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Neuropeptidases and the metabolic inactivation of insect neuropeptides

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Neuropeptidases and the metabolic inactivation of insect neuropeptides. / Isaac, R. Elwyn; Bland, Nicholas D.; Shirras, Alan D.
In: General and Comparative Endocrinology, Vol. 162, No. 1, 15.05.2009, p. 8-17.

Research output: Contribution to Journal/MagazineJournal articlepeer-review

Harvard

Isaac, RE, Bland, ND & Shirras, AD 2009, 'Neuropeptidases and the metabolic inactivation of insect neuropeptides', General and Comparative Endocrinology, vol. 162, no. 1, pp. 8-17. https://doi.org/10.1016/j.ygcen.2008.12.011

APA

Isaac, R. E., Bland, N. D., & Shirras, A. D. (2009). Neuropeptidases and the metabolic inactivation of insect neuropeptides. General and Comparative Endocrinology, 162(1), 8-17. https://doi.org/10.1016/j.ygcen.2008.12.011

Vancouver

Isaac RE, Bland ND, Shirras AD. Neuropeptidases and the metabolic inactivation of insect neuropeptides. General and Comparative Endocrinology. 2009 May 15;162(1):8-17. doi: 10.1016/j.ygcen.2008.12.011

Author

Isaac, R. Elwyn ; Bland, Nicholas D. ; Shirras, Alan D. / Neuropeptidases and the metabolic inactivation of insect neuropeptides. In: General and Comparative Endocrinology. 2009 ; Vol. 162, No. 1. pp. 8-17.

Bibtex

@article{d8450558be924c839f429c28d2f4941c,
title = "Neuropeptidases and the metabolic inactivation of insect neuropeptides",
abstract = "Neuropeptidases play a key role in regulating neuropeptide signalling activity in the central nervous system of animals. They are oligopeptidases that are generally found on the surface of neuronal cells facing the synaptic and peri-synaptic space and therefore are ideally placed for the metabolic inactivation of neuropeptide transmitters/modulators. This review discusses the structure of insect neuropeptides in relation to their susceptibility to hydrolysis by peptidases and the need for specialist enzymes to degrade many neuropeptides. It focuses on five neuropeptidase families (neprilysin, dipeptidyl-peptidase IV, angiotensin-converting enzyme, aminopeptidase and dipeptidyl aminopeptidase III) that have been implicated in the metabolic inactivation of neuropeptides in the central nervous system of insects. Experimental evidence for the involvement of these peptidases in neuropeptide metabolism is reviewed and their properties are compared to similar neuropeptide inactivating peptidases of the mammalian brain. We also discuss how the sequencing of insect genomes has led to the molecular identification of candidate neuropeptidase genes. (C) 2008 Elsevier Inc. All rights reserved.",
keywords = "Neuropeptide metabolism, Neprilysin, Dipeptidyl-peptidase IV, Angiotensin-converting enzyme, Aminopeptidase, Dipeptidyl aminopeptidase III, ANGIOTENSIN-CONVERTING ENZYME, TACHYKININ-RELATED PEPTIDES, DIPEPTIDYL AMINOPEPTIDASE-III, LOCUST SCHISTOCERCA-GREGARIA, COCKROACH LEUCOPHAEA-MADERAE, DROSOPHILA-MELANOGASTER, PERIPLANETA-AMERICANA, DIPLOPTERA-PUNCTATA, CRYSTAL-STRUCTURE, MUSCA-DOMESTICA",
author = "Isaac, {R. Elwyn} and Bland, {Nicholas D.} and Shirras, {Alan D.}",
year = "2009",
month = may,
day = "15",
doi = "10.1016/j.ygcen.2008.12.011",
language = "English",
volume = "162",
pages = "8--17",
journal = "General and Comparative Endocrinology",
issn = "0016-6480",
publisher = "Academic Press Inc.",
number = "1",

}

RIS

TY - JOUR

T1 - Neuropeptidases and the metabolic inactivation of insect neuropeptides

AU - Isaac, R. Elwyn

AU - Bland, Nicholas D.

AU - Shirras, Alan D.

PY - 2009/5/15

Y1 - 2009/5/15

N2 - Neuropeptidases play a key role in regulating neuropeptide signalling activity in the central nervous system of animals. They are oligopeptidases that are generally found on the surface of neuronal cells facing the synaptic and peri-synaptic space and therefore are ideally placed for the metabolic inactivation of neuropeptide transmitters/modulators. This review discusses the structure of insect neuropeptides in relation to their susceptibility to hydrolysis by peptidases and the need for specialist enzymes to degrade many neuropeptides. It focuses on five neuropeptidase families (neprilysin, dipeptidyl-peptidase IV, angiotensin-converting enzyme, aminopeptidase and dipeptidyl aminopeptidase III) that have been implicated in the metabolic inactivation of neuropeptides in the central nervous system of insects. Experimental evidence for the involvement of these peptidases in neuropeptide metabolism is reviewed and their properties are compared to similar neuropeptide inactivating peptidases of the mammalian brain. We also discuss how the sequencing of insect genomes has led to the molecular identification of candidate neuropeptidase genes. (C) 2008 Elsevier Inc. All rights reserved.

AB - Neuropeptidases play a key role in regulating neuropeptide signalling activity in the central nervous system of animals. They are oligopeptidases that are generally found on the surface of neuronal cells facing the synaptic and peri-synaptic space and therefore are ideally placed for the metabolic inactivation of neuropeptide transmitters/modulators. This review discusses the structure of insect neuropeptides in relation to their susceptibility to hydrolysis by peptidases and the need for specialist enzymes to degrade many neuropeptides. It focuses on five neuropeptidase families (neprilysin, dipeptidyl-peptidase IV, angiotensin-converting enzyme, aminopeptidase and dipeptidyl aminopeptidase III) that have been implicated in the metabolic inactivation of neuropeptides in the central nervous system of insects. Experimental evidence for the involvement of these peptidases in neuropeptide metabolism is reviewed and their properties are compared to similar neuropeptide inactivating peptidases of the mammalian brain. We also discuss how the sequencing of insect genomes has led to the molecular identification of candidate neuropeptidase genes. (C) 2008 Elsevier Inc. All rights reserved.

KW - Neuropeptide metabolism

KW - Neprilysin

KW - Dipeptidyl-peptidase IV

KW - Angiotensin-converting enzyme

KW - Aminopeptidase

KW - Dipeptidyl aminopeptidase III

KW - ANGIOTENSIN-CONVERTING ENZYME

KW - TACHYKININ-RELATED PEPTIDES

KW - DIPEPTIDYL AMINOPEPTIDASE-III

KW - LOCUST SCHISTOCERCA-GREGARIA

KW - COCKROACH LEUCOPHAEA-MADERAE

KW - DROSOPHILA-MELANOGASTER

KW - PERIPLANETA-AMERICANA

KW - DIPLOPTERA-PUNCTATA

KW - CRYSTAL-STRUCTURE

KW - MUSCA-DOMESTICA

U2 - 10.1016/j.ygcen.2008.12.011

DO - 10.1016/j.ygcen.2008.12.011

M3 - Journal article

VL - 162

SP - 8

EP - 17

JO - General and Comparative Endocrinology

JF - General and Comparative Endocrinology

SN - 0016-6480

IS - 1

ER -