Resting membrane properties of locust muscle and their modulation I. Actions of the neuropeptides YGGFMRFamide and proctolin.
The resting K+ conductance (GK,r) of locust jumping muscle and its modulation by two neuropeptides, proctolin (Arg-Tyr-Leu-Pro-Thr) and YGGFMRFamide (Tyr-Gly-Gly-Phe-Met-Arg-Phe-NH2), were investigated using the two-electrode voltage clamp. At a physiological [K+]o of 10 mM, GK,r accounts for approximately 90% of the membrane resting conductance, and the resting membrane potential differs by </=1 mV from EK (mean: -74 mV). There is a K+ conductance that slowly activates on hyperpolarization (GK,H) and that seems to be largely located in the transverse tubules. Steady-state activation of GK,H was analyzed by tail current measurements. GK,H is activated partially at EK but accounts for probably </=50% of total resting K+ conductance. Raising [K+]o caused a large increase in GK,r and in maximal steady state GK,H without shifting the voltage sensitivity of GK,H. YGGFMRFamide and proctolin reduce GK,H, mainly affecting the maximal steady-state conductance. The voltage-insensitive component of the resting K+ conductance is also reduced. The conductance suppressed by the peptides exhibited an outwardly rectifying instantaneous current/voltage-characteristic that is quite similar to that of GK,H. The actions of the two peptides appeared to be identical, but proctolin was by some two orders of magnitude more potent than YGGFMRFamide. The effects of both peptides are mediated by G proteins. They are mimicked by phorbol esters but do not seem to be initiated by either branch of the phospholipase C-dependent intracellular pathways. The properties of the resting K+ conductance in locust muscle and other invertebrate muscles are compared. The biological significance of peptide-induced reduction in resting K+ conductance is discussed in view of the known property of proctolin to support tonic force as opposed to FMRFamide-peptides that support quick leg movements.
Walther
C
C
Physiological Institute, Neuroendocrinology Working Group, University of Marburg, 35037 Marburg, Germany.
Zittlau
K E
KE
Murck
H
H
Voigt
K
K
D000818:Animals; D002614:Chelating Agents / Q000494:pharmacology; D017364:Collagenases / Q000494:pharmacology; D004533:Egtazic Acid / Q000031:analogs & derivatives / Q000494:pharmacology; D004553:Electric Conductivity; D004744:Enkephalin, Methionine / Q000031:analogs & derivatives* / Q000494:pharmacology; D019204:GTP-Binding Proteins / Q000502:physiology; D006110:Grasshoppers; D016244:Guanosine 5'-O-(3-Thiotriphosphate) / Q000494:pharmacology; D007478:Iontophoresis; D008564:Membrane Potentials / Q000502:physiology; D009046:Motor Neurons / Q000737:chemistry / Q000187:drug effects* / Q000502:physiology*; D009132:Muscles / Q000294:innervation / Q000502:physiology; D009479:Neuropeptides; D018377:Neurotransmitter Agents / Q000494:pharmacology*; D009842:Oligopeptides / Q000494:pharmacology*; D018408:Patch-Clamp Techniques; D011188:Potassium / Q000378:metabolism; D015221:Potassium Channels / Q000502:physiology; D015290:Second Messenger Systems / Q000502:physiology
D002614:Chelating Agents; D009479:Neuropeptides; D018377:Neurotransmitter Agents; D009842:Oligopeptides; D015221:Potassium Channels; D016244:Guanosine 5'-O-(3-Thiotriphosphate); D004533:Egtazic Acid; C011536:proctolin; D004744:Enkephalin, Methionine; C027511:enkephalin-Met, Arg(6)-Phe(7)-; D017364:Collagenases; D019204:GTP-Binding Proteins; C025603:1,2-bis(2-aminophenoxy)ethane-N,N,N',N'-tetraacetic acid; D011188:Potassium