Research output: Contribution to Journal/Magazine › Journal article › peer-review
Research output: Contribution to Journal/Magazine › Journal article › peer-review
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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 -