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China Pharmaceuticals Inc lfhp-1c
Lfhp 1c, supplied by China Pharmaceuticals Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/lfhp-1c/lfhp+1c/10__1016_slash_s2211___3835_ascii40_21_ascii41_00234___3-29-86-80
Average 90 stars, based on 1 article reviews

lfhp-1c - by Bioz Stars, 2026-11

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Article Title: Table of Contents
Article Snippet: Chenglong Gaoa, Yazhou Xua, Zhuangzhuang Lianga, Yunjie Wanga, Qinghong Shangb, Shengbin Zhangc, Cunfang Wangc, Mingmin Nic, Dalei Wub, Zhangjian Huanga, Tao Panga,d aState Key Laboratory of Natural Medicines, Jiangsu Key Laboratory of Drug Screening, Jiangsu Key Laboratory of Drug Discovery for Metabolic Diseases, China Pharmaceutical University, Nanjing 210009, China bHelmholtz International Lab, State Key Laboratory of Microbial Technology, Shandong University, Qingdao 266237, China cGuangdong Long Fu Pharmaceutical Co., Ltd., Zhongshan 528451, China dKey Laboratory of Drug Quality Control and Pharmacovigilance (China Pharmaceutical University), Ministry of Education, Nanjing 210009, China LFHP-1c directly binding to PGAM5 inhibits PGAM5 enzyme activity and impairs PGAM5 interaction with NRF2, promoting NRF2 transcription activity to protect against blood–brain barrier disruption and ischemic brain injury.

Control:

Binding Assay:

Activity Assay:

Disruption:

Image Search Results

a PGAM5 inhibitor, LFHP-1c treatment suppresses erastin-induced ferroptosis and lipid peroxidation. AC16 cells were treated with erastin (20 μM) with or without LFHP-1c (2 μM) for 16 h for cell death measurement or 12 h for lipid ROS measurement. Cells were stained with Propidium Iodide (PI) and cell death was analyzed by flow cytometry. Cells treated as indicated were stained with BODIPY 581/591 C11, and lipid ROS levels were measured by flow cytometry. b Knockdown of PGAM5 blocked erastin-induced ferroptosis and lipid peroxidation. Western blot images confirm the expression of the indicated proteins. Cells, as indicated, were treated with erastin (20 μM) for 16 h for cell death measurement, or 12 h for lipid ROS measurement. Cell death and lipid ROS were measured as described in ( a ). c DRP1 was dramatically phosphorylated at serine 616 and de-phosphorylated at serine 637 in a time-dependent manner upon erastin treatment. AC16 cells were treated with erastin (20 μM) as indicated. Western blot images confirm the expression of the indicated proteins. d PGAM5 inhibitor LFPH-1c treatment suppresses erastin induced de-phosphorylation of DRP1 at serine 637. AC16 cells were treated with erastin (20 μM) with or without LFPH-1c (2 μM) for the indicated time. Western blot images confirm the expression of the indicated proteins. e Knockdown of PGAM5 blocks erastin-induced de-phosphorylation of DRP1 at serine 637. AC16 cells, as indicated, were treated with erastin (20 μM) for the indicated time. Western blot images confirm the expression of the indicated proteins. f Knockdown of PGAM5 blocks ferroptosis-associated mitochondrial fragmentation. SU9-GFP labeled AC16 cells were treated with erastin (20 μM) as indicated. SU9-GFP labeled mitochondria were imaged by using a confocal laser scanning microscope (scale bars in images of all figures were 10 μM). Quantification of mitochondria with different morphologies (fragmented, short, long). “Short” represents cells with a majority of mitochondria shorter than 10 µm, “Long” represents cells with a majority of mitochondria longer than 10 µm, “Fragmented” represents cells with a majority of granular mitochondria. At least 100 cells were counted for each sample. g Overexpression of PGAM5 suppresses erastin-induced ferroptosis and lipid peroxidation. Western blot images confirm the expression of the indicated proteins. AC16 cells, as indicated, were treated with erastin (20 μM) for 16 h for cell death measurement, or 12 h for lipid ROS measurement. Cell death and lipid ROS were measured as described in ( a ). h The level of PGAM5 influences erastin-induced ferroptosis. Different dose PGAM5-flag plasmids were transfected into AC16 cells, and AC16 cells were cultured for 48 h, and then treated with erastin (20 μM) for 16 h for cell death measurement, or 12 h for lipid ROS measurement. Cell death and lipid ROS were measured as described in ( a ). Western blot images confirmed the expression of the indicated proteins. Data are derived from three independent experiments, and each value represents the mean ± SD. *P < 0.05, **P < 0.01, ***P < 0.001, t test ( n = 3).

Journal: Cell Death & Disease

Article Title: Targeting mitochondrial phosphatase PGAM5 alleviates ferroptosis and acute pancreatitis by upregulating NRF2-mediated FSP1 expression

doi: 10.1038/s41419-026-08484-9

Figure Lengend Snippet: a PGAM5 inhibitor, LFHP-1c treatment suppresses erastin-induced ferroptosis and lipid peroxidation. AC16 cells were treated with erastin (20 μM) with or without LFHP-1c (2 μM) for 16 h for cell death measurement or 12 h for lipid ROS measurement. Cells were stained with Propidium Iodide (PI) and cell death was analyzed by flow cytometry. Cells treated as indicated were stained with BODIPY 581/591 C11, and lipid ROS levels were measured by flow cytometry. b Knockdown of PGAM5 blocked erastin-induced ferroptosis and lipid peroxidation. Western blot images confirm the expression of the indicated proteins. Cells, as indicated, were treated with erastin (20 μM) for 16 h for cell death measurement, or 12 h for lipid ROS measurement. Cell death and lipid ROS were measured as described in ( a ). c DRP1 was dramatically phosphorylated at serine 616 and de-phosphorylated at serine 637 in a time-dependent manner upon erastin treatment. AC16 cells were treated with erastin (20 μM) as indicated. Western blot images confirm the expression of the indicated proteins. d PGAM5 inhibitor LFPH-1c treatment suppresses erastin induced de-phosphorylation of DRP1 at serine 637. AC16 cells were treated with erastin (20 μM) with or without LFPH-1c (2 μM) for the indicated time. Western blot images confirm the expression of the indicated proteins. e Knockdown of PGAM5 blocks erastin-induced de-phosphorylation of DRP1 at serine 637. AC16 cells, as indicated, were treated with erastin (20 μM) for the indicated time. Western blot images confirm the expression of the indicated proteins. f Knockdown of PGAM5 blocks ferroptosis-associated mitochondrial fragmentation. SU9-GFP labeled AC16 cells were treated with erastin (20 μM) as indicated. SU9-GFP labeled mitochondria were imaged by using a confocal laser scanning microscope (scale bars in images of all figures were 10 μM). Quantification of mitochondria with different morphologies (fragmented, short, long). “Short” represents cells with a majority of mitochondria shorter than 10 µm, “Long” represents cells with a majority of mitochondria longer than 10 µm, “Fragmented” represents cells with a majority of granular mitochondria. At least 100 cells were counted for each sample. g Overexpression of PGAM5 suppresses erastin-induced ferroptosis and lipid peroxidation. Western blot images confirm the expression of the indicated proteins. AC16 cells, as indicated, were treated with erastin (20 μM) for 16 h for cell death measurement, or 12 h for lipid ROS measurement. Cell death and lipid ROS were measured as described in ( a ). h The level of PGAM5 influences erastin-induced ferroptosis. Different dose PGAM5-flag plasmids were transfected into AC16 cells, and AC16 cells were cultured for 48 h, and then treated with erastin (20 μM) for 16 h for cell death measurement, or 12 h for lipid ROS measurement. Cell death and lipid ROS were measured as described in ( a ). Western blot images confirmed the expression of the indicated proteins. Data are derived from three independent experiments, and each value represents the mean ± SD. *P < 0.05, **P < 0.01, ***P < 0.001, t test ( n = 3).

Article Snippet: Chemical reagents used were erastin (Selleck, Cat#S7242), ML385 (APE×BIO, Cat#B8300), LFHP-1c (MCE, Cat# HY139598 ), L -arginine (Sigma, Cat#74-79-3), and iFSP1 (MCE, Cat#HY-136057).

Techniques: Staining, Flow Cytometry, Knockdown, Western Blot, Expressing, De-Phosphorylation Assay, Labeling, Laser-Scanning Microscopy, Over Expression, Transfection, Cell Culture, Derivative Assay

a Schematic illustration of the experimental design of the mouse arginine-induced acute pancreatitis model. b LFHP-1c treatment protects against arginine-induced higher levels of serum α-AMS. n = 6. c LFHP-1c treatment protects against arginine-induced higher levels of serum LDH and ALT. n = 6. d LFHP-1c treatment blocks arginine-induced upregulation of pro-inflammatory cytokines (miL-1β, miL-6, and TNF-α) in pancreatic tissue. RT-qPCR analyzes the expression of indicated pro-inflammatory cytokines. n = 3. e Representative H&E sections obtained from the mouse pancreas in response to different treatments after 72 h. f LFHP-1c treatment suppresses arginine-induced upregulation of 4-HNE and activates AMPK and promotes the expression of NRF2 and FSP1 in pancreatic tissue. g LFHP-1c treatment suppresses the arginine-induced higher level of pancreatic tissue MDA. n = 6. h LFHP-1c treatment promotes the mRNA level of FSP1 in pancreatic tissue. RT-qPCR analyzes the expression of FSP1. i LFHP-1c treatment suppresses the elevated mRNA level of PTGS2 induced by arginine in pancreatic tissue. RT-qPCR analyzes the expression of PTGS2. n = 3. Data are derived from independent experiments, and each value represents the mean ± SD. *P < 0.05, **P < 0.01, ***P < 0.001, t test.

Journal: Cell Death & Disease

Article Title: Targeting mitochondrial phosphatase PGAM5 alleviates ferroptosis and acute pancreatitis by upregulating NRF2-mediated FSP1 expression

doi: 10.1038/s41419-026-08484-9

Figure Lengend Snippet: a Schematic illustration of the experimental design of the mouse arginine-induced acute pancreatitis model. b LFHP-1c treatment protects against arginine-induced higher levels of serum α-AMS. n = 6. c LFHP-1c treatment protects against arginine-induced higher levels of serum LDH and ALT. n = 6. d LFHP-1c treatment blocks arginine-induced upregulation of pro-inflammatory cytokines (miL-1β, miL-6, and TNF-α) in pancreatic tissue. RT-qPCR analyzes the expression of indicated pro-inflammatory cytokines. n = 3. e Representative H&E sections obtained from the mouse pancreas in response to different treatments after 72 h. f LFHP-1c treatment suppresses arginine-induced upregulation of 4-HNE and activates AMPK and promotes the expression of NRF2 and FSP1 in pancreatic tissue. g LFHP-1c treatment suppresses the arginine-induced higher level of pancreatic tissue MDA. n = 6. h LFHP-1c treatment promotes the mRNA level of FSP1 in pancreatic tissue. RT-qPCR analyzes the expression of FSP1. i LFHP-1c treatment suppresses the elevated mRNA level of PTGS2 induced by arginine in pancreatic tissue. RT-qPCR analyzes the expression of PTGS2. n = 3. Data are derived from independent experiments, and each value represents the mean ± SD. *P < 0.05, **P < 0.01, ***P < 0.001, t test.

Techniques: Quantitative RT-PCR, Expressing, Derivative Assay

$Otud1 knockout alleviates transverse aortic constriction (TAC)-induced cardiac hypertrophy in vivo . (A) Representative M-mode echocardiographic images from each group in mice (n=6). (B) Assessments of ejection fraction (EF) in Flox and CKO mice at 4 weeks after Sham or TAC surgery (n=6). (C) Assessments of fraction shortening (FS) in Flox and CKO mice at 4 weeks after Sham or TAC surgery (n=6). (D) Assessments of left ventricular end-systolic dimension (LVEDs) in Flox and CKO mice at 4 weeks after Sham or TAC surgery (n=6). (E) Assessments of left ventricular (LV) end-diastolic dimension (LVEDd) in Flox and CKO mice at 4 weeks after Sham or TAC surgery (n=6). (F) Assessments of heart weight (HW) in Flox and CKO mice at 4 weeks after Sham or TAC surgery (n=6). (G) Assessments of HW/body weight (BW) ratios in Flox and CKO mice at 4 weeks after Sham or TAC surgery (n=6). (H) Assessments of lung weight (LW)/BW ratios in Flox and CKO mice at 4 weeks after Sham or TAC surgery (n=6). (I) Assessments of HW/tibia length (TL) ratios in Flox and CKO mice at 4 weeks after Sham or TAC surgery (n=6). (J) Representative images of hematoxylin-eosin (HE) staining of LV cross sections in the hearts of Flox and CKO mice at 4 weeks after Sham or TAC surgery (n=6). Scale bar, 1000 μm for the top set and 50 μm for the bottom parts. (K) Relative cross-sectional areas from the hearts of in Flox and CKO mice at 4 weeks after Sham or TAC surgery (n=6). (L) Representative images of Masson staining of cross-sections in the hearts of in Flox and CKO mice at 4 weeks after Sham or TAC surgery (n=6). Scale bar, 50 μm. (M) Representative images of picrosirius red staining of cross-sections in the hearts of Flox and CKO mice at 4 weeks after Sham or TAC surgery (n=6). Scale bar, 50 μm. (N) Relative cardiac fibrosis from the hearts of Flox and CKO mice at 4 weeks after Sham or TAC surgery (n=6). (O) Representative western blotting results of Myh7 and Anp in hearts from Flox and CKO mice at 4 weeks after Sham or TAC surgery. The experiment was repeated three times. (P) Real-time qPCR analysis of Bnp, Myh7, Col1a1 in heart tissues from Flox and CKO mice at 4 weeks after Sham or TAC surgery (n=6). (Q) The content of Anp, Il-6, Tnf-a in plasma from Flox and CKO mice at 4 weeks after Sham or TAC surgery (n=6).$

Journal: International Journal of Biological Sciences

Article Title: METTL3-mediated m6A modification of OTUD1 aggravates press overload induced myocardial hypertrophy by deubiquitinating PGAM5

doi: 10.7150/ijbs.95707

Figure Lengend Snippet: Otud1 knockout alleviates transverse aortic constriction (TAC)-induced cardiac hypertrophy in vivo . (A) Representative M-mode echocardiographic images from each group in mice (n=6). (B) Assessments of ejection fraction (EF) in Flox and CKO mice at 4 weeks after Sham or TAC surgery (n=6). (C) Assessments of fraction shortening (FS) in Flox and CKO mice at 4 weeks after Sham or TAC surgery (n=6). (D) Assessments of left ventricular end-systolic dimension (LVEDs) in Flox and CKO mice at 4 weeks after Sham or TAC surgery (n=6). (E) Assessments of left ventricular (LV) end-diastolic dimension (LVEDd) in Flox and CKO mice at 4 weeks after Sham or TAC surgery (n=6). (F) Assessments of heart weight (HW) in Flox and CKO mice at 4 weeks after Sham or TAC surgery (n=6). (G) Assessments of HW/body weight (BW) ratios in Flox and CKO mice at 4 weeks after Sham or TAC surgery (n=6). (H) Assessments of lung weight (LW)/BW ratios in Flox and CKO mice at 4 weeks after Sham or TAC surgery (n=6). (I) Assessments of HW/tibia length (TL) ratios in Flox and CKO mice at 4 weeks after Sham or TAC surgery (n=6). (J) Representative images of hematoxylin-eosin (HE) staining of LV cross sections in the hearts of Flox and CKO mice at 4 weeks after Sham or TAC surgery (n=6). Scale bar, 1000 μm for the top set and 50 μm for the bottom parts. (K) Relative cross-sectional areas from the hearts of in Flox and CKO mice at 4 weeks after Sham or TAC surgery (n=6). (L) Representative images of Masson staining of cross-sections in the hearts of in Flox and CKO mice at 4 weeks after Sham or TAC surgery (n=6). Scale bar, 50 μm. (M) Representative images of picrosirius red staining of cross-sections in the hearts of Flox and CKO mice at 4 weeks after Sham or TAC surgery (n=6). Scale bar, 50 μm. (N) Relative cardiac fibrosis from the hearts of Flox and CKO mice at 4 weeks after Sham or TAC surgery (n=6). (O) Representative western blotting results of Myh7 and Anp in hearts from Flox and CKO mice at 4 weeks after Sham or TAC surgery. The experiment was repeated three times. (P) Real-time qPCR analysis of Bnp, Myh7, Col1a1 in heart tissues from Flox and CKO mice at 4 weeks after Sham or TAC surgery (n=6). (Q) The content of Anp, Il-6, Tnf-a in plasma from Flox and CKO mice at 4 weeks after Sham or TAC surgery (n=6).

Article Snippet: To test the role of PGAM5 in pathological cardiac hypertrophy, we used PGAM5 inhibitor LFHP-1c (HY-139598, MCE) in TAC mice.

Techniques: Knock-Out, In Vivo, Staining, Western Blot, Clinical Proteomics

$METTL3 promotes cardiac hypertrophy in an OTUD1 depend way. (A) Representative M-mode echocardiographic images from each group in mice (n=6). (B) Assessments of ejection fraction (EF) in PBS and STM2457 treated TAC mice injected with AAV9-GFP or AAV9-Otud1 at 4 weeks (n=6). (C) Assessments of fraction shortening (FS) in PBS and STM2457 treated TAC mice injected with AAV9-GFP or AAV9-Otud1 at 4 weeks (n=6). (D) Assessments of left ventricular end-systolic dimension (LVEDs) in PBS and STM2457 treated TAC mice injected with AAV9-GFP or AAV9-Otud1 at 4 weeks (n=6). (E) Assessments of left ventricular (LV) end-diastolic dimension (LVEDd) in PBS and STM2457 treated TAC mice injected with AAV9-GFP or AAV9-Otud1 at 4 weeks (n=6). (F) Assessments of heart weight (HW) in PBS and STM2457 treated TAC mice injected with AAV9-GFP or AAV9-Otud1 at 4 weeks (n=6). (G) Assessments of HW/body weight (BW) ratios in PBS and STM2457 treated TAC mice injected with AAV9-GFP or AAV9-Otud1 at 4 weeks (n=6). (H) Assessments of lung weight (LW)/BW ratios in PBS and STM2457 treated TAC mice injected with AAV9-GFP or AAV9-Otud1 at 4 weeks (n=6). (I) Assessments of HW/tibia length (TL) ratios in PBS and STM2457 treated TAC mice injected with AAV9-GFP or AAV9-Otud1 at 4 weeks (n=6). (J) Representative images of hematoxylin-eosin (HE) staining of LV cross sections in the hearts of PBS and STM2457 treated TAC mice injected with AAV9-GFP or AAV9-Otud1 at 4 weeks (n=6). Scale bar, 1000 μm for the top set and 50 μm for the bottom parts. (K) Relative cross-sectional areas from the hearts of PBS and STM2457 treated TAC mice injected with AAV9-GFP or AAV9-Otud1 at 4 weeks (n=6). (L) Representative images of Masson staining of cross-sections in the hearts of PBS and STM2457 treated TAC mice injected with AAV9-GFP or AAV9-Otud1 at 4 weeks (n=6). Scale bar, 50 μm. (M) Representative images of picrosirius red staining of cross-sections in the hearts of PBS and STM2457 treated TAC mice injected with AAV9-GFP or AAV9-Otud1 at 4 weeks (n=6). Scale bar, 50 μm. (N) Relative cardiac fibrosis from the hearts of PBS and STM2457 treated TAC mice injected with AAV9-GFP or AAV9-Otud1 at 4 weeks (n=6). (O) Representative western blotting results of Myh7 and Anp in hearts from PBS and STM2457 treated TAC mice injected with AAV9-GFP or AAV9-Otud1 at 4 weeks. The experiment was repeated three times. (P) Real-time qPCR analysis of Bnp, Myh7, Col1a1 in heart tissues from PBS and STM2457 treated TAC mice injected with AAV9-GFP or AAV9-Otud1 at 4 weeks (n=6). (Q) The content of Anp, Il-6, Tnf-a in plasma from PBS and STM2457 treated TAC mice injected with AAV9-GFP or AAV9-Otud1 at 4 weeks (n=6).$

Journal: International Journal of Biological Sciences

Article Title: METTL3-mediated m6A modification of OTUD1 aggravates press overload induced myocardial hypertrophy by deubiquitinating PGAM5

doi: 10.7150/ijbs.95707

Figure Lengend Snippet: METTL3 promotes cardiac hypertrophy in an OTUD1 depend way. (A) Representative M-mode echocardiographic images from each group in mice (n=6). (B) Assessments of ejection fraction (EF) in PBS and STM2457 treated TAC mice injected with AAV9-GFP or AAV9-Otud1 at 4 weeks (n=6). (C) Assessments of fraction shortening (FS) in PBS and STM2457 treated TAC mice injected with AAV9-GFP or AAV9-Otud1 at 4 weeks (n=6). (D) Assessments of left ventricular end-systolic dimension (LVEDs) in PBS and STM2457 treated TAC mice injected with AAV9-GFP or AAV9-Otud1 at 4 weeks (n=6). (E) Assessments of left ventricular (LV) end-diastolic dimension (LVEDd) in PBS and STM2457 treated TAC mice injected with AAV9-GFP or AAV9-Otud1 at 4 weeks (n=6). (F) Assessments of heart weight (HW) in PBS and STM2457 treated TAC mice injected with AAV9-GFP or AAV9-Otud1 at 4 weeks (n=6). (G) Assessments of HW/body weight (BW) ratios in PBS and STM2457 treated TAC mice injected with AAV9-GFP or AAV9-Otud1 at 4 weeks (n=6). (H) Assessments of lung weight (LW)/BW ratios in PBS and STM2457 treated TAC mice injected with AAV9-GFP or AAV9-Otud1 at 4 weeks (n=6). (I) Assessments of HW/tibia length (TL) ratios in PBS and STM2457 treated TAC mice injected with AAV9-GFP or AAV9-Otud1 at 4 weeks (n=6). (J) Representative images of hematoxylin-eosin (HE) staining of LV cross sections in the hearts of PBS and STM2457 treated TAC mice injected with AAV9-GFP or AAV9-Otud1 at 4 weeks (n=6). Scale bar, 1000 μm for the top set and 50 μm for the bottom parts. (K) Relative cross-sectional areas from the hearts of PBS and STM2457 treated TAC mice injected with AAV9-GFP or AAV9-Otud1 at 4 weeks (n=6). (L) Representative images of Masson staining of cross-sections in the hearts of PBS and STM2457 treated TAC mice injected with AAV9-GFP or AAV9-Otud1 at 4 weeks (n=6). Scale bar, 50 μm. (M) Representative images of picrosirius red staining of cross-sections in the hearts of PBS and STM2457 treated TAC mice injected with AAV9-GFP or AAV9-Otud1 at 4 weeks (n=6). Scale bar, 50 μm. (N) Relative cardiac fibrosis from the hearts of PBS and STM2457 treated TAC mice injected with AAV9-GFP or AAV9-Otud1 at 4 weeks (n=6). (O) Representative western blotting results of Myh7 and Anp in hearts from PBS and STM2457 treated TAC mice injected with AAV9-GFP or AAV9-Otud1 at 4 weeks. The experiment was repeated three times. (P) Real-time qPCR analysis of Bnp, Myh7, Col1a1 in heart tissues from PBS and STM2457 treated TAC mice injected with AAV9-GFP or AAV9-Otud1 at 4 weeks (n=6). (Q) The content of Anp, Il-6, Tnf-a in plasma from PBS and STM2457 treated TAC mice injected with AAV9-GFP or AAV9-Otud1 at 4 weeks (n=6).

Article Snippet: To test the role of PGAM5 in pathological cardiac hypertrophy, we used PGAM5 inhibitor LFHP-1c (HY-139598, MCE) in TAC mice.

Techniques: Injection, Staining, Western Blot, Clinical Proteomics

OTUD1 activates the ASK1-p38/JNK pathways during cardiac hypertrophy. (A) The significantly enriched pathways for the function of Otud1 were determined by KEGG enrichment analysis. (B) Immunoblotting analysis of p-p38, p38, p-JNK and JNK in NRCMs infected with Ad-Otud1 and stimulated with AngⅡ (10 μM) for 48h. Quantification of the relative protein level (right; n= 3). (C) Immunoblotting analysis of p-Ask1, Ask1 in NRCMs infected with Ad-Otud1 and stimulated with AngⅡ (10 μM) for 48h. Quantification of the relative protein level (right; n= 3). (D) Immunoblotting analysis of p-p38, p38, p-JNK and JNK in NRCMs infected with Ad-shOtud1 and stimulated with AngⅡ (10 μM) for 48h. Quantification of the relative protein level (right; n= 3). (E) Immunoblotting analysis of p-Ask1, Ask1 in NRCMs infected with Ad-shOtud1 and stimulated with AngⅡ (10 μM) for 48h. Quantification of the relative protein level (right; n= 3). (F) Immunoblotting analysis of p-p38, p38, p-JNK and JNK in hearts infected with AAV9-Otud1 and subjected to TAC for 4 weeks. Quantification of the relative protein level (right; n= 3). (G) Immunoblotting analysis of p-Ask1, Ask1 in hearts infected with AAV9-Otud1 and subjected to TAC for 4 weeks. Quantification of the relative protein level (right; n= 3). (H) Immunoblotting analysis of p-p38, p38, p-JNK and JNK in Otud1-CKO hearts subjected to TAC for 4 weeks. Quantification of the relative protein level (right; n= 3). (I) Immunoblotting analysis of p-Ask1, Ask1 in Otud1-CKO hearts subjected to TAC for 4 weeks. Quantification of the relative protein level (right; n= 3).

Journal: International Journal of Biological Sciences

Article Title: METTL3-mediated m6A modification of OTUD1 aggravates press overload induced myocardial hypertrophy by deubiquitinating PGAM5

doi: 10.7150/ijbs.95707

Figure Lengend Snippet: OTUD1 activates the ASK1-p38/JNK pathways during cardiac hypertrophy. (A) The significantly enriched pathways for the function of Otud1 were determined by KEGG enrichment analysis. (B) Immunoblotting analysis of p-p38, p38, p-JNK and JNK in NRCMs infected with Ad-Otud1 and stimulated with AngⅡ (10 μM) for 48h. Quantification of the relative protein level (right; n= 3). (C) Immunoblotting analysis of p-Ask1, Ask1 in NRCMs infected with Ad-Otud1 and stimulated with AngⅡ (10 μM) for 48h. Quantification of the relative protein level (right; n= 3). (D) Immunoblotting analysis of p-p38, p38, p-JNK and JNK in NRCMs infected with Ad-shOtud1 and stimulated with AngⅡ (10 μM) for 48h. Quantification of the relative protein level (right; n= 3). (E) Immunoblotting analysis of p-Ask1, Ask1 in NRCMs infected with Ad-shOtud1 and stimulated with AngⅡ (10 μM) for 48h. Quantification of the relative protein level (right; n= 3). (F) Immunoblotting analysis of p-p38, p38, p-JNK and JNK in hearts infected with AAV9-Otud1 and subjected to TAC for 4 weeks. Quantification of the relative protein level (right; n= 3). (G) Immunoblotting analysis of p-Ask1, Ask1 in hearts infected with AAV9-Otud1 and subjected to TAC for 4 weeks. Quantification of the relative protein level (right; n= 3). (H) Immunoblotting analysis of p-p38, p38, p-JNK and JNK in Otud1-CKO hearts subjected to TAC for 4 weeks. Quantification of the relative protein level (right; n= 3). (I) Immunoblotting analysis of p-Ask1, Ask1 in Otud1-CKO hearts subjected to TAC for 4 weeks. Quantification of the relative protein level (right; n= 3).

Article Snippet: To test the role of PGAM5 in pathological cardiac hypertrophy, we used PGAM5 inhibitor LFHP-1c (HY-139598, MCE) in TAC mice.

Techniques: Western Blot, Infection

OTUD1 deubiquitinates PGAM5. (A) Representative western blot of Pgam5 protein in heart of Flox and Otud1-CKO mice subjected to Sham or TAC (n=3). (B) Representative western blotting result of Pgam5 in NRCMs infected with Ad-GFP and Ad-Otud1 and treated with Ang II (10 μM) for 48h and cycloheximide (CHX, 50 μM) for the indicated time points (n=3). (C) Results of ubiquitination assays confirming the ubiquitination of PGAM5 after overexpression of OTUD1 for 48 h and treated with MG132 (50 μM) for 6 h in 293T. (D) Results of ubiquitination assays confirming the K48 ubiquitination of PGAM5 after co-transfected with Flag-OTUD1, HA-Ub-WT, HA-Ub-K48, HA-Ub-K63 for 24 h and treatment with MG132 (50 μM) for 6 h in 293T. (E) Results of ubiquitination assays confirming the expression and ubiquitination of Pgam5 in NRCMs infected with Ad-GFP and Ad-Otud1 and followed by Ang Ⅱ treatment. (F) Results of ubiquitination assays confirming the expression and ubiquitination of Pgam5 in heart tissue from Flox and CKO mice subjected to sham or TAC. (G) Results of ubiquitination assays confirming the ubiquitination of Pham5 after overexpression of OTUD1, OTUD1(C320A) and Pgam5 for 24 h and treated with MG132 (50 μM) for 6 h in 293T cells. (H) Immunoblotting analysis of Pgam5, Ad-Otud1 and Ad-Otud1 (C294S) in NRCMs.

Journal: International Journal of Biological Sciences

Article Title: METTL3-mediated m6A modification of OTUD1 aggravates press overload induced myocardial hypertrophy by deubiquitinating PGAM5

doi: 10.7150/ijbs.95707

Figure Lengend Snippet: OTUD1 deubiquitinates PGAM5. (A) Representative western blot of Pgam5 protein in heart of Flox and Otud1-CKO mice subjected to Sham or TAC (n=3). (B) Representative western blotting result of Pgam5 in NRCMs infected with Ad-GFP and Ad-Otud1 and treated with Ang II (10 μM) for 48h and cycloheximide (CHX, 50 μM) for the indicated time points (n=3). (C) Results of ubiquitination assays confirming the ubiquitination of PGAM5 after overexpression of OTUD1 for 48 h and treated with MG132 (50 μM) for 6 h in 293T. (D) Results of ubiquitination assays confirming the K48 ubiquitination of PGAM5 after co-transfected with Flag-OTUD1, HA-Ub-WT, HA-Ub-K48, HA-Ub-K63 for 24 h and treatment with MG132 (50 μM) for 6 h in 293T. (E) Results of ubiquitination assays confirming the expression and ubiquitination of Pgam5 in NRCMs infected with Ad-GFP and Ad-Otud1 and followed by Ang Ⅱ treatment. (F) Results of ubiquitination assays confirming the expression and ubiquitination of Pgam5 in heart tissue from Flox and CKO mice subjected to sham or TAC. (G) Results of ubiquitination assays confirming the ubiquitination of Pham5 after overexpression of OTUD1, OTUD1(C320A) and Pgam5 for 24 h and treated with MG132 (50 μM) for 6 h in 293T cells. (H) Immunoblotting analysis of Pgam5, Ad-Otud1 and Ad-Otud1 (C294S) in NRCMs.

Article Snippet: To test the role of PGAM5 in pathological cardiac hypertrophy, we used PGAM5 inhibitor LFHP-1c (HY-139598, MCE) in TAC mice.

Techniques: Western Blot, Infection, Ubiquitin Proteomics, Over Expression, Transfection, Expressing

OTUD1 directly binds to PGAM5. (A) Schematic illustration of mass spectrometry analysis to identify proteins binding to OTUD1. (B) PGAM5 peptides derived from the mass spectrometric analysis of OTUD1. (C-D) Co-IP assays of the interaction between OTUD1 and PGAM5 in 293T cells transfected with the indicated plasmids. (E-F) Co-IP assays of Otud1 and Pgam5 in NRCMs. (G-H) Co-IP assays of Otud1 and Pgam5 in heart tissues. (I) Schematic illustration of the OTUD1 domain deletion mutants. (J) Co-IP analysis of the binding region of OTUD1 and PGAM5.

Journal: International Journal of Biological Sciences

Article Title: METTL3-mediated m6A modification of OTUD1 aggravates press overload induced myocardial hypertrophy by deubiquitinating PGAM5

doi: 10.7150/ijbs.95707

Figure Lengend Snippet: OTUD1 directly binds to PGAM5. (A) Schematic illustration of mass spectrometry analysis to identify proteins binding to OTUD1. (B) PGAM5 peptides derived from the mass spectrometric analysis of OTUD1. (C-D) Co-IP assays of the interaction between OTUD1 and PGAM5 in 293T cells transfected with the indicated plasmids. (E-F) Co-IP assays of Otud1 and Pgam5 in NRCMs. (G-H) Co-IP assays of Otud1 and Pgam5 in heart tissues. (I) Schematic illustration of the OTUD1 domain deletion mutants. (J) Co-IP analysis of the binding region of OTUD1 and PGAM5.

Article Snippet: To test the role of PGAM5 in pathological cardiac hypertrophy, we used PGAM5 inhibitor LFHP-1c (HY-139598, MCE) in TAC mice.

Techniques: Mass Spectrometry, Binding Assay, Derivative Assay, Co-Immunoprecipitation Assay, Transfection

Journal: International Journal of Biological Sciences

Article Title: METTL3-mediated m6A modification of OTUD1 aggravates press overload induced myocardial hypertrophy by deubiquitinating PGAM5

doi: 10.7150/ijbs.95707

Article Snippet: To test the role of PGAM5 in pathological cardiac hypertrophy, we used PGAM5 inhibitor LFHP-1c (HY-139598, MCE) in TAC mice.

Techniques: Western Blot, Infection, Over Expression, Transfection, Expressing

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