Primary structure of four allatostatins: neuropeptide inhibitors of juvenile hormone synthesis.

Woodhead, Andrea P.; Stay, Barbara; Seidel, Sharon L.; Khan, M. A. Q.; Tobe, Stephen S.

doi:10.1073/pnas.86.15.5997

Cited by 359 publications

(206 citation statements)

References 32 publications

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“…The allostatins, an important group of insect neuropeptides, have a C-terminal tripeptide sequence (Phe-Gly-Leu) that is also found in substance P [19]. A second group of insect neuropeptides, the sulfakinins, has amino acid sequence similarity to the mammalian neuropep- tides, cholecystokinin and gastrin.…”

Section: Discussionmentioning

confidence: 99%

Cloning and Characterisation of Angiotensin‐Converting Enzyme from the Dipteran Species, Haematobia irritans exigua, and Its Expression in the Maturing Male Reproductive System

Wijffels

Fitzgerald

Gough

et al. 1996

European Journal of Biochemistry

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The angiotensin-converting enzymes (ACE) are involved in the regulation of the specific maturation or degradation of a number of mammalian bioactive peptides. A carboxydipeptidase similar to mammalian ACE has now been identified in the adult stage of the haematophagous fly, Haematobia irritans exigua (buffalo fly), a close relative of the horn fly of North America. The enzyme was purified by lectin-affinity chromatography and ion-exchange chromatography and migrated as a doublet of 70 kDa upon reducing SDSPAGE. Unlike mammalian ACE, the fly carboxydipeptidase (HieACE) is not membrane bound. The amino acid sequence of an internal peptide from HieACE and a conserved amino acid region present in all mammalian ACE were used to design degenerate oligonucleotide primers suitable for PCR. A DNA fragment amplified from adult buffalo fly cDNA was used to identify a cDNA clone that encoded the enzyme. The cDNA sequence encodes a carboxydipeptidase with 41-42% amino acid identity to the mammalian testicular ACE. The active-site regions of mammalian ACE are conserved in the deduced amino acid sequence of HieACE. Enzymatically, HieACE is very similar to its mammalian counterparts, with comparable K. , and V,,, values for the synthetic substrate, benzoylglycylglycylglycine, and similar patterns of inhibition by EDTA, ACE inhibitor peptide and captopril. HieACE also specifically activates angiotensin I to angiotensin I1 and degrades other mammalian ACE substrates such as bradykinin, substance P and cholecystokinin-8. In the adult fly, HieACE is expressed in the compound ganglion and in the posterior region of the midgut. Similar to the mammalian system, expression of this enzyme is induced in the maturing male reproductive system, which suggests conservation of ACE function in these species.

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Section: Discussionmentioning

confidence: 99%

Cloning and Characterisation of Angiotensin‐Converting Enzyme from the Dipteran Species, Haematobia irritans exigua, and Its Expression in the Maturing Male Reproductive System

Wijffels

Fitzgerald

Gough

et al. 1996

European Journal of Biochemistry

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“…AS-A was initially identified by its inhibitory activity on JH production in the cockroach D. punctata (Pratt et al 1989;Woodhead et al 1989). We have previously reported that Aedes AS-A have no effect on JH biosynthesis in female A. aegypti ).…”

Section: Discussionmentioning

confidence: 99%

“…Allatostatins (AS) and allatotropins (AT) are structurally diverse peptides that were first described as modulators of juvenile hormone (JH) biosynthesis in the corpora allata (CA) of a number of insect species (Kataoka et al 1989;Woodhead et al 1989;Kramer et al 1991;Lorenz and Hoffmann 1995;Gilbert et al 2000). AS and AT have subsequently been recognized as having multiple physiological effects, controlling processes such as heart rate and gut motility, nutrient absorption, migratory preparedness, and modulation of the circadian cycle (Bendena et al 1999;Nässel 2002;Petri et al 2002;Elekonich and Horodyski 2003).…”

Section: Introductionmentioning

confidence: 99%

Immunostaining for allatotropin and allatostatin-A and -C in the mosquitoes Aedes aegypti and Anopheles albimanus

Hernández‐Martínez

Lanz‐Mendoza

et al. 2005

Cell Tissue Res

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Confocal laser-scanning microscopy was used to carry out a comparative study of the immunostaining for three families of neuropeptides, viz., allatostatin-A (AS-A), allatostatin-C (AS-C) and allatotropin (AT), in adult female mosquitoes of Aedes aegypti and Anopheles albimanus. The specific patterns of immunostaining for each of the three peptides were similar in both species. The antisera raised against AT, AS-A, and AS-C revealed intense immunoreactivity in the cells of each protocerebral lobe of the brain and stained cells in each of the ventral ganglia and neuronal projections innervating various thoracic and abdominal tissues. Only the AS-A antiserum labeled immunoreactive endocrine cells in the midgut. The distribution of the peptides supports the concept that they play multiple regulatory roles in both species.

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“…Allatostatins are a family of neuropeptides that share a conserved C-terminal sequence -Tyr/PheXaaPheGlyLeu-NH 2 and are widespread throughout the invertebrate lineage (9,10). In insects, allatostatins regulate numerous physiological functions, including inhibition of juvenile hormone biosynthesis (11,12), inhibition of muscle contraction (13), myoendocrine regulation (14,15), neuromodulation (16), and regulation of enzymatic activities (17) and ecdysis (18). Similarly, mammalian galanin modulates a wide variety of processes that range from neurotransmission, nociception, feeding and metabolism, energy and osmotic homeostasis and learning and memory (19).…”

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confidence: 99%

A Caenorhabditis elegans allatostatin/galanin-like receptor NPR-9 inhibits local search behavior in response to feeding cues

Bendena

Boudreau

Papanicolaou

et al. 2008

Proc. Natl. Acad. Sci. U.S.A.

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Movement inCaenorhabditis elegans is the result of sensory cues creating stimulatory and inhibitory output from sensory neurons. Four interneurons (AIA, AIB, AIY, and AIZ) are the primary recipients of this information that is further processed en route to motor neurons and muscle contraction. C. elegans has >1,000 G proteincoupled receptors (GPCRs), and their contribution to sensory-based movement is largely undefined. We show that an allatostatin/ galanin-like GPCR (NPR-9) is found exclusively in the paired AIB interneuron. AIB interneurons are associated with local search/ pivoting behavior. npr-9 mutants display an increased local search/ pivoting that impairs their ability to roam and travel long distances on food. With impaired roaming behavior on food npr-9 mutants accumulate more intestinal fat as compared with wild type. Overexpression of NPR-9 resulted in a gain-of-function phenotype that exhibits enhanced forward movement with lost pivoting behavior off food. As such the animal travels a great distance off food, creating arcs to return to food. These findings indicate that NPR-9 has inhibitory effects on the AIB interneuron to regulate foraging behavior, which, in turn, may affect metabolic rate and lipid storage.neuropeptide receptor ͉ nerve transmission ͉ foraging ͉ glutamate receptor ͉ interneuron A major challenge in neurobiology is to understand the control of behavior at the molecular level. Neuropeptides and their receptors offer promising candidates for the regulation of various behaviors and changes in physiology. The Caenorhabditis elegans genome sequence has allowed the identification of 109 putative neuropeptide genes encoding precursors that may be processed to Ϸ250 neuropeptides (1-3). These neuropeptides are grouped into three families: FMRFamide-related peptides (f lp), insulin-like peptides (ins), and neuropeptide-like-peptides (nlps). C. elegans expresses Ͼ1,000 orphan G protein-coupled receptors (GPCRs). More than 50 GPCRs resemble known receptors for known neuropeptide families based on phylogenetic comparisons with known vertebrate GPCRs (4). Of these GPCRs, based on sequence identity, C. elegans gene ZK455.3 expresses an nlp receptor, NPR-9, that is most similar to insect allatostatin/ mammalian galanin receptors (5-8). Allatostatins are a family of neuropeptides that share a conserved C-terminal sequence -Tyr/PheXaaPheGlyLeu-NH 2 and are widespread throughout the invertebrate lineage (9, 10). In insects, allatostatins regulate numerous physiological functions, including inhibition of juvenile hormone biosynthesis (11, 12), inhibition of muscle contraction (13), myoendocrine regulation (14, 15), neuromodulation (16), and regulation of enzymatic activities (17) and ecdysis (18). Similarly, mammalian galanin modulates a wide variety of processes that range from neurotransmission, nociception, feeding and metabolism, energy and osmotic homeostasis and learning and memory (19). We report that NPR-9 is uniquely localized in interneuron AIB to negatively regulate a variety of inputs th...

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Primary structure of four allatostatins: neuropeptide inhibitors of juvenile hormone synthesis.

Cited by 359 publications

References 32 publications

Cloning and Characterisation of Angiotensin‐Converting Enzyme from the Dipteran Species, Haematobia irritans exigua, and Its Expression in the Maturing Male Reproductive System

Cloning and Characterisation of Angiotensin‐Converting Enzyme from the Dipteran Species, Haematobia irritans exigua, and Its Expression in the Maturing Male Reproductive System

Immunostaining for allatotropin and allatostatin-A and -C in the mosquitoes Aedes aegypti and Anopheles albimanus

A Caenorhabditis elegans allatostatin/galanin-like receptor NPR-9 inhibits local search behavior in response to feeding cues

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