Voltage-dependent calcium channels play a role in many cellular phenomena. Very little is known about Ca2+ channels in Drosophila, especially those in muscles. Existing literature on neuronal Ca2+ channels of Drosophila suggests that their pharmacology may be distinct from that of vertebrate Ca2+ channels. This raises questions on the pharmacology and diversity of Ca2+ channels in Drosophila muscles. Here we show that the Ca2+ channel current in the body-wall muscles of Drosophila larvae consists of two main components. One component is sensitive to 1,4-dihydropyridines and diltiazem, which block vertebrate L-type Ca2+ channels. The second component is sensitive to amiloride, which blocks vertebrate T-type Ca2+ channels. In contrast to Drosophila brain membrane preparations in which a majority of the Ca2+ channels are phenylalkylamine-sensitive but dihydropyridine-insensitive, the major current in the muscles was dihydropyridine-sensitive but relatively less sensitive to verapamil. This might indicate an underlying tissue specific distribution of distinct subtypes of dihydropyridine/phenylalkylamine-sensitive Ca2+ channels in Drosophila. Low verapamil sensitivity of the dihydropyridine-sensitive current of Drosophila muscles also set it apart from the vertebrate L-type channels which are sensitive to 1,4-dihydropyridines, benzothiazepines as well as phenylalkylamines. The dihydropyridine-sensitive current in Drosophila muscles activated in a similar voltage range as the vertebrate L-type current. As with the vertebrate current, blockade by dihydropyridines was voltage dependent.(ABSTRACT TRUNCATED AT 250 WORDS)
Analysis of the mechanisms underlying cardiac excitability can be facilitated greatly by mutations that disrupt ion channels and receptors involved in this excitability. With an extensive repertoire of such mutations, Drosophila provides the best available genetic model for these studies. However, the use of Drosophila for this purpose has been severely handicapped by lack of a suitable preparation of heart and a complete lack of knowledge about the ionic currents that underlie its excitability. We describe a simple preparation to measure heartbeat in Drosophila. This preparation was used to ask if heartbeat in Drosophila is myogenic in origin, and to determine the types of ion channels involved in influencing the heart rate. Tetrodotoxin, even at a high concentration of 40 microM, did not affect heart rate, indicating that heartbeat may be myogenic in origin and that it may not be determined by Na+ channels. Heart rate was affected by PN200-110, verapamil, and diltiazem, which block vertebrate L-type Ca2+ channels. Thus, L-type channels, which contribute to the prolonged plateau of action potentials in vertebrate heart, may play a role in Drosophila cardiac excitability. It also suggests that Drosophila heart is subject to a similar intervention by organic Ca2+ channel blockers as the vertebrate heart. A role for K+ currents in the function of Drosophila heart was suggested by an effect of tetraethylammonium, which blocks all the four identified K+ currents in the larval body wall muscles, and quinidine, which blocks the delayed rectifier K+ current in these muscles. The preparation described here also provides an extremely simple method for identifying mutations that affect heart rate. Such mutations and pharmacological agents will be very useful for analyzing molecular components of cardiac excitability in Drosophila.
Disruption of phospholipase C‐β (PLC) by the norpA mutations of Drosophila renders flies blind by affecting the light‐evoked photoreceptor potential. We report here that the norpA‐coded PLC modulates the 1,4‐dihydropyridine (DHP)‐sensitive Ca2+ channels in larval muscles. The DHP‐sensitive current was reduced in the norpA mutants. Application of 1 μM phorbol 12‐myristate 13‐acetate (TPA) and 1 μM phorbol 12,13‐didecanoate (PDD), activators of protein kinase C (PKC), rescued the current in the mutant fibers without significantly affecting the normal current. 4α‐phorbol 12,13‐didecanoate (4αPDD), an inactive analog of PDD, did not affect either the normal or the mutant current. One micromolar bisindolylmaleimide (BIM), an inhibitor of PKC, reduced the current in the normal fibers without affecting the mutant current. 300 μM sn‐1,2‐dioctanoyl‐glycerol (DOG), an analog of diacylglycerol (DAG), increased the current in the mutant fibers. These experiments suggest that the DHP‐sensitive Ca2+ channels in Drosophila may be modulated by the PLC‐DAG‐PKC pathway, and that the same PLC isozyme which is involved in phototransduction in the adult flies may also modulate muscle Ca2+ channels in the larval stage of development. © 1997 John Wiley & Sons, Inc. J Neurobiol 33: 265–275, 1997
Mutations and pharmacological agents have been used to resolve and analyze several K(+) currents in Drosophila. Mutations that affect channels carrying the voltage-activated I(A) and the Ca(2+) -activated I(CF) have helped greatly in analyzing the structure, function and regulation of these channels. We now report mutations that selectively affect the delayed rectifier current, I(K). Flies mutagenized with ethylmethanesulfonate were screened for temperature-induced paralysis. Paralytic mutants identified in the screen were examined for K(+) currents in the larval body-wall muscles. The z66 mutant larvae showed a significant reduction in I(K). The mutation did not affect other K(+) currents (I(A), I(CF), or I(CS) ) or the Ca(2+) channel current in the muscles. Another mutation, z4, which showed reduced I(K), failed to complement z66. Genetic analysis localized the gene disrupted by z66 and z4 to the left arm of chromosome 3, in the 63A1-63B6 region on polytene chromosomes. The z66 and the z4 mutations, which lie in the Shab K(+) channel gene, provide an opportunity to undertake analysis of the functioning of these channels and to study the role of these channels in membrane excitability.
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.
customersupport@researchsolutions.com
10624 S. Eastern Ave., Ste. A-614
Henderson, NV 89052, USA
This site is protected by reCAPTCHA and the Google Privacy Policy and Terms of Service apply.
Copyright © 2025 scite LLC. All rights reserved.
Made with 💙 for researchers
Part of the Research Solutions Family.