Eclosion Hormone Stimulates Cyclic GMP Levels in <i>Manduca sexta</i> Nervous Tissue via Arachidonic Acid Metabolism with Little or No Contribution from the Production of Nitric Oxide

Morton, David B.; Giunta, Michael A.

doi:10.1111/j.1471-4159.1992.tb08469.x

Cited by 45 publications

(51 citation statements)

References 36 publications

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“…Biochemical results obtained using the abdominal CNS of Manduca suggest that EH stimulates cGMP via metabolites of arachidonic acid (Morton and Giunta, 1992). In contrast, experiments in the commercial silkworm, Bombyx mori, on saponin-treated ganglia support a pathway leading from inositol triphosphate production and through subsequent calcium activation of nitric oxide synthase and, hence, to the soluble guanylate cyclase (Shibanaka et al, 1993(Shibanaka et al, , 1994.…”

Section: Role Of Synaptic Interactions In the Eh-induced Increase In mentioning

confidence: 94%

Neuropeptide induction of cyclic GMP increases in the insect CNS: resolution at the level of single identifiable neurons

1994

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In insects, the neuropeptide eclosion hormone (EH) acts on the CNS to evoke the stereotyped behaviors that cause ecdysis, the shedding of the cuticle at the end of each molt. Concomitantly, EH induces an increase in cyclic GMP (cGMP). Using antibodies against this second messenger, we show that this increase is confined to a network of 50 peptidergic neurons distributed throughout the CNS. Increases appeared 30 min after EH treatment, spread rapidly throughout these neurons, and were extremely long lived. We show that this response is synaptically driven, and does not involve the soluble, nitric oxide (NO)-activated, guanylate cyclase. Stereotyped variations in the duration of the cGMP response among neurons suggest a role in coordinating responses having different latencies and durations.

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Section: Role Of Synaptic Interactions In the Eh-induced Increase In mentioning

confidence: 94%

Neuropeptide induction of cyclic GMP increases in the insect CNS: resolution at the level of single identifiable neurons

1994

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“…Biochemical characterization of the eclosion hormone-stimulated cGMP increase suggested that eclosion hormone might activate a NOinsensitive, soluble guanylyl cyclase (15)(16)(17)(18). In an attempt to identify the pathway for eclosion hormone-stimulated cGMP levels, we used reverse transcription-polymerase chain reaction (RT-PCR) to identify guanylyl cyclases from Manduca nervous tissue.…”

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confidence: 99%

Identification and Characterization of a Novel β Subunit of Soluble Guanylyl Cyclase That Is Active in the Absence of a Second Subunit and Is Relatively Insensitive to Nitric Oxide

Nighorn

Byrnes

Morton

1999

Journal of Biological Chemistry

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Previously characterized soluble guanylyl cyclases form ␣-␤ heterodimers that can be activated by the gaseous messenger, nitric oxide. In mammals, four subunits have been cloned, named ␣1, ␣2, ␤1, and ␤2. We have identified a novel soluble guanylyl cyclase isoform from the nervous system of the insect Manduca sexta that we have named M. sexta guanylyl cyclase ␤3 (MsGC-␤3). It is most closely related to the mammalian ␤ subunits but has several features that distinguish it from previously identified soluble cyclases. Most importantly, MsGC-␤3 does not need to form heterodimers to form an active enzyme because guanylyl cyclase activity can be measured when it is expressed alone in COS-7 cells. Moreover, this activity is only weakly enhanced in the presence of the nitric oxide donor, sodium nitroprusside. Several of the amino acids in rat ␤1 subunits, previously identified as being important in heme binding or necessary for nitric oxide activation, are substituted with nonsimilar amino acids in MsGC-␤3. There are also an additional 315 amino acids C-terminal to the catalytic domain of MsGC-␤3 that have no sequence similarity to any known protein. Northern blot analysis shows that MsGC-␤3 is primarily expressed in the nervous system of Manduca.The intracellular messenger cGMP mediates a wide variety of cellular and physiological processes. It functions as the primary messenger in visual transduction (1, 2), is an important regulator in vascular smooth muscle and kidney function (3, 4), and has been implicated in a number of forms of neuronal plasticity (5-7).The enzymes that regulate the synthesis of cGMP fall into two major classes: the cytoplasmically localized, soluble guanylyl cyclases and the membrane associated, receptor guanylyl cyclases (4). Soluble guanylyl cyclases are obligate heterodimers composed of an ␣ and a ␤ subunit. Two ␣ (␣1 and ␣2) and two ␤ (␤1 and ␤2) subunits have been cloned from mammalian tissues (8 -13). The active heterodimer requires and binds heme as a prosthetic group and can be potently activated by the gaseous messenger, nitric oxide (NO) 1 (14). The soluble cyclases are found in the cytosol of cells, although the mammalian ␤2 subunit has a consensus isoprenylation site, suggesting that it might be associated with membranes. The receptor guanylyl cyclases, by contrast, are integral membrane proteins with transmembrane and extracellular domains (4).We have been using the insect Manduca sexta as a model system to study cGMP regulation and have previously shown that a neuropeptide, eclosion hormone, is a potent stimulator of cGMP levels in the central nervous system (15). Biochemical characterization of the eclosion hormone-stimulated cGMP increase suggested that eclosion hormone might activate a NOinsensitive, soluble guanylyl cyclase (15-18). In an attempt to identify the pathway for eclosion hormone-stimulated cGMP levels, we used reverse transcription-polymerase chain reaction (RT-PCR) to identify guanylyl cyclases from Manduca nervous tissue. This approach has yielded a number of dif...

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“…An alternate possibility is that an NO-insensitive enzyme might be targeted by an albsteric regulatory factor analogous to (but distinct from) NO. For example, numerous studies document the ability of arachidonic acid (or one of its downstream metabolites) to stimulate guanylate cyclase activity in cytoplasm isolated from both vertebrate (Waldman and Murad, 1987) and invertebrate (Morton and Giunta, 1992) tissues. In insects, it is believed that this is how eclosion hormone activates cyclic GMP synthesis in a set of neurons that are insensitive to NO (Morton and Giunta, 1992;Morton and Simpson, 1995).…”

Section: Discussionmentioning

confidence: 99%

Identification of Nitric Oxide‐Sensitive and ‐Insensitive Forms of Cytoplasmic Guanylate Cyclase

Prabhakar

Short

Scholz

et al. 1997

Journal of Neurochemistry

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Cytoplasmic, nitric oxide-activated guanylate cyclases are expressed in many regions of the mammaian brain and are thought to participate in functions as diverse as synaptogenesis and long-term potentiation. In this study, we have characterized cytoplasmic guanylate cyclases in the nervous system of an invertebrate, the American lobster. Cytoplasmic cyclase specific activity is higher in lobster nerve cord than in any other lobster tissue tested, and considerably higher than in typical rat tissues (cerebellum, lung, and liver). However, nitric oxide donors have minimal effects on lobster nerve cord cyclic GMP production, when applied either to intact tissue or to cytoplasmic extracts. Parallel immunocytochemical studies, using an anti-cyclic GMP antibody, reveal that only a small subset of lobster neurons responds to nitric oxide with a significant elevation of cyclic GMP levels. HPLC analysis of nerve cord cytoplasm reveals two chromatographically separable cyclases, a minor nitric oxide-sensitive form whose retention time is identical to that of the conventional mammalian enzyme and a more abundant nitric oxide-insensitive form that appears to be novel. The physiological function and phylogenetic distribution of this nitric oxide-insensitive enzyme, and the signaling mechanisms that regulate its activity, are not known.

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Eclosion Hormone Stimulates Cyclic GMP Levels in Manduca sexta Nervous Tissue via Arachidonic Acid Metabolism with Little or No Contribution from the Production of Nitric Oxide

Cited by 45 publications

References 36 publications

Neuropeptide induction of cyclic GMP increases in the insect CNS: resolution at the level of single identifiable neurons

Neuropeptide induction of cyclic GMP increases in the insect CNS: resolution at the level of single identifiable neurons

Identification and Characterization of a Novel β Subunit of Soluble Guanylyl Cyclase That Is Active in the Absence of a Second Subunit and Is Relatively Insensitive to Nitric Oxide

Identification of Nitric Oxide‐Sensitive and ‐Insensitive Forms of Cytoplasmic Guanylate Cyclase

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