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prmt1 (Cell Signaling Technology Inc)

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10-week combined exercise preconditioning prevented 1-week hindlimb immobilization-induced muscle atrophy in mice. (A–C) Body weight, gross weight gain and food intake data during 10-week exercise preconditioning. ∗ p < 0.05 vs. C; # p < 0.05 vs. E. Two-way ANOVA was used and data are shown as means ± standard error of the mean ( SEM ) (C, n = 16, E, n = 8, E+5003, n = 8). (D) Food intake data during 1-week immobilization. ∗ p < 0.05 vs. C. Two-way ANOVA was used and data are shown as means ± SEM . (E–F) aDMA level indicated for <t>Prmt1</t> enzymatic activity after 10-week TC-E−5003 administration via subcutaneous injection at a dose of 2 mg/kg body weight, once daily, 5 days a week. (G–J) Skeletal muscle functions tests, G, grip strength, H, suspension time of hang test, I, time of the latency to fall in rotarod test, J, maximum voluntary climbing capacity (MVCC) test. (K–P) Total hindlimb mass and specific muscle mass of various parts of hindlimb, GAS, gastrocnemius, SOL, soleus, QUA, quadriceps femoris, lateralis, TA, tibialis anterior, EDL, extensor digitorum longus. H-S, ∗ p < 0.05 vs. C; ∗∗ p < 0.01 vs. C; # p < 0.05 vs. Im; ## p < 0.01 vs. Im; $ p < 0.05 vs. E + Im; $$ p < 0.01 vs. E + Im. Two-way ANOVA was used and data are shown as means ± SEM (C, n = 8, Im, n = 8, E + Im, n = 8, E+5003+Im, n = 8).

Prmt1, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/prmt1/pmc12926326-78-165-169?v=Cell+Signaling+Technology+Inc
Average 86 stars, based on 1 article reviews

prmt1 - by Bioz Stars, 2026-07

86/100 stars

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1) Product Images from "Exercise preconditioning prevents immobilization-induced skeletal muscle atrophy by activating Prmt1-p38/ATF2-Sesn1 signaling axis in C57BL/6J mice"

Article Title: Exercise preconditioning prevents immobilization-induced skeletal muscle atrophy by activating Prmt1-p38/ATF2-Sesn1 signaling axis in C57BL/6J mice

Journal: Sports Medicine and Health Science

doi: 10.1016/j.smhs.2025.04.001

Figure Legend Snippet: 10-week combined exercise preconditioning prevented 1-week hindlimb immobilization-induced muscle atrophy in mice. (A–C) Body weight, gross weight gain and food intake data during 10-week exercise preconditioning. ∗ p < 0.05 vs. C; # p < 0.05 vs. E. Two-way ANOVA was used and data are shown as means ± standard error of the mean ( SEM ) (C, n = 16, E, n = 8, E+5003, n = 8). (D) Food intake data during 1-week immobilization. ∗ p < 0.05 vs. C. Two-way ANOVA was used and data are shown as means ± SEM . (E–F) aDMA level indicated for Prmt1 enzymatic activity after 10-week TC-E−5003 administration via subcutaneous injection at a dose of 2 mg/kg body weight, once daily, 5 days a week. (G–J) Skeletal muscle functions tests, G, grip strength, H, suspension time of hang test, I, time of the latency to fall in rotarod test, J, maximum voluntary climbing capacity (MVCC) test. (K–P) Total hindlimb mass and specific muscle mass of various parts of hindlimb, GAS, gastrocnemius, SOL, soleus, QUA, quadriceps femoris, lateralis, TA, tibialis anterior, EDL, extensor digitorum longus. H-S, ∗ p < 0.05 vs. C; ∗∗ p < 0.01 vs. C; # p < 0.05 vs. Im; ## p < 0.01 vs. Im; $ p < 0.05 vs. E + Im; $$ p < 0.01 vs. E + Im. Two-way ANOVA was used and data are shown as means ± SEM (C, n = 8, Im, n = 8, E + Im, n = 8, E+5003+Im, n = 8).

Techniques Used: Activity Assay, Injection, Suspension

10-week combined exercise preconditioning ameliorated 1-week hindlimb immobilization-induced imbalance between synthesis and degradation of protein in skeletal muscle. (A) Representative images of hematoxylin and eosin staining (H&E) of GAS muscle cross-sections. Scale bar = 50 μm. (B) The average CSA of GAS muscle was quantified. (C–D) Real-time PCR results of TIRM63 (MuRF1), FBXO32 (Atrogin-1), Prmt1, and Sesn1 in GAS muscle. (E–N) Western blot results of Prmt1, Sesn1, p-FoxO3a, FoxO3a, Atrogin-1, MuRF1, IGF-1, pAkt-S473, Akt, mTOR, Raptor in GAS muscle. B-N, ∗ p < 0.05 vs. C; ∗∗ p < 0.01 vs. C; # p < 0.05 vs. Im; ## p < 0.01 vs. Im; $ p < 0.05 vs. E + Im; $$ p < 0.01 vs. E + Im. Two-way ANOVA was used and data are shown as means ± standard error of the mean (C, n = 8, Im, n = 8, E + Im, n = 8, E+5003+Im, n = 8).

Figure Legend Snippet: 10-week combined exercise preconditioning ameliorated 1-week hindlimb immobilization-induced imbalance between synthesis and degradation of protein in skeletal muscle. (A) Representative images of hematoxylin and eosin staining (H&E) of GAS muscle cross-sections. Scale bar = 50 μm. (B) The average CSA of GAS muscle was quantified. (C–D) Real-time PCR results of TIRM63 (MuRF1), FBXO32 (Atrogin-1), Prmt1, and Sesn1 in GAS muscle. (E–N) Western blot results of Prmt1, Sesn1, p-FoxO3a, FoxO3a, Atrogin-1, MuRF1, IGF-1, pAkt-S473, Akt, mTOR, Raptor in GAS muscle. B-N, ∗ p < 0.05 vs. C; ∗∗ p < 0.01 vs. C; # p < 0.05 vs. Im; ## p < 0.01 vs. Im; $ p < 0.05 vs. E + Im; $$ p < 0.01 vs. E + Im. Two-way ANOVA was used and data are shown as means ± standard error of the mean (C, n = 8, Im, n = 8, E + Im, n = 8, E+5003+Im, n = 8).

Techniques Used: Staining, Real-time Polymerase Chain Reaction, Western Blot

Exercise preconditioning increased Sestrin1 (Sesn1) expression by activating protein arginine methyltransferase 1 (Prmt1)-p38/activating transcription factor 2 (ATF2) signaling in mice. (A) ChIP analysis of Prmt1 binding to the ATF2 sequence of mouse Sesn1 promoter in GAS muscle. (B–D) Western blot results of p-p38-T180/182, p38, and ATF2 in GAS muscle. (E–F) Co-IP results, IP: Prmt1, GAS muscle was used. (G–H) Co-IP results, IP: ATF2, GAS muscle was used. (I–J) Co-IP results, IP: p38, GAS muscle was used. A-J, ∗ p < 0.05 vs. C; ∗∗ p < 0.01 vs. C; # p < 0.05 vs. Im; ## p < 0.01 vs. Im; $ p < 0.05 vs. E + Im; $$ p < 0.01 vs. E + Im. Two-way ANOVA was used and data are shown as means ± standard error of the mean (C, n = 8, Im, n = 8, E + Im, n = 8, E+5003+Im, n = 8).

Figure Legend Snippet: Exercise preconditioning increased Sestrin1 (Sesn1) expression by activating protein arginine methyltransferase 1 (Prmt1)-p38/activating transcription factor 2 (ATF2) signaling in mice. (A) ChIP analysis of Prmt1 binding to the ATF2 sequence of mouse Sesn1 promoter in GAS muscle. (B–D) Western blot results of p-p38-T180/182, p38, and ATF2 in GAS muscle. (E–F) Co-IP results, IP: Prmt1, GAS muscle was used. (G–H) Co-IP results, IP: ATF2, GAS muscle was used. (I–J) Co-IP results, IP: p38, GAS muscle was used. A-J, ∗ p < 0.05 vs. C; ∗∗ p < 0.01 vs. C; # p < 0.05 vs. Im; ## p < 0.01 vs. Im; $ p < 0.05 vs. E + Im; $$ p < 0.01 vs. E + Im. Two-way ANOVA was used and data are shown as means ± standard error of the mean (C, n = 8, Im, n = 8, E + Im, n = 8, E+5003+Im, n = 8).

Techniques Used: Expressing, Binding Assay, Sequencing, Western Blot, Co-Immunoprecipitation Assay

Protein arginine methyltransferase 1 (Prmt1)-Sestrin1 (Sesn1) coordinated the differentiation of C2C12 myoblasts into mature myotubes. (A–B) H&E staining of C2C12 myotubes at the 7 th day of differentiation with si-Sesn, and Ad-Sesn1 treatment. Scale bar = 100 μm. (C–D) Western blot results of Sesn1, FoxO3a, Atrogin-1 and MuRF1 in C2C12. A-D, C, control, si-Sesn1, si-RNA of Sesn1, Ad-Sesn1, Adenoviruses overexpressing Sesn1, ∗ p < 0.05 vs. C; ∗∗ p < 0.01 vs. C; # p < 0.05 vs. si-Sesn1; ## p < 0.01 vs. Si-Sesn1. Two-way ANOVA was used and data are shown as means ± standard error of the mean ( SEM ) ( n = 6 in each group). (E–F) H&E staining of C2C12 myotubes at the 7 th day of differentiation with si-Prmt1, and Ad-Prmt1. Scale bar = 100 μm. (G–N) Western blot results of Prmt1, p-p38-T180/182, p38, ATF2, Sesn1, FoxO3a, Atrogin-1 and MuRF1 in C2C12. E-N, C, control, si-Prmt1, si-RNA of Prmt1, Ad-Prmt1, Adenoviruses overexpressing Prmt1, ∗ p < 0.05 vs. C; ∗∗ p < 0.01 vs. C; # p < 0.05 vs. si-Prmt1; ## p < 0.01 vs. si-Prmt1. Two-way ANOVA was used and data are shown as means ± SEM ( n = 3 in each group). (O–R) Western blot results of Prmt1, ATF2 and Sesn1 in C2C12 myoblasts, ∗ p < 0.05; ∗∗ p < 0.01, unpaired Student's t -test was used and data are shown as means ± SEM ( n = 6 in each group). (S–W) Western blot results of Prmt1, FoxO3a, Atrogin-1 and MuRF1 in C2C12 myoblasts, ∗ p < 0.05; ∗∗ p < 0.01, unpaired Student's t -test was used and data are shown as means ± SEM ( n = 6 in each group).

Figure Legend Snippet: Protein arginine methyltransferase 1 (Prmt1)-Sestrin1 (Sesn1) coordinated the differentiation of C2C12 myoblasts into mature myotubes. (A–B) H&E staining of C2C12 myotubes at the 7 th day of differentiation with si-Sesn, and Ad-Sesn1 treatment. Scale bar = 100 μm. (C–D) Western blot results of Sesn1, FoxO3a, Atrogin-1 and MuRF1 in C2C12. A-D, C, control, si-Sesn1, si-RNA of Sesn1, Ad-Sesn1, Adenoviruses overexpressing Sesn1, ∗ p < 0.05 vs. C; ∗∗ p < 0.01 vs. C; # p < 0.05 vs. si-Sesn1; ## p < 0.01 vs. Si-Sesn1. Two-way ANOVA was used and data are shown as means ± standard error of the mean ( SEM ) ( n = 6 in each group). (E–F) H&E staining of C2C12 myotubes at the 7 th day of differentiation with si-Prmt1, and Ad-Prmt1. Scale bar = 100 μm. (G–N) Western blot results of Prmt1, p-p38-T180/182, p38, ATF2, Sesn1, FoxO3a, Atrogin-1 and MuRF1 in C2C12. E-N, C, control, si-Prmt1, si-RNA of Prmt1, Ad-Prmt1, Adenoviruses overexpressing Prmt1, ∗ p < 0.05 vs. C; ∗∗ p < 0.01 vs. C; # p < 0.05 vs. si-Prmt1; ## p < 0.01 vs. si-Prmt1. Two-way ANOVA was used and data are shown as means ± SEM ( n = 3 in each group). (O–R) Western blot results of Prmt1, ATF2 and Sesn1 in C2C12 myoblasts, ∗ p < 0.05; ∗∗ p < 0.01, unpaired Student's t -test was used and data are shown as means ± SEM ( n = 6 in each group). (S–W) Western blot results of Prmt1, FoxO3a, Atrogin-1 and MuRF1 in C2C12 myoblasts, ∗ p < 0.05; ∗∗ p < 0.01, unpaired Student's t -test was used and data are shown as means ± SEM ( n = 6 in each group).

Techniques Used: Staining, Western Blot, Control

Exercise preconditioning activated AMP-Activated protein kinase α2 (AMPKα2)-transcriptional co-activator PPAR-γ co-activator-1 α (PGC-1α) through protein arginine methyltransferase 1 (Prmt1)-Sestrin1 (Sesn1) in immobilized mice. (A–C) Western blot results of p-AMPKα2, AMPKα2, and PGC-1α in GAS muscle. (D–E) Co-IP results, IP: Prmt1, GAS muscle was used. (F–G) Co-IP results, IP: PGC-1α, GAS muscle was used. (H–I) Co-IP results, IP: Sesn1, GAS muscle was used. (J–K) Co-IP results, IP: PGC-1α, GAS muscle was used. (L–M) Co-IP results, IP: AMPKα2, GAS muscle was used. A-M, ∗ p < 0.05 vs. C; ∗∗ p < 0.01 vs. C; # p < 0.05 vs. Im; ## p < 0.01 vs. Im; $ p < 0.05 vs. E + Im; $$ p < 0.01 vs. E + Im. Two-way ANOVA was used and data are shown as means ± standard error of the mean (C, n = 8, Im, n = 8, E + Im, n = 8, E+5003+Im, n = 8).

Figure Legend Snippet: Exercise preconditioning activated AMP-Activated protein kinase α2 (AMPKα2)-transcriptional co-activator PPAR-γ co-activator-1 α (PGC-1α) through protein arginine methyltransferase 1 (Prmt1)-Sestrin1 (Sesn1) in immobilized mice. (A–C) Western blot results of p-AMPKα2, AMPKα2, and PGC-1α in GAS muscle. (D–E) Co-IP results, IP: Prmt1, GAS muscle was used. (F–G) Co-IP results, IP: PGC-1α, GAS muscle was used. (H–I) Co-IP results, IP: Sesn1, GAS muscle was used. (J–K) Co-IP results, IP: PGC-1α, GAS muscle was used. (L–M) Co-IP results, IP: AMPKα2, GAS muscle was used. A-M, ∗ p < 0.05 vs. C; ∗∗ p < 0.01 vs. C; # p < 0.05 vs. Im; ## p < 0.01 vs. Im; $ p < 0.05 vs. E + Im; $$ p < 0.01 vs. E + Im. Two-way ANOVA was used and data are shown as means ± standard error of the mean (C, n = 8, Im, n = 8, E + Im, n = 8, E+5003+Im, n = 8).

Techniques Used: Western Blot, Co-Immunoprecipitation Assay

Exercise preconditioning prevented muscle atrophy through protein arginine methyltransferase 1 (Prmt1)-Sestrin1 (Sesn1)-transcriptional co-activator PPAR-γ co-activator-1 α (PGC-1α)-mediated skeletal muscle regeneration. (A–B) Western blot results of MyoD, Myf5, MEF2 and MyoG in GAS muscle. (C–D) Co-IP results, IP: MyoD, GAS muscle was used. A-B, ∗ p < 0.05 vs. C; ∗∗ p < 0.01 vs. C; ## p < 0.01 vs. Im; $ p < 0.05 vs. E + Im; $$ p < 0.01 vs. E + Im. Two-way ANOVA was used, and data are shown as means ± standard error of the mean ( SEM ) (C, n = 8, Im, n = 8, E + Im, n = 8, E+5003+Im, n = 8). (E–F) H&E staining of myotubes at each differentiation time points of C2C12 myoblasts overexpressing Sesn1. Scale bar = 100 μm ∗ p < 0.05 vs. Ad-Sesn1-, unpaired Student's t-test was used and data are shown as means ± SEM ( n = 3 in each group). (G–H) Western blot results of Sesn1, Prmt1, PGC-1α, MyoD, MEF2, Myf5, and MyoG in C2C12 myoblasts at each time points of differentiation. ∗ p < 0.05 vs. D0, unpaired Student's t -test was used and data are shown as means ± SEM ( n = 6 in each group). (I–J) Western blot results of PGC-1α in nucleus of C2C12 myoblasts overexpressing Sesn1 at each time points of differentiation. ∗∗ p < 0.01 vs. Ad-Sesn1, unpaired Student's t -test was used and data are shown as means ± SEM ( n = 6 in each group). (K–L) Western blot results of PGC-1α in cytoplasm of C2C12 myoblasts overexpressing Sesn1 at each time points of differentiation. ∗∗ p < 0.01 vs. Ad-Sesn1-, unpaired Student's t -test was used and data are shown as means ± SEM ( n = 6 in each group).

Figure Legend Snippet: Exercise preconditioning prevented muscle atrophy through protein arginine methyltransferase 1 (Prmt1)-Sestrin1 (Sesn1)-transcriptional co-activator PPAR-γ co-activator-1 α (PGC-1α)-mediated skeletal muscle regeneration. (A–B) Western blot results of MyoD, Myf5, MEF2 and MyoG in GAS muscle. (C–D) Co-IP results, IP: MyoD, GAS muscle was used. A-B, ∗ p < 0.05 vs. C; ∗∗ p < 0.01 vs. C; ## p < 0.01 vs. Im; $ p < 0.05 vs. E + Im; $$ p < 0.01 vs. E + Im. Two-way ANOVA was used, and data are shown as means ± standard error of the mean ( SEM ) (C, n = 8, Im, n = 8, E + Im, n = 8, E+5003+Im, n = 8). (E–F) H&E staining of myotubes at each differentiation time points of C2C12 myoblasts overexpressing Sesn1. Scale bar = 100 μm ∗ p < 0.05 vs. Ad-Sesn1-, unpaired Student's t-test was used and data are shown as means ± SEM ( n = 3 in each group). (G–H) Western blot results of Sesn1, Prmt1, PGC-1α, MyoD, MEF2, Myf5, and MyoG in C2C12 myoblasts at each time points of differentiation. ∗ p < 0.05 vs. D0, unpaired Student's t -test was used and data are shown as means ± SEM ( n = 6 in each group). (I–J) Western blot results of PGC-1α in nucleus of C2C12 myoblasts overexpressing Sesn1 at each time points of differentiation. ∗∗ p < 0.01 vs. Ad-Sesn1, unpaired Student's t -test was used and data are shown as means ± SEM ( n = 6 in each group). (K–L) Western blot results of PGC-1α in cytoplasm of C2C12 myoblasts overexpressing Sesn1 at each time points of differentiation. ∗∗ p < 0.01 vs. Ad-Sesn1-, unpaired Student's t -test was used and data are shown as means ± SEM ( n = 6 in each group).

Techniques Used: Western Blot, Co-Immunoprecipitation Assay, Staining

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15 , 16 , 17 ) to molecular definition of protein arginine methyltransferases (PRMTs) ( 18 , 19 ). Early mechanistic studies demonstrated that arginine methylation regulates protein–protein interactions ( 20 ) and chromatin function through histone methylation by CARM1/PRMT4, PRMT1, and PRMT5 ( 21 , 22 , 23 ), while PRMT7 is unique in only catalyzing monomethylation ( 24 , 25 ). Tool development of specific antibodies ( 26 , 27 ) and inhibitors helped advance the field. The identification of methylarginine reader proteins, including SMN and TDRD3, and the structural definition of Tudor domain recognition established principles of methylarginine-dependent signaling ( 28 , 29 , 30 , 31 , 32 , 33 ). Translational advances include the development of selective PRMT5 inhibitors ( 34 , 35 ) and the discovery that MTAP loss leads to accumulation of methylthioadenosine (MTA), creating a synthetic lethal vulnerability to PRMT5 inhibition ( 36 , 37 , 38 ). More recent discoveries expanded methylarginine reader biology beyond Tudor domains, including SART3 ( 39 ) and established MTA-cooperative PRMT5 inhibitors that exploit tumor metabolic state for selective targeting ( 40 , 41 ). Colored boxes denote conceptual categories: enzyme discovery, biochemistry, and biology (green); methylarginine readers and mechanisms (purple); and therapeutic development (orange). B , Biochemical reactions catalyzed by PRMTs. Type I, II, and III PRMTs catalyze processive methylation of arginine residues using S-adenosylmethionine (SAM) as a methyl donor, generating monomethylarginine (MMA/Rme1), asymmetric dimethylarginine (ADMA/Rme2a), or symmetric dimethylarginine (SDMA/Rme2s), with S-adenosylhomocysteine (SAH) as a byproduct. PRMT family members are classified by product specificity: Type I catalyzing MMA and ADMA (PRMT1, 2, 3, 4, 6, and 8), Type II catalyzing MMA and SDMA (PRMT5 and 9), and Type III only catalyzing MMA (PRMT7). " width="250" height="auto" />
Protein Arginine Methyltransferase 1, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Image Search Results

Journal: The Journal of Biological Chemistry

Article Title: Meeting report on FASEB protein arginine methylation: mechanism to therapeutics

doi: 10.1016/j.jbc.2026.111448

Figure Lengend Snippet: Protein arginine methylation from biochemical discovery to therapeutic targeting. A , Timeline of key advances in arginine methylation biology, highlighting the progression from early biochemical identification of methylarginine and methyltransferase activity ( 15 , 16 , 17 ) to molecular definition of protein arginine methyltransferases (PRMTs) ( 18 , 19 ). Early mechanistic studies demonstrated that arginine methylation regulates protein–protein interactions ( 20 ) and chromatin function through histone methylation by CARM1/PRMT4, PRMT1, and PRMT5 ( 21 , 22 , 23 ), while PRMT7 is unique in only catalyzing monomethylation ( 24 , 25 ). Tool development of specific antibodies ( 26 , 27 ) and inhibitors helped advance the field. The identification of methylarginine reader proteins, including SMN and TDRD3, and the structural definition of Tudor domain recognition established principles of methylarginine-dependent signaling ( 28 , 29 , 30 , 31 , 32 , 33 ). Translational advances include the development of selective PRMT5 inhibitors ( 34 , 35 ) and the discovery that MTAP loss leads to accumulation of methylthioadenosine (MTA), creating a synthetic lethal vulnerability to PRMT5 inhibition ( 36 , 37 , 38 ). More recent discoveries expanded methylarginine reader biology beyond Tudor domains, including SART3 ( 39 ) and established MTA-cooperative PRMT5 inhibitors that exploit tumor metabolic state for selective targeting ( 40 , 41 ). Colored boxes denote conceptual categories: enzyme discovery, biochemistry, and biology (green); methylarginine readers and mechanisms (purple); and therapeutic development (orange). B , Biochemical reactions catalyzed by PRMTs. Type I, II, and III PRMTs catalyze processive methylation of arginine residues using S-adenosylmethionine (SAM) as a methyl donor, generating monomethylarginine (MMA/Rme1), asymmetric dimethylarginine (ADMA/Rme2a), or symmetric dimethylarginine (SDMA/Rme2s), with S-adenosylhomocysteine (SAH) as a byproduct. PRMT family members are classified by product specificity: Type I catalyzing MMA and ADMA (PRMT1, 2, 3, 4, 6, and 8), Type II catalyzing MMA and SDMA (PRMT5 and 9), and Type III only catalyzing MMA (PRMT7).

Article Snippet: In addition, Misuzu Hashimoto linked PRMT1 to CNS development and presented a model in which PRMT1 coordinates cell-type specific pathways critical for brain maturation.

Techniques: Methylation, Activity Assay, Protein-Protein interactions, Inhibition

Journal: Sports Medicine and Health Science

Article Title: Exercise preconditioning prevents immobilization-induced skeletal muscle atrophy by activating Prmt1-p38/ATF2-Sesn1 signaling axis in C57BL/6J mice

doi: 10.1016/j.smhs.2025.04.001

Figure Lengend Snippet: 10-week combined exercise preconditioning prevented 1-week hindlimb immobilization-induced muscle atrophy in mice. (A–C) Body weight, gross weight gain and food intake data during 10-week exercise preconditioning. ∗ p < 0.05 vs. C; # p < 0.05 vs. E. Two-way ANOVA was used and data are shown as means ± standard error of the mean ( SEM ) (C, n = 16, E, n = 8, E+5003, n = 8). (D) Food intake data during 1-week immobilization. ∗ p < 0.05 vs. C. Two-way ANOVA was used and data are shown as means ± SEM . (E–F) aDMA level indicated for Prmt1 enzymatic activity after 10-week TC-E−5003 administration via subcutaneous injection at a dose of 2 mg/kg body weight, once daily, 5 days a week. (G–J) Skeletal muscle functions tests, G, grip strength, H, suspension time of hang test, I, time of the latency to fall in rotarod test, J, maximum voluntary climbing capacity (MVCC) test. (K–P) Total hindlimb mass and specific muscle mass of various parts of hindlimb, GAS, gastrocnemius, SOL, soleus, QUA, quadriceps femoris, lateralis, TA, tibialis anterior, EDL, extensor digitorum longus. H-S, ∗ p < 0.05 vs. C; ∗∗ p < 0.01 vs. C; # p < 0.05 vs. Im; ## p < 0.01 vs. Im; $ p < 0.05 vs. E + Im; $$ p < 0.01 vs. E + Im. Two-way ANOVA was used and data are shown as means ± SEM (C, n = 8, Im, n = 8, E + Im, n = 8, E+5003+Im, n = 8).

Article Snippet: The antibodies are listed below: aDMA (Anti-Asymmetric Di-Methyl Arginine Motif) (1:1 500, Rabbit, Cell Signal Tech, USA), Akt (protein kinase B) (1:2 000, Mouse, Proteintech, USA), pAkt-Ser473 (1:2 000, Rabbit, Cell Signal Tech, USA), AMPKα2 (1:2 000, Rabbit, Cell Signal Tech, USA), pAMPK-Thr172 (1:2 000, Rabbit, Cell Signal Tech, USA), ATF2 (1:2 000, Rabbit, Proteintech, USA), Atrogin-1 (FBXO32) (1:15 000, Mouse, Proteintech, USA), FoxO3a (Forkhead box O3) (1:1 000, Mouse, Proteintech, USA), pFoxO3a-Ser315 (1:2 000, Rabbit, Proteintech, USA), GAPDH (1:5 000, Rabbit, Utibody, CN), IGF-1 (insulin-like growth factor 1) (1:2 000, Mouse, Proteintech, USA), LaminB (1:2 000, Rabbit, Abcam, USA), MEF2 (myocyte enhancer factor 2) (1:2 000, Rabbit, Proteintech, USA), Myf5 (myogenic factor 5) (1:2 000, Rabbit, Abclonal, CN), MyoD (myogenic differentiation antigen) (1:2 000, Rabbit, Proteintech, USA), MyoG (myogenin) (1:2 000, Rabbit, Proteintech, USA). mTOR (mammalian target of rapamycin) (1:2 000, Rabbit, Cell Signal Tech, USA), p38 (1:2 000, Rabbit, WANLEIBIO, CN), p-p38-Thr180/Tyr182 (1:2 000, Rabbit, WANLEIBIO, CN), PGC-1α (1:1 000, Rabbit, Abcam, USA), Prmt1 (1:2 000, Rabbit, Cell Signal Tech, USA), Raptor (1:1 000, Rabbit, Cell Signal Tech, USA), Sesn1 (1:1 000, Rabbit, HUABIO, CN), Sesn1 (1:1 000, Rabbit, Abcam, USA), TRIM63 (MuRF1) (1:2 000, Rabbit, Proteintech, USA).

Techniques: Activity Assay, Injection, Suspension

Journal: Sports Medicine and Health Science

Article Title: Exercise preconditioning prevents immobilization-induced skeletal muscle atrophy by activating Prmt1-p38/ATF2-Sesn1 signaling axis in C57BL/6J mice

doi: 10.1016/j.smhs.2025.04.001

Figure Lengend Snippet: 10-week combined exercise preconditioning ameliorated 1-week hindlimb immobilization-induced imbalance between synthesis and degradation of protein in skeletal muscle. (A) Representative images of hematoxylin and eosin staining (H&E) of GAS muscle cross-sections. Scale bar = 50 μm. (B) The average CSA of GAS muscle was quantified. (C–D) Real-time PCR results of TIRM63 (MuRF1), FBXO32 (Atrogin-1), Prmt1, and Sesn1 in GAS muscle. (E–N) Western blot results of Prmt1, Sesn1, p-FoxO3a, FoxO3a, Atrogin-1, MuRF1, IGF-1, pAkt-S473, Akt, mTOR, Raptor in GAS muscle. B-N, ∗ p < 0.05 vs. C; ∗∗ p < 0.01 vs. C; # p < 0.05 vs. Im; ## p < 0.01 vs. Im; $ p < 0.05 vs. E + Im; $$ p < 0.01 vs. E + Im. Two-way ANOVA was used and data are shown as means ± standard error of the mean (C, n = 8, Im, n = 8, E + Im, n = 8, E+5003+Im, n = 8).

Techniques: Staining, Real-time Polymerase Chain Reaction, Western Blot

Journal: Sports Medicine and Health Science

Article Title: Exercise preconditioning prevents immobilization-induced skeletal muscle atrophy by activating Prmt1-p38/ATF2-Sesn1 signaling axis in C57BL/6J mice

doi: 10.1016/j.smhs.2025.04.001

Figure Lengend Snippet: Exercise preconditioning increased Sestrin1 (Sesn1) expression by activating protein arginine methyltransferase 1 (Prmt1)-p38/activating transcription factor 2 (ATF2) signaling in mice. (A) ChIP analysis of Prmt1 binding to the ATF2 sequence of mouse Sesn1 promoter in GAS muscle. (B–D) Western blot results of p-p38-T180/182, p38, and ATF2 in GAS muscle. (E–F) Co-IP results, IP: Prmt1, GAS muscle was used. (G–H) Co-IP results, IP: ATF2, GAS muscle was used. (I–J) Co-IP results, IP: p38, GAS muscle was used. A-J, ∗ p < 0.05 vs. C; ∗∗ p < 0.01 vs. C; # p < 0.05 vs. Im; ## p < 0.01 vs. Im; $ p < 0.05 vs. E + Im; $$ p < 0.01 vs. E + Im. Two-way ANOVA was used and data are shown as means ± standard error of the mean (C, n = 8, Im, n = 8, E + Im, n = 8, E+5003+Im, n = 8).

Techniques: Expressing, Binding Assay, Sequencing, Western Blot, Co-Immunoprecipitation Assay

Journal: Sports Medicine and Health Science

Article Title: Exercise preconditioning prevents immobilization-induced skeletal muscle atrophy by activating Prmt1-p38/ATF2-Sesn1 signaling axis in C57BL/6J mice

doi: 10.1016/j.smhs.2025.04.001

Figure Lengend Snippet: Protein arginine methyltransferase 1 (Prmt1)-Sestrin1 (Sesn1) coordinated the differentiation of C2C12 myoblasts into mature myotubes. (A–B) H&E staining of C2C12 myotubes at the 7 th day of differentiation with si-Sesn, and Ad-Sesn1 treatment. Scale bar = 100 μm. (C–D) Western blot results of Sesn1, FoxO3a, Atrogin-1 and MuRF1 in C2C12. A-D, C, control, si-Sesn1, si-RNA of Sesn1, Ad-Sesn1, Adenoviruses overexpressing Sesn1, ∗ p < 0.05 vs. C; ∗∗ p < 0.01 vs. C; # p < 0.05 vs. si-Sesn1; ## p < 0.01 vs. Si-Sesn1. Two-way ANOVA was used and data are shown as means ± standard error of the mean ( SEM ) ( n = 6 in each group). (E–F) H&E staining of C2C12 myotubes at the 7 th day of differentiation with si-Prmt1, and Ad-Prmt1. Scale bar = 100 μm. (G–N) Western blot results of Prmt1, p-p38-T180/182, p38, ATF2, Sesn1, FoxO3a, Atrogin-1 and MuRF1 in C2C12. E-N, C, control, si-Prmt1, si-RNA of Prmt1, Ad-Prmt1, Adenoviruses overexpressing Prmt1, ∗ p < 0.05 vs. C; ∗∗ p < 0.01 vs. C; # p < 0.05 vs. si-Prmt1; ## p < 0.01 vs. si-Prmt1. Two-way ANOVA was used and data are shown as means ± SEM ( n = 3 in each group). (O–R) Western blot results of Prmt1, ATF2 and Sesn1 in C2C12 myoblasts, ∗ p < 0.05; ∗∗ p < 0.01, unpaired Student's t -test was used and data are shown as means ± SEM ( n = 6 in each group). (S–W) Western blot results of Prmt1, FoxO3a, Atrogin-1 and MuRF1 in C2C12 myoblasts, ∗ p < 0.05; ∗∗ p < 0.01, unpaired Student's t -test was used and data are shown as means ± SEM ( n = 6 in each group).

Techniques: Staining, Western Blot, Control

Journal: Sports Medicine and Health Science

Article Title: Exercise preconditioning prevents immobilization-induced skeletal muscle atrophy by activating Prmt1-p38/ATF2-Sesn1 signaling axis in C57BL/6J mice

doi: 10.1016/j.smhs.2025.04.001

Figure Lengend Snippet: Exercise preconditioning activated AMP-Activated protein kinase α2 (AMPKα2)-transcriptional co-activator PPAR-γ co-activator-1 α (PGC-1α) through protein arginine methyltransferase 1 (Prmt1)-Sestrin1 (Sesn1) in immobilized mice. (A–C) Western blot results of p-AMPKα2, AMPKα2, and PGC-1α in GAS muscle. (D–E) Co-IP results, IP: Prmt1, GAS muscle was used. (F–G) Co-IP results, IP: PGC-1α, GAS muscle was used. (H–I) Co-IP results, IP: Sesn1, GAS muscle was used. (J–K) Co-IP results, IP: PGC-1α, GAS muscle was used. (L–M) Co-IP results, IP: AMPKα2, GAS muscle was used. A-M, ∗ p < 0.05 vs. C; ∗∗ p < 0.01 vs. C; # p < 0.05 vs. Im; ## p < 0.01 vs. Im; $ p < 0.05 vs. E + Im; $$ p < 0.01 vs. E + Im. Two-way ANOVA was used and data are shown as means ± standard error of the mean (C, n = 8, Im, n = 8, E + Im, n = 8, E+5003+Im, n = 8).

Techniques: Western Blot, Co-Immunoprecipitation Assay

Journal: Sports Medicine and Health Science

Article Title: Exercise preconditioning prevents immobilization-induced skeletal muscle atrophy by activating Prmt1-p38/ATF2-Sesn1 signaling axis in C57BL/6J mice

doi: 10.1016/j.smhs.2025.04.001

Figure Lengend Snippet: Exercise preconditioning prevented muscle atrophy through protein arginine methyltransferase 1 (Prmt1)-Sestrin1 (Sesn1)-transcriptional co-activator PPAR-γ co-activator-1 α (PGC-1α)-mediated skeletal muscle regeneration. (A–B) Western blot results of MyoD, Myf5, MEF2 and MyoG in GAS muscle. (C–D) Co-IP results, IP: MyoD, GAS muscle was used. A-B, ∗ p < 0.05 vs. C; ∗∗ p < 0.01 vs. C; ## p < 0.01 vs. Im; $ p < 0.05 vs. E + Im; $$ p < 0.01 vs. E + Im. Two-way ANOVA was used, and data are shown as means ± standard error of the mean ( SEM ) (C, n = 8, Im, n = 8, E + Im, n = 8, E+5003+Im, n = 8). (E–F) H&E staining of myotubes at each differentiation time points of C2C12 myoblasts overexpressing Sesn1. Scale bar = 100 μm ∗ p < 0.05 vs. Ad-Sesn1-, unpaired Student's t-test was used and data are shown as means ± SEM ( n = 3 in each group). (G–H) Western blot results of Sesn1, Prmt1, PGC-1α, MyoD, MEF2, Myf5, and MyoG in C2C12 myoblasts at each time points of differentiation. ∗ p < 0.05 vs. D0, unpaired Student's t -test was used and data are shown as means ± SEM ( n = 6 in each group). (I–J) Western blot results of PGC-1α in nucleus of C2C12 myoblasts overexpressing Sesn1 at each time points of differentiation. ∗∗ p < 0.01 vs. Ad-Sesn1, unpaired Student's t -test was used and data are shown as means ± SEM ( n = 6 in each group). (K–L) Western blot results of PGC-1α in cytoplasm of C2C12 myoblasts overexpressing Sesn1 at each time points of differentiation. ∗∗ p < 0.01 vs. Ad-Sesn1-, unpaired Student's t -test was used and data are shown as means ± SEM ( n = 6 in each group).

Techniques: Western Blot, Co-Immunoprecipitation Assay, Staining

Journal: Sports Medicine and Health Science

Article Title: Exercise preconditioning prevents immobilization-induced skeletal muscle atrophy by activating Prmt1-p38/ATF2-Sesn1 signaling axis in C57BL/6J mice

doi: 10.1016/j.smhs.2025.04.001

Article Snippet: ChIP grade antibodies to Prmt1 (1:100, Proteintech, USA) were used to perform immunoprecipitation.

Techniques: Activity Assay, Injection, Suspension

Journal: Sports Medicine and Health Science

Article Title: Exercise preconditioning prevents immobilization-induced skeletal muscle atrophy by activating Prmt1-p38/ATF2-Sesn1 signaling axis in C57BL/6J mice

doi: 10.1016/j.smhs.2025.04.001

Article Snippet: ChIP grade antibodies to Prmt1 (1:100, Proteintech, USA) were used to perform immunoprecipitation.

Techniques: Staining, Real-time Polymerase Chain Reaction, Western Blot

Journal: Sports Medicine and Health Science

Article Title: Exercise preconditioning prevents immobilization-induced skeletal muscle atrophy by activating Prmt1-p38/ATF2-Sesn1 signaling axis in C57BL/6J mice

doi: 10.1016/j.smhs.2025.04.001

Article Snippet: ChIP grade antibodies to Prmt1 (1:100, Proteintech, USA) were used to perform immunoprecipitation.

Techniques: Expressing, Binding Assay, Sequencing, Western Blot, Co-Immunoprecipitation Assay

Journal: Sports Medicine and Health Science

Article Title: Exercise preconditioning prevents immobilization-induced skeletal muscle atrophy by activating Prmt1-p38/ATF2-Sesn1 signaling axis in C57BL/6J mice

doi: 10.1016/j.smhs.2025.04.001

Article Snippet: ChIP grade antibodies to Prmt1 (1:100, Proteintech, USA) were used to perform immunoprecipitation.

Techniques: Staining, Western Blot, Control

Journal: Sports Medicine and Health Science

Article Title: Exercise preconditioning prevents immobilization-induced skeletal muscle atrophy by activating Prmt1-p38/ATF2-Sesn1 signaling axis in C57BL/6J mice

doi: 10.1016/j.smhs.2025.04.001

Article Snippet: ChIP grade antibodies to Prmt1 (1:100, Proteintech, USA) were used to perform immunoprecipitation.

Techniques: Western Blot, Co-Immunoprecipitation Assay

Journal: Sports Medicine and Health Science

Article Title: Exercise preconditioning prevents immobilization-induced skeletal muscle atrophy by activating Prmt1-p38/ATF2-Sesn1 signaling axis in C57BL/6J mice

doi: 10.1016/j.smhs.2025.04.001

Article Snippet: ChIP grade antibodies to Prmt1 (1:100, Proteintech, USA) were used to perform immunoprecipitation.

Techniques: Western Blot, Co-Immunoprecipitation Assay, Staining