal Science and Zoology,Aquatic Science,Physiology,Ecology, Evolution, Behavior and Systematics

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