NMS

Last update 08 May 2025

Basic Info

Synonyms

neuromedin S, Neuromedin-S, NMS

Introduction

Implicated in the regulation of circadian rhythms through autocrine and/or paracrine actions.

100 Clinical Results associated with NMS

100 Translational Medicine associated with NMS

0 Patents (Medical) associated with NMS

114

Literatures (Medical) associated with NMS

26 Mar 2025·The Journal of Neuroscience

Identification of a Novel Population of Neuromedin S Expressing Neurons in the Ventral Tegmental Area That Promote Morphine-Elicited Behavior

Article

Author: Huang, Xuefei ; Alday, Milagros ; Heller, Elizabeth A ; Mazei-Robison, Michelle S ; Rivera Quiles, Cristina ; Simmons, Sarah C ; Garrison, Amber ; Dodson, Olivia ; Caico, Samantha ; Camacho Fontánez, Nicole ; Hu, Qiwen ; Shafieichaharberoud, Fatemeh

Opioid use disorder constitutes a major health and economic burden, but our limited understanding of the underlying neurobiology impedes better interventions. Alteration in the activity and output of dopamine (DA) neurons in the ventral tegmental area (VTA) contributes to drug effects, but the mechanisms underlying these changes remain relatively unexplored. We used translating ribosome affinity purification (TRAP) and RNA sequencing to identify gene expression changes in mouse VTA DA neurons following chronic morphine exposure. We found that expression of the neuropeptide neuromedin S (NMS) is robustly increased in VTA DA neurons by morphine. Using an NMS-iCre driver line, we confirmed that a subset of VTA neurons express NMS and that chemogenetic modulation of VTA NMS neuron activity altered morphine responses in male and female mice. Specifically, VTA NMS neuronal activation promoted morphine locomotor activity while inhibition reduced morphine locomotor activity and conditioned place preference. Interestingly, these effects appear specific to morphine, as modulation of VTA NMS activity did not affect cocaine behaviors, consistent with our data that cocaine administration does not increase VTA Nms expression. Chemogenetic manipulation of VTA neurons that express glucagon-like peptide, a transcript also robustly increased in VTA DA neurons by morphine, does not alter morphine-elicited behavior, further highlighting the functional relevance of VTA NMS-expressing neurons. Together, our current data suggest that NMS-expressing neurons represent a novel subset of VTA neurons that may be functionally relevant for morphine responses and support the utility of cell-type–specific analyses like TRAP to identify neuronal adaptations underlying substance use disorder.

27 Jan 2025·JACS Au

Native Mass Spectrometry Captures the Conformational Plasticity of Proteins with Low-Complexity Domains

Article

Author: Brackmann, Klaus ; Marklund, Erik G. ; Leppert, Axel ; Lama, Dilraj ; Abramsson, Mia L. ; Deindl, Sebastian ; Rising, Anna ; Elofsson, Arne ; Stevens, Alexander ; Osterholz, Hannah ; Landreh, Michael

Disordered regions are an important functional feature of many multidomain proteins. A prime example is proteins in membraneless organelles, which contain folded domains that engage in specific interactions and disordered low-complexity (LC) domains that mediate liquid-liquid phase separation. Studying these complex architectures remains challenging due to their conformational variability. Native mass spectrometry (nMS) is routinely employed to analyze conformations and interactions of folded or disordered proteins; however, its ability to analyze proteins with disordered LC domains has not been investigated. Here, we analyze the ionization and conformational states of designed model proteins that recapitulate key features of proteins found in membraneless organelles. Our results show that charge state distributions (CSDs) in nMS reflect partial disorder regardless of the protein sequence, providing insights into their conformational plasticity and interactions. By applying the same CSD analysis to a spider silk protein fragment, we find that interactions between folded domains that trigger silk assembly simultaneously induce conformational changes in the LC domains. Lastly, using intact nucleosomes, we demonstrate that CSDs are a good predictor for the disorder content of complex native assemblies. We conclude that nMS reliably informs about the conformational landscape of proteins with LC domains, which is crucial for understanding protein condensates in cellular environments.

01 Jan 2025·Metabolic Engineering

Metabolic engineering of Escherichia coli for N-methylserotonin biosynthesis

Article

Author: Qi, Feng ; Wang, Yukun ; Li, Chenxi ; Lin, Shengyuan ; Huang, Jianzhong ; Yang, Qinghua ; Li, Qingchen ; Wang, Bingmei ; Zhong, Jie ; He, Wenjin

N-methylserotonin (NMS) is a valuable indole alkaloid with therapeutic potential for psychiatric and neurological disorders, and it is used in health foods, cosmetics, and weight loss supplements. However, environmental challenges and low reaction efficiencies significantly hinder cost-effective, large-scale production of NMS in plants or through chemical synthesis. Herein, we have successfully engineered Escherichia coli strains to enhance NMS production from L-tryptophan using whole-cell catalysis. We developed multiple biosynthesis pathways incorporating modules for serotonin (5-hydroxytryptamine, 5-HT), tetrahydromonapterin (MH₄), and S-adenosylmethionine (SAM) synthesis. To enhance MH₄ availability, we employed a high-activity Bacillus subtilis FolE and minimized carbon flux loss through targeted gene knockouts in competitive metabolic pathways, improving 5-HT production. Additionally, we constructed a comprehensive SAM biosynthesis module to facilitate transmethylation by a selected N-methyltransferase fused with ProS2. These engineered modules were coexpressed in two plasmids within the optimized strain NMS-19, producing 128.6 mg/L of NMS in a 5-L bioreactor using fed-batch cultivation-a 92-fold increase over the original strain. This study introduces a viable strategy for NMS production and provides insights into the biosynthesis of SAM-dependent methylated tryptamine derivatives.

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