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Loss of angiotensin-converting enzyme-related (ACER) peptidase disrupts behavioural and metabolic responses to diet in Drosophila melanogaster

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Loss of angiotensin-converting enzyme-related (ACER) peptidase disrupts behavioural and metabolic responses to diet in Drosophila melanogaster. / Glover, Zoe; Hodges, Matthew David John; Dravecz, Nikolett et al.
In: Journal of Experimental Biology, Vol. 222, No. 8, 194332, 25.04.2019.

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Glover Z, Hodges MDJ, Dravecz N, Cameron J, Askwith H, Shirras AD et al. Loss of angiotensin-converting enzyme-related (ACER) peptidase disrupts behavioural and metabolic responses to diet in Drosophila melanogaster. Journal of Experimental Biology. 2019 Apr 25;222(8):194332. Epub 2019 Apr 2. doi: 10.1242/jeb.194332

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@article{02aff51b17f74155904971928ad30cfc,
title = "Loss of angiotensin-converting enzyme-related (ACER) peptidase disrupts behavioural and metabolic responses to diet in Drosophila melanogaster",
abstract = "Drosophila Acer (Angiotensin-converting enzyme-related) encodes a member of the angiotensin-converting enzyme (ACE) family of metallopeptidases that in mammals play roles in the endocrine regulation of blood homeostasis. ACE is also expressed in adipose tissue where it is thought to play a role in metabolic regulation. Drosophila Acer is expressed in the adult fat body of the head and abdomen and is secreted into the haemolymph. Acer null mutants have previously been found to have reduced night time sleep and greater sleep fragmentation. Acer may thus be part of a signalling system linking metabolism with sleep. To further understand the role of Acer in response to diet, we measured sleep and other nutrient-responsive phenotypes in Acer null flies under different dietary conditions. We show that loss of Acer disrupts the normal response of sleep to changes in nutrition. Other nutrient sensitive phenotypes, including survival and glycogen storage, were also altered in the Acer mutant but lipid storage was not. Although the physiological substrate of the Acer peptidase has not been identified, an alteration of the normal nutrient dependent control of Drosophila insulin-like peptide 5 protein in the Acer mutant suggests insulin/IGF-like signalling as a candidate pathway modulated by Acer in the nutrient-dependent control of sleep, survival and metabolism.",
keywords = "Drosophila, nutrition, sleep, Acer",
author = "Zoe Glover and Hodges, {Matthew David John} and Nikolett Dravecz and Jack Cameron and Helen Askwith and Shirras, {Alan Duncan} and Broughton, {Susan Jane}",
year = "2019",
month = apr,
day = "25",
doi = "10.1242/jeb.194332",
language = "English",
volume = "222",
journal = "Journal of Experimental Biology",
issn = "0022-0949",
publisher = "Company of Biologists Ltd",
number = "8",

}

RIS

TY - JOUR

T1 - Loss of angiotensin-converting enzyme-related (ACER) peptidase disrupts behavioural and metabolic responses to diet in Drosophila melanogaster

AU - Glover, Zoe

AU - Hodges, Matthew David John

AU - Dravecz, Nikolett

AU - Cameron, Jack

AU - Askwith, Helen

AU - Shirras, Alan Duncan

AU - Broughton, Susan Jane

PY - 2019/4/25

Y1 - 2019/4/25

N2 - Drosophila Acer (Angiotensin-converting enzyme-related) encodes a member of the angiotensin-converting enzyme (ACE) family of metallopeptidases that in mammals play roles in the endocrine regulation of blood homeostasis. ACE is also expressed in adipose tissue where it is thought to play a role in metabolic regulation. Drosophila Acer is expressed in the adult fat body of the head and abdomen and is secreted into the haemolymph. Acer null mutants have previously been found to have reduced night time sleep and greater sleep fragmentation. Acer may thus be part of a signalling system linking metabolism with sleep. To further understand the role of Acer in response to diet, we measured sleep and other nutrient-responsive phenotypes in Acer null flies under different dietary conditions. We show that loss of Acer disrupts the normal response of sleep to changes in nutrition. Other nutrient sensitive phenotypes, including survival and glycogen storage, were also altered in the Acer mutant but lipid storage was not. Although the physiological substrate of the Acer peptidase has not been identified, an alteration of the normal nutrient dependent control of Drosophila insulin-like peptide 5 protein in the Acer mutant suggests insulin/IGF-like signalling as a candidate pathway modulated by Acer in the nutrient-dependent control of sleep, survival and metabolism.

AB - Drosophila Acer (Angiotensin-converting enzyme-related) encodes a member of the angiotensin-converting enzyme (ACE) family of metallopeptidases that in mammals play roles in the endocrine regulation of blood homeostasis. ACE is also expressed in adipose tissue where it is thought to play a role in metabolic regulation. Drosophila Acer is expressed in the adult fat body of the head and abdomen and is secreted into the haemolymph. Acer null mutants have previously been found to have reduced night time sleep and greater sleep fragmentation. Acer may thus be part of a signalling system linking metabolism with sleep. To further understand the role of Acer in response to diet, we measured sleep and other nutrient-responsive phenotypes in Acer null flies under different dietary conditions. We show that loss of Acer disrupts the normal response of sleep to changes in nutrition. Other nutrient sensitive phenotypes, including survival and glycogen storage, were also altered in the Acer mutant but lipid storage was not. Although the physiological substrate of the Acer peptidase has not been identified, an alteration of the normal nutrient dependent control of Drosophila insulin-like peptide 5 protein in the Acer mutant suggests insulin/IGF-like signalling as a candidate pathway modulated by Acer in the nutrient-dependent control of sleep, survival and metabolism.

KW - Drosophila

KW - nutrition

KW - sleep

KW - Acer

U2 - 10.1242/jeb.194332

DO - 10.1242/jeb.194332

M3 - Journal article

VL - 222

JO - Journal of Experimental Biology

JF - Journal of Experimental Biology

SN - 0022-0949

IS - 8

M1 - 194332

ER -