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Last update 08 May 2025

ACTG2

Last update 08 May 2025

Basic Info

Synonyms

ACTA3, ACTG2, actin gamma 2, smooth muscle

+ [7]

Introduction

Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.

Drugs associated with ACTG2

Taget ACTG2 siRNA(Dante Genomics)

Target

ACTG2

Mechanism

ACTG2 inhibitors

Active Org.

Dante Labs, Inc.

Originator Org.

Dante Labs, Inc.

Active Indication

Megacystis Microcolon Intestinal Hypoperistalsis Syndrome

Inactive Indication-

Drug Highest PhasePreclinical

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with ACTG2

100 Translational Medicine associated with ACTG2

0 Patents (Medical) associated with ACTG2

195

Literatures (Medical) associated with ACTG2

01 Jun 2025·Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease

Overexpression of LMOD1 induces oxidative stress and enhances cell apoptosis of melanoma through the RIG-I like receptor pathway

Article

Author: Lei, Hua ; Wan, Huiying ; Huang, Linxue ; Chen, Mingyi

BACKGROUNDOxidative stress is crucial in the development of cutaneous melanoma, but its role in melanoma is controversial. We aimed to identify melanoma-associated targets and understand the underlying mechanism.METHODSDifferential expressed genes (DEGs) were discovered between control and melanoma samples, and a protein-protein interaction (PPI) network was constructed to find key genes. The prediction accuracy of LMOD1 was assessed by receiver operating characteristic (ROC) curves, and pan-cancer analysis was also performed for LMOD1 expression and immune characteristics. The downstream pathway of LMOD1 was found via KEGG analysis. The effects of LMOD1 on oxidative stress, apoptosis, CD4 + T cells and the downstream pathway were evaluated in melanoma cells and mice.RESULTSWe identified ACTG2, CNN1, LMOD1, MYH11, MYL9, MYLK, TAGLN, TPM1 and TPM2 as melanoma-related DEGs, which could separate control and melanoma samples. The area under curve (AUC) of LMOD1 was > 0.89, indicating high prediction accuracy. LMOD1 expression was decreased in melanoma, and LMOD1 notably correlated with B cells, CD4 T cells, neutrophils, macrophages and dendritic cells (DCs). Overexpression of LMOD1 promoted apoptosis, enhanced migration and invasion, and activated oxidative stress in melanoma cells. LMOD1 promoted apoptosis via activating oxidative stress. The RIG-I-like receptor signaling (RLR) was a downstream pathway of LMOD1. Overexpression of LMOD1 activated oxidative stress, increased apoptosis and CD4 + T cells, and elevated RIG-I and MDA5, while Cyclo (Phe-Pro) (cFP) reversed the results.CONCLUSIONLMOD1 triggers oxidative stress-mediated apoptosis in melanoma via activating the RLR pathway, which provides promising targets and regulatory pathway for melanoma.

01 Apr 2025·Journal of Biological Chemistry

Declining activity of serum response factor in aging aorta in relation to aneurysm progression

Article

Author: Bastrup, Joakim Armstrong ; Swärd, Karl ; Holmberg, Johan ; Arévalo Martinez, Marycarmen ; Kawka, Katarzyna ; Rippe, Catarina ; Jepps, Thomas A ; Albinsson, Sebastian

Age is a critical determinant of arterial disease, including aneurysm formation. Here, to understand the impact of aging on the arterial transcriptome, we leveraged RNA-sequencing data to define transcripts that change with advancing age in human arteries. Among the most repressed transcripts in aged individuals were those that are relevant for actomyosin structure and organization, including both myosin light chain kinase (MYLK) and smooth muscle γ-actin (ACTG2). This was associated with a reduction of serum response factor (SRF), which controls these transcripts via defined promoter elements. To determine the consequences of isolated Srf depletion, we conditionally deleted Srf in vascular smooth muscle of young mice (i8-SRF-KO mice). This led to a reduction of the SRF regulon, including Mylk and Actg2, and impaired arterial contractility, but left endothelial-dependent dilatation unaffected. Srf-depletion also increased aortic diameter and Alcian blue staining of the aortic media, which are cardinal features of aortopathy, such as aortic aneurysmal disease. Despite this, i8-SRF-KO mice were protected from aortic lesions elicited by angiotensin II (AngII). Proteomics demonstrated that Srf-depletion mimicked a protein signature of AngII treatment involving increases of the mechanoresponsive transcriptional coactivators YAP and TAZ and reduction of the Hippo kinase Lats2. Protection from aortopathy could be overcome by changing the order of KO induction and AngII administration resulting in advanced aneurysms in both i8-SRF-KO and control mice. Our work provides important insights into the molecular underpinnings of age-dependent changes in aortic function and mechanisms of adaptation in hypertension.

01 Jan 2025·Computational and Structural Biotechnology Journal

Dynamical features of smooth muscle actin pathological mutants: The arginine-257(258)-Cysteine cases

Article

Author: de Rosa, M ; Cavalli, A ; Chiappori, F ; Viti, F ; Palma, F Di

The R257(8)C mutation in smooth muscle actins, ACTG2 and ACTA2, is the most frequent cause of severe genetic diseases: namely, visceral myopathy, and familial thoracic aortic aneurysms and dissections, which respectively, stem from impairment of the visceral and vascular muscle. The molecular mechanisms underlying such pathologies are not fully elucidated. In the absence of experimental data of WT and mutated actins in their monomeric (g-) and filamentous (f-) form, molecular dynamics can shed light on the role of the R257(8)C in protein structure and dynamics. Analysis of g-actins does not show significant differences between WT and mutated proteins suggesting the correct monomers folding. On the contrary, mutated filaments are destabilized. Subunits of R257C f-ACTG2 adopt non optimal angles and in R258C f-ACTA2 we observe depolymerization already in the simulated time frame. Overall, our data points to a crucial role of residue R257(8) in actin structure and dynamics, in particular when the protein assembles into the filament.

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ACTG2

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