Identification of a Novel Guanylyl Cyclase That Is Related to Receptor Guanylyl Cyclases, but Lacks Extracellular and Transmembrane Domains

Simpson, P. Jeanette; Nighorn, Alan; Morton, David B.

doi:10.1074/jbc.274.7.4440

Cited by 35 publications

(30 citation statements)

References 24 publications

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“…The regulation of the generation of cGMP through the activation of guanilate cyclase, responsible for cGMP synthesis, is involved in the adaptation of the olfactory cells of Antheraea polyphemus and Bombix mori (Ziegelberger et al, 1990). These results are also supported by the finding of different types of guanilate cyclase in M. sexta (Simpson et al, 1999;Nighorn et al, 2001;Stengl et al, 2001;Morton & Nighorn, 2003).…”

Section: Discussionsupporting

confidence: 74%

Deterrence of feeding in Rhodnius prolixus (Hemiptera: Reduviidae) after treatment of antennae with a nitric oxide donor

Sfara¹,

Zerba²,

Alzogaray³

2011

Eur. J. Entomol.

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Abstract. The blood-sucking bug Rhodnius prolixus is the main vector of Chagas Disease in Colombia, Venezuela and several countries in Central America. Nitric oxide (NO) is a ubiquitous gaseous molecule present in most types of cell and participates in the olfactory pathway of insects. In this work, nitroso-acetyl-cysteine (SNAC), a nitric oxide donor, was topically applied to the antennae of fifth instar nymphs of R. prolixus. After SNAC treatment, these insects showed a dose-dependent reluctance to feed when provided with a living pigeon as the food source (ED50 = 5.2 µg/insect). However, there was no reluctance to feed when dbcGMP was applied to the antennae of nymphs. In another experiment, insects that had their antennae treated with SNAC were less attracted than the control group to a CO2 source. A possible role of NO in the olfactory pathway of R. prolixus is discussed.

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Section: Discussionsupporting

confidence: 74%

Deterrence of feeding in Rhodnius prolixus (Hemiptera: Reduviidae) after treatment of antennae with a nitric oxide donor

Sfara¹,

Zerba²,

Alzogaray³

2011

Eur. J. Entomol.

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“…We have previously identified additional guanylyl cyclases within the nervous system of Manduca, which are either NO-sensitive heterodimeric cyclases (19) or NO-insensitive cyclases (32). MsGC-␤3 forms a complementary class of guanylyl cyclase that is active as a homomer and only weakly activated by NO.…”

Section: Discussionmentioning

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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“…Interest in the cGMP-dependent serine/threonine kinase, or PKG, has grown with the awareness of the diversity of biochemical pathways that involve cGMP (Koesling et al 1991;Garbers 1992;Sheth et al 1997;Wang and Robinson 1997;Moon et al 1998;Simpson et al 1999). PKG has been shown to influence characteristics involved in both functional and developmental plasticity of neural circuits (Zhuo et al 1994(Zhuo et al , 1999Lev-Ram et al 1997;Wu et al 1998b;Calabresi et al 1999;Lewin and Walters 1999;Renger et al 1999;Yawo 1999).…”

mentioning

confidence: 99%

A cGMP-Dependent Protein Kinase Gene, foraging, Modifies Habituation-Like Response Decrement of the Giant Fiber Escape Circuit in Drosophila

Engel¹,

Xie²,

Sokolowski³

et al. 2000

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The Drosophila giant fiber jump-and-flight escape response is a model for genetic analysis of both the physiology and the plasticity of a sensorimotor behavioral pathway. We previously established the electrically induced giant fiber response in intact tethered flies as a model for habituation, a form of nonassociative learning. Here, we show that the rate of stimulus-dependent response decrement of this neural pathway in a habituation protocol is correlated with PKG (cGMP-Dependent Protein Kinase) activity and foraging behavior. We assayed response decrement for natural and mutant rover and sitter alleles of the foraging (for) gene that encodes a Drosophila PKG. Rover larvae and adults, which have higher PKG activities, travel significantly farther while foraging than sitters with lower PKG activities. Response decrement was most rapid in genotypes previously shown to have low PKG activities and sitter-like foraging behavior. We also found differences in spontaneous recovery (the reversal of response decrement during a rest from stimulation) and a dishabituation-like phenomenon (the reversal of response decrement evoked by a novel stimulus). This electrophysiological study in an intact animal preparation provides one of the first direct demonstrations that PKG can affect plasticity in a simple learning paradigm. It increases our understanding of the complex interplay of factors that can modulate the sensitivity of the giant fiber escape response, and it defines a new adult-stage phenotype of the foraging locus. Finally, these results show that behaviorally relevant neural plasticity in an identified circuit can be influenced by a single-locus genetic polymorphism existing in a natural population of Drosophila.Protein kinases play key roles in the activity-dependent modulation of neuronal activity and morphology. Interest in the cGMP-dependent serine/threonine kinase, or PKG, has grown with the awareness of the diversity of biochemical pathways that involve cGMP (Koesling et al.

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Identification of a Novel Guanylyl Cyclase That Is Related to Receptor Guanylyl Cyclases, but Lacks Extracellular and Transmembrane Domains

Cited by 35 publications

References 24 publications

Deterrence of feeding in Rhodnius prolixus (Hemiptera: Reduviidae) after treatment of antennae with a nitric oxide donor

Deterrence of feeding in Rhodnius prolixus (Hemiptera: Reduviidae) after treatment of antennae with a nitric oxide donor

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

A cGMP-Dependent Protein Kinase Gene, foraging, Modifies Habituation-Like Response Decrement of the Giant Fiber Escape Circuit in Drosophila

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