Neprilysin 4: an essential peptidase with multifaceted physiological relevance-Reference-Cited by-同舟云学术

Neprilysin 4: an essential peptidase with multifaceted physiological relevance

Published:2023-01-19 Issue:5 Volume:404 Page:513-520
ISSN:1431-6730
Container-title:Biological Chemistry
language:en
Short-container-title:

Author:

Buhr Annika¹,Schiemann Ronja¹,Meyer Heiko¹²^ORCID

Affiliation:

1. Department of Biology/Chemistry, Zoology and Developmental Biology Section , Osnabruck University , Barbarastrasse 11, D-49076 Osnabruck , Germany

2. Center for Cellular Nanoanalytics (CellNanOs) , Barbarastrasse 11, D-49076 Osnabruck , Germany

Abstract

Abstract Neprilysins are highly conserved ectoenzymes that hydrolyze and thus inactivate signaling peptides in the extracellular space. Herein, we focus on Neprilysin 4 from Drosophila melanogaster and evaluate the existing knowledge on the physiological relevance of the peptidase. Particular attention is paid to the role of the neprilysin in regulating feeding behavior and the expression of insulin-like peptides in the central nervous system. In addition, we assess the function of the peptidase in controlling the activity of the sarcoplasmic and endoplasmic reticulum Ca2+ ATPase in myocytes, as well as the underlying molecular mechanism in detail.

Funder

Deutsche Forschungsgemeinschaft

Publisher

Walter de Gruyter GmbH

Subject

Clinical Biochemistry,Molecular Biology,Biochemistry

Link

https://www.degruyter.com/document/doi/10.1515/hsz-2022-0286/pdf

Reference55 articles.

1. Abrol, N., Smolin, N., Armanious, G., Ceholski, D.K., Trieber, C.A., Young, H.S., and Robia, S.L. (2014). Phospholamban C-terminal residues are critical determinants of the structure and function of the calcium ATPase regulatory complex. J. Biol. Chem. 289: 25855–25866, https://doi.org/10.1074/jbc.m114.562579.

2. Anderson, D.M., Makarewich, C.A., Anderson, K.M., Shelton, J.M., Bezprozvannaya, S., Bassel-Duby, R., and Olson, E.N. (2016). Widespread control of calcium signaling by a family of SERCA-inhibiting micropeptides. Sci. Signal. 9: ra119, https://doi.org/10.1126/scisignal.aaj1460.

3. Bavishi, C., Messerli, F.H., Kadosh, B., Ruilope, L.M., and Kario, K. (2015). Role of neprilysin inhibitor combinations in hypertension: insights from hypertension and heart failure trials. Eur. Heart J. 36: 1967–1973, https://doi.org/10.1093/eurheartj/ehv142.

4. Bayes-Genis, A., Barallat, J., and Richards, A.M. (2016). A test in context: neprilysin: function, inhibition, and biomarker. J. Am. Coll. Cardiol. 68: 639–653, https://doi.org/10.1016/j.jacc.2016.04.060.

5. Bland, N.D., Pinney, J.W., Thomas, J.E., Turner, A.J., and Isaac, R.E. (2008). Bioinformatic analysis of the neprilysin (M13) family of peptidases reveals complex evolutionary and functional relationships. BMC Evol. Biol. 8: 16, https://doi.org/10.1186/1471-2148-8-16.

Cited by 3 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. A structure-based pharmacophore modelling approach to identify and design new neprilysin (NEP) inhibitors: An in silico-based investigation;Archives of Biochemistry and Biophysics;2024-06

2. Selenium Treatment Alleviates the Inhibition Caused by Nep-L Gene Knockdown in Silkworm (Bombyx mori);Biological Trace Element Research;2024-05-31

3. Highlight: on the past and the future of cellular microcompartments;Biological Chemistry;2023-03-24