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Evaluation of VGF peptides as potential anti-obesity candidates in pre-clinical animal models.

Authors :
Dalbøge LS
Jacobsen JM
Mehrotra S
Mercer AJ
Cox N
Liu F
Bennett CM
Said M
Tang-Christensen M
Raun K
Hansen JL
Grove KL
Baquero AF
Source :
Peptides [Peptides] 2021 Feb; Vol. 136, pp. 170444. Date of Electronic Publication: 2020 Nov 24.
Publication Year :
2021

Abstract

VGF is a peptide precursor expressed in neuroendocrine cells that is suggested to play a role in the regulation of energy homeostasis. VGF is proteolytically cleaved to yield multiple bioactive peptides. However, the specific actions of VGF-derived peptides on energy homeostasis remain unclear. The aim of the present work was to investigate the role of VGF-derived peptides in energy homeostasis and explore the pharmacological actions of VGF-derived peptides on body weight in preclinical animal models. VGF-derived peptides (NERP-1, NERP-2, PGH-NH <subscript>2</subscript> , PGH-OH, NERP-4, TLQP-21, TLQP-30, TLQP-62, HHPD-41, AQEE-30, and LQEQ-19) were synthesized and screened for their ability to affect neuronal activity in vitro on hypothalamic brain slices and modulate food intake and energy expenditure after acute central administration in vivo. In addition, the effects of NERP-1, NERP-2, PGH-NH <subscript>2</subscript> , TLQP-21, TLQP-62, and HHPD-41 on energy homeostasis were studied after chronic central infusion. NERP-1, PGH-NH <subscript>2</subscript> , HHPD-41, and TLQP-62 increased the functional activity of hypothalamic neuronal networks. However, none of the peptides altered energy homeostasis after either acute or chronic ICV administration. The present data do not support the potential use of the tested VGF-derived peptides as novel anti-obesity drug candidates.<br /> (Copyright © 2020 The Authors. Published by Elsevier Inc. All rights reserved.)

Details

Language :
English
ISSN :
1873-5169
Volume :
136
Database :
MEDLINE
Journal :
Peptides
Publication Type :
Academic Journal
Accession number :
33245952
Full Text :
https://doi.org/10.1016/j.peptides.2020.170444