Isolation and identification of a diuretic hormone from the tobacco hornworm,
            <i>Manduca sexta</i>

Kataoka, Hiroshi; Troetschler, Ruth G.; Li, Jorge P.; Kramer, Steven J.; Carney, Robert L.; Schooley, David A.

doi:10.1073/pnas.86.8.2976

Cited by 175 publications

(97 citation statements)

References 31 publications

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“…Studies conducted primarily in insect models, where only a single CRH-like peptide (DHs) is present, suggest that the earliest function of the peptide family was associated with diuresis and feeding (Kataoka et al 1989, Audsley et al 1997, Coast 2007, 1998. Given the phylogenetic age of the CRH peptides, this is not surprising.…”

Section: Description Of Crh Family Of Peptides and Their Functionsmentioning

confidence: 99%

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MOLECULAR EVOLUTION OF GPCRS: CRH/CRH receptors

Lovejoy¹,

Chang²,

Lovejoy³

et al. 2014

Journal of Molecular Endocrinology

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Corticotrophin-releasing hormone (CRH) is the pivotal neuroendocrine peptide hormone associated with the regulation of the stress response in vertebrates. However, CRH-like peptides are also found in a number of invertebrate species. The origin of this peptide can be traced to a common ancestor of lineages leading to chordates and to arthropods, postulated to occur some 500 million years ago. Evidence indicates the presence of a single CRH-like receptor and a soluble binding protein system that acted to transduce and regulate the actions of the early CRH peptide. In vertebrates, genome duplications led to the divergence of CRH receptors into CRH1 and CRH2 forms in tandem with the development of four paralogous ligand lineages that included CRH; urotensin I/urocortin (Ucn), Ucn2 and Ucn3. In addition, taxon-specific genome duplications led to further local divergences in CRH ligands and receptors. Functionally, the CRH ligand-receptor system evolved initially as a molecular system to integrate early diuresis and nutrient acquisition. As multicellular organisms evolved into more complex forms, this ligand-receptor system became integrated with the organismal stress response to coordinate homoeostatic challenges with internal energy usage. In vertebrates, CRH and the CRH1 receptor became associated with the hypothalamo-pituitary-adrenal/interrenal axis and the initial stress response, whereas the CRH2 receptor was selected to play a greater role in diuresis, nutrient acquisition and the latter aspects of the stress response.

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Section: Description Of Crh Family Of Peptides and Their Functionsmentioning

confidence: 99%

“…In 1989, a peptide hormone associated with diuresis in the tobacco hornworm (Manduca sexta; Kataoka et al 1989) was characterised and showed remarkable structural similarity to the CRH peptides, notably SVG. Its high degree of residue identity indicated that it was homologous to the vertebrate CRH.…”

Section: Discovery Evolution and Function Of Crh Peptidesmentioning

confidence: 99%

MOLECULAR EVOLUTION OF GPCRS: CRH/CRH receptors

Lovejoy¹,

Chang²,

Lovejoy³

et al. 2014

Journal of Molecular Endocrinology

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“…It is a 41 residues, C-terminally amidated peptide that has 29-35% sequence identity with the vertebrate CRF family of peptides. 64) Insect DHs are produced by the median neurosecretory cells (MNC) as well as neurosecretory cells in the abdominal ganglia. Axons from these regions reach the corpora cardiaca and perisympathetic organs and other neurohemal release sites.…”

Section: Diuretic Hormones (Dh)mentioning

confidence: 99%

Molecular physiology of crustacean and insect neuropeptides

Mercier¹,

Doucet

Retnakaran³

2007

J. Pestic. Sci.

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One of the principal hallmarks of a living organism is its ability to respond to stimuli. As the unicellular organisms evolved into multicellular metazoans, the external signals perceived had to be transduced to several other cells requiring a neuronal network with its accompanying biochemical neurotransmitters. The progressive increase in complexity of the organisms necessitated the need for an integrated signal transducing system collecting external sensory stimuli and sending them to effector systems such that a dynamic equilibrium or homeostasis, which is essential for survival, could be maintained. During the course of evolution many advanced sense organs were developed to detect various parameters in the environment, and concomitantly different internal effector systems were formed to respond to these signals received from outside to maintain homeostasis. Coordination was achieved with a network of electrical conductors in the form of an arborized nervous system and a variety of hydrophilic biochemicals that acted as neurotransmitters carrying the sensory signals to the internal effector systems. As the animal became increasingly complex, a sophisticated neurotransmission system catering to the spatial and temporal needs during growth, development and reproduction had to be in place. Parts of the nervous tissue in many locations took on a secretory role and released protein signal transducers, the neuropeptides. A panoply of such neuropeptides exist in all organisms functioning as neurohormones, neurotransmitters or neuromodulators. Aspects of neuropeptide structure and function in insects and crustaceans have been reviewed by various authors. [1][2][3][4][5][6][7][8][9][10] The neuropeptides are ligands to their cognate receptors in the ef- Organisms have to constantly respond to environmental conditions to maintain a status of dynamic homeostasis for survival. As single celled organisms evolved into multicellular animals, intercellular and inter-organ communications became indispensable not only to orchestrate homeostasis but also to control the many events punctuating metazoan development. To accomplish this need, a signal transduction system was evolved, consisting of an arborized network of nerves as well as a collection of oligopeptide neurotransmitters (neuropeptides) along with their cognate receptors. We review here the current state of our understanding of the physiology of neuropeptides in the most species-rich group of animals, the crustaceans and insects. The vast majority of neuropeptides signal through cell-surface guanosine-protein coupled receptors (GPCRs). These neuropeptide-receptor systems control a variety of physiological functions, for instance the numerous involuntary movements of internal ducts that are precisely timed for transporting reproductive, digestive and secretory materials. The rigid exoskeleton in Crustaceans and Insects require periodic molts to accomplish growth and metamorphosis and this is harmoniously regulated by a cascade of neuropeptides. Neuropeptides also regul...

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“…This peptide shows homology to a family of vertebrate neuropeptides, including sauvagine, corticotropin-releasing factor, and urotensin I (1). Since the isolation of Mas-DH, other peptides of related structure, which function in regulating fluid balance in insects, have been isolated from Manduca (2) and from two orthopteran genera: Locusta (3,4) and Acheta (5).…”

mentioning

confidence: 99%

“…Manduca sexta diuretic hormone (Mas-DH) is an amidated 41-amino acid peptide that was isolated from pharate adult tobacco hornworm heads on the basis of induction of fluid loss in beheaded adult cabbageworms (1). This peptide shows homology to a family of vertebrate neuropeptides, including sauvagine, corticotropin-releasing factor, and urotensin I (1).…”

mentioning

confidence: 99%

Characterization of the precursor for Manduca sexta diuretic hormone Mas-DH.

Digan¹,

Roberts²,

Enderlin³

et al. 1992

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

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We have isolated a cDNA clone encoding a precursor form of the diuretic hormone from the tobacco hornworm Manduca sexta (Mas-DH). Translation of the cDNA revealed a 138-amino acid precursor consisting of the Mas-DH amino acid sequence bounded by dibasic amino acid processing sites, a putative signal sequence, and additional peptide sequence on either side of the Mas-DH coding sequence. The region of the precursor upstream of the mature Mas-DH sequence shows limited (28%) homology to the cryptic region of the ovine corticotropin-releasing factor precursor. The Mas-DH RNA is 1.5-1.6 kilobases long; it is present in both the heads and bodies of adult and larval insects. In prewandering fifth stadium larvae, Mas-DH mRNA is expressed in brain, nerve cord, gut, and Malpighian tubules, but not in the fat body. There is a single genomic copy of the Mas-DH gene; the message is multiply spliced.Manduca sexta diuretic hormone (Mas-DH) is an amidated 41-amino acid peptide that was isolated from pharate adult tobacco hornworm heads on the basis of induction of fluid loss in beheaded adult cabbageworms (1). This peptide shows homology to a family of vertebrate neuropeptides, including sauvagine, corticotropin-releasing factor, and urotensin I (1). Since the isolation of Mas-DH, other peptides of related structure, which function in regulating fluid balance in insects, have been isolated from Manduca (2) and from two orthopteran genera: Locusta (3, 4) and Acheta (5). Mas-DH itself has been shown to induce water loss in both lepidopteran (1, 6) and orthopteran (7) species. The structural and biological properties of these related insect diuretic hormones have been reviewed recently (8).Due to the importance of Mas-DH and to the possibility of improving the utility for insect control of recombinant baculoviruses expressing this insect hormone (9), we have determined a precursor sequence for Mas-DH after isolation of a cDNA clone for the peptide.t In addition to the coding sequence for the mature diuretic hormone and a signal sequence, the precursor peptide encodes additional peptide sequences on either side of the coding region and is bounded by processing sites similar to processing sites extensively characterized in mammalian systems (10). Mas-DH is expressed in both heads and bodies of pharate adult and prewandering fifth stadium larvae; in these larval bodies, Mas-DH mRNA is observed in nerve cord, gut, and Malpighian tubules. The gene for the hormone appears to be present as a single copy in the M. sexta genome; multiple splicing events are required for mRNA assembly. MATERIALS AND METHODSDNA Synthesis and Sequencing. Degenerate oligonucleotides were purchased from Clontech. Nondegenerate oligonucleotides were synthesized by using an Applied Biosystems model 380A DNA synthesizer. Plasmid DNA was sequenced using the chain-termination method (11) and the Sequenase kit (United States Biochemical).Reverse Transcriptase-PCR. Two sets of degenerate oligonucleotides were used to reverse transcribe RNA for later amplificati...

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Isolation and identification of a diuretic hormone from the tobacco hornworm, Manduca sexta

Cited by 175 publications

References 31 publications

MOLECULAR EVOLUTION OF GPCRS: CRH/CRH receptors

MOLECULAR EVOLUTION OF GPCRS: CRH/CRH receptors

Molecular physiology of crustacean and insect neuropeptides

Characterization of the precursor for Manduca sexta diuretic hormone Mas-DH.

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