ACSM3

Last update 08 May 2025

Basic Info

Synonyms

ACSM3, acyl-CoA synthetase medium chain family member 3, Acyl-CoA synthetase medium-chain family member 3

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Introduction

Catalyzes the activation of fatty acids by CoA to produce an acyl-CoA, the first step in fatty acid metabolism (PubMed:11772874). Capable of activating medium-chain fatty acids with a preference for isobutyrate among fatty acids with 2-6 carbon atoms (By similarity).

100 Clinical Results associated with ACSM3

100 Translational Medicine associated with ACSM3

0 Patents (Medical) associated with ACSM3

321

Literatures (Medical) associated with ACSM3

24 Apr 2025·Biochemical Journal

Dynamic interchange of local residue–residue interactions in the largely extended single alpha-helix in Drebrin

Article

Author: Péterfia, Bálint Ferenc ; Varga, Soma ; Farkas, Viktor ; Permi, Perttu ; Gáspári, Zoltán ; Dudola, Dániel ; Jeffries, Cy M.

Single alpha-helices (SAHs) are protein regions with unique mechanical properties, forming long, stable, monomeric helical structures in solution. To date, only a few naturally occurring SAH regions have been extensively characterized, primarily from myosins, leaving the structural and dynamic variability of SAH regions largely unexplored. Drebrin (developmentally regulated brain protein) contains a predicted SAH segment with unique sequence characteristics, including aromatic residues within the SAH region and a preference for arginine over lysine in its C-terminal half. Using circular dichroism (CD) and NMR spectroscopy, combined with small-angle X-ray scattering (SAXS) measurements, we demonstrate that the Drebrin-SAH is helical and monomeric in solution. NMR resonance assignment required specific 4D techniques to resolve severe signal overlap resulting from the low complexity and largely helical conformation of the sequence. To further characterize its structure, we generated a structural ensemble consistent with Cα, Cβ chemical shifts and SAXS data, revealing a primarily extended structure with non-uniform helicity. Our results suggest that dynamic rearrangement of salt bridges and potential transient cation-π interactions contribute to the formation and stabilization of both helical and non-helical local conformational states.

01 Mar 2025·Advanced Biology

ACSM3 Suppresses Ovarian Cancer Progression by Inactivating the IFN‐γ/JAK/STAT3 Signaling Pathway

Article

Author: Sun, Yanqiu ; Wang, Juan ; Wu, Ruixue

AbstractThis study aimed to investigate the role of Acyl‐CoA medium‐chain synthetase 3 (ACSM3) in ovarian cancer (OC) progression. ACSM3 expression in OC tissues and cells is detected by real‐time quantitative polymerase chain reaction, immunohistochemistry, or western blot. The influences of ACSM3 on OC progression are assessed in vitro and in vivo experiments. Gene set enrichment analysis is performed to find significantly enriched pathways related to ACSM3. In this study, ACSM3 expression in OC tissues and cells is downregulated. ACSM3 inhibited tumor growth in vivo. Knockdown of ACSM3 promoted cell proliferation, migration, and invasion, inhibited cell apoptosis, and activated JAK/STAT3 signaling pathway in SKOV3 cells, while overexpression of ACSM3 in A2780 cells led to the opposite results. Moreover, treatment with interferon‐gamma (IFN‐γ) in A2780 cells reversed the effects of ACSM3 on cell proliferation, migration, invasion, and apoptosis, but IFN‐γ further enhanced the effects of ACSM3 knockdown on SKOV3 cell proliferation, migration, invasion, and apoptosis. In conclusion, ACSM3 inhibited OC cell proliferation, migration, and invasion, and promoted cell apoptosis by suppressing the IFN‐γ/JAK/STAT3 signaling pathway, which might provide a promising therapeutic target for OC treatment.

01 Feb 2025·Journal of Pharmaceutical and Biomedical Analysis

Proteomics exploration of metformin hydrochloride for diabetic kidney disease treatment via the butanoate metabolism pathway

Article

Author: Qiu, Shi ; Wang, Xian ; Cai, Ying ; Zhang, Aihua ; Guo, Sifan ; Chen, Hongwei ; Wang, Yan ; Chai, Jinxuan ; Wang, Zhibo ; Xie, Dandan ; Wang, Shiwei ; Hu, Zhencai

Diabetic nephropathy (DKD) is a diabetesrelated kidney injury with an increasing incidence every year. Metformin hydrochloride (MET), a cornerstone treatment for glucose lowering, has been widely reported for the treatment of DKD, but the specific molecular mechanisms and potential therapeutic targets still need to be further explored. We used kidney tissues from db/db mice as samples and used proteomics and bioinformatics to analyse the function, distribution and related pathways of differential proteins in DKD, focusing on the assessment of the binding energies of key proteins in the butyrate pathway and drugs at the molecular level, which showed that the expression profiles of differential proteins in kidney tissues were altered after MET treatment, involving energy metabolism. The key proteins involved in the butanoate metabolism pathway, including AACS, ACSM3, EHHADH and HMGCS2, exhibit binding energies to MET of ＜-5 kcal. It is therefore plausible that MET treatment may affect the butanoate metabolism pathway, potentially ameliorating the progression of DKD by modulating mitochondrial function and inflammatory responses.

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ACSM3

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