Review

senp2 antibody (ABclonal Biotechnology)

ABclonal Biotechnology is a verified supplier

About

News

Press Release

Team

Advisors

Partners

Contact

Bioz Stars

Bioz vStars

Buy from Supplier

Structured Review

ABclonal Biotechnology senp2 antibody
Senp2 Antibody, supplied by ABclonal Biotechnology, 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/senp2+antibody/pmc11387118__Supplementary_Data2-4-51-52?v=ABclonal+Biotechnology
Average 90 stars, based on 1 article reviews

senp2 antibody - by Bioz Stars, 2026-07

90/100 stars

Images

Image Search Results

Journal: iScience

Article Title: SENP2-based N-terminal truncation of α-synuclein in Lewy pathology propagation

doi: 10.1016/j.isci.2025.111935

Figure Lengend Snippet: Screening of αSyn-processing enzyme

Article Snippet: Rabbit anti-SENP2 antibody , GeneTex , Cat# 110504; RRID: AB_1951846.

Techniques: Inhibition, Activity Assay, Ubiquitin Proteomics

Identification of processing enzyme (A–F) Inhibition of aggregate formation by NSC632839. Primary neurons were treated with PFFs and cultured in the presence of DMSO (A) or NSC632839 (B). The region marked by a white square in (A) and (B) is magnified in (C) and (D), respectively. Arrowheads in (A) and (C) indicate the formation of the aggregates. Quantitative comparison of the phosphorylated-αSyn-positive area (E) and DAPI-positive area (F) between DMSO-treated and NSC632839-treated neurons ( n = 3 fluorescent images from 2 coverslips were analyzed for each treatment; According to the F-test to compare variances in (E) and (F), F-values were 8.17 and 2.39 ( p = 0.218 and 0.589), respectively. Significant difference was shown in (E), p = 0.0096. ∗∗ p < 0.01, two-tailed, unpaired t test; two independent cultures were performed and confirmed reproducibility). Data represent mean ± SEM. (G) Cleavage of αSyn by GST-fused recombinant SENP2 for 4 h at 37°C. A cleaved fragment is indicated by the arrowhead. Mono, αSyn monomer. (H–J) Dose-dependent effect of SENP2 on αSyn-cleavage. αSyn was processed for 24 h at 37°C. The cleaved fragment (red arrowhead) was gradually increased in the presence of a higher amount of SENP2. Black and white arrowheads show His-tagged full-length αSyn- and GST-fused SENP2 recombinant protein, respectively. Note that αSyn-cleavage increased high-molecular-weight SDS-resistant immunoreactivity (asterisk). This αSyn-cleavage by SENP2 for 4 h was inhibited by the insertion of the N-terminal mutations (J). Scale bar: 20 μm in (A)–(D).

Journal: iScience

Article Title: SENP2-based N-terminal truncation of α-synuclein in Lewy pathology propagation

doi: 10.1016/j.isci.2025.111935

Figure Lengend Snippet: Identification of processing enzyme (A–F) Inhibition of aggregate formation by NSC632839. Primary neurons were treated with PFFs and cultured in the presence of DMSO (A) or NSC632839 (B). The region marked by a white square in (A) and (B) is magnified in (C) and (D), respectively. Arrowheads in (A) and (C) indicate the formation of the aggregates. Quantitative comparison of the phosphorylated-αSyn-positive area (E) and DAPI-positive area (F) between DMSO-treated and NSC632839-treated neurons ( n = 3 fluorescent images from 2 coverslips were analyzed for each treatment; According to the F-test to compare variances in (E) and (F), F-values were 8.17 and 2.39 ( p = 0.218 and 0.589), respectively. Significant difference was shown in (E), p = 0.0096. ∗∗ p < 0.01, two-tailed, unpaired t test; two independent cultures were performed and confirmed reproducibility). Data represent mean ± SEM. (G) Cleavage of αSyn by GST-fused recombinant SENP2 for 4 h at 37°C. A cleaved fragment is indicated by the arrowhead. Mono, αSyn monomer. (H–J) Dose-dependent effect of SENP2 on αSyn-cleavage. αSyn was processed for 24 h at 37°C. The cleaved fragment (red arrowhead) was gradually increased in the presence of a higher amount of SENP2. Black and white arrowheads show His-tagged full-length αSyn- and GST-fused SENP2 recombinant protein, respectively. Note that αSyn-cleavage increased high-molecular-weight SDS-resistant immunoreactivity (asterisk). This αSyn-cleavage by SENP2 for 4 h was inhibited by the insertion of the N-terminal mutations (J). Scale bar: 20 μm in (A)–(D).

Article Snippet: Rabbit anti-SENP2 antibody , GeneTex , Cat# 110504; RRID: AB_1951846.

Techniques: Inhibition, Cell Culture, Comparison, Two Tailed Test, Recombinant, High Molecular Weight

Presence of endogenous SENP2 in αSyn-aggregates (A) Presence of SENP2 in PFF-induced αSyn-aggregates formed in primary cultured neurons. (B) Presence of SENP2 in αSyn-aggregates formed in the neuron of the substantia nigra pars compacta of PD-brain. Arrowheads indicate examples of the overlapping intense signals of SENP2 and phosphorylated αSyn. Scale bar: 5 μm.

Journal: iScience

Article Title: SENP2-based N-terminal truncation of α-synuclein in Lewy pathology propagation

doi: 10.1016/j.isci.2025.111935

Figure Lengend Snippet: Presence of endogenous SENP2 in αSyn-aggregates (A) Presence of SENP2 in PFF-induced αSyn-aggregates formed in primary cultured neurons. (B) Presence of SENP2 in αSyn-aggregates formed in the neuron of the substantia nigra pars compacta of PD-brain. Arrowheads indicate examples of the overlapping intense signals of SENP2 and phosphorylated αSyn. Scale bar: 5 μm.

Article Snippet: Rabbit anti-SENP2 antibody , GeneTex , Cat# 110504; RRID: AB_1951846.

Techniques: Cell Culture

Journal: iScience

Article Title: SENP2-based N-terminal truncation of α-synuclein in Lewy pathology propagation

doi: 10.1016/j.isci.2025.111935

Figure Lengend Snippet:

Article Snippet: Rabbit anti-SENP2 antibody , GeneTex , Cat# 110504; RRID: AB_1951846.

Techniques: Plasmid Preparation, Recombinant, Derivative Assay, Silver Staining, H&E Stain, Knock-Out, Software, Sequencing, Fluorsave

Effects of Topotecan on SENP2. ( a ) Top Panel: cells expressing OAT3 were treated with topotecan (1 µM, 12 h) and lysed, followed by immunoblotting (IB) with anti-SENP2 to measure endogenous SENP2 in the whole-cell lysate. Bottom panel: The same blot was re-probed with anti-GAPDH to detect the total protein marker GAPDH. ( b ) The densitometry of a and other repeats. Density values were normalized to GAPDH. Values are mean ± S.D. ( n = 3). ns, not significant. ( c ) Top Panel: Cells expressing OAT3 were treated with topotecan (1 µM, 12 h). OAT3 was immunoprecipitated (IP) first and immunoblotted (IB) with anti-SENP2 to detect SENP2 that bound to OAT3. Bottom panel: The same blot was re-probed with an anti-myc antibody to assess the total amount of OAT3 pulled down. ( d ) The densitometry of c and other repeats. Density values were normalized to total pulled-down OAT3. Values are mean ± S.D. ( n = 3). * p < 0.05.

Journal: Pharmaceutics

Article Title: Topotecan and Ginkgolic Acid Inhibit the Expression and Transport Activity of Human Organic Anion Transporter 3 by Suppressing SUMOylation of the Transporter

doi: 10.3390/pharmaceutics16050638

Figure Lengend Snippet: Effects of Topotecan on SENP2. ( a ) Top Panel: cells expressing OAT3 were treated with topotecan (1 µM, 12 h) and lysed, followed by immunoblotting (IB) with anti-SENP2 to measure endogenous SENP2 in the whole-cell lysate. Bottom panel: The same blot was re-probed with anti-GAPDH to detect the total protein marker GAPDH. ( b ) The densitometry of a and other repeats. Density values were normalized to GAPDH. Values are mean ± S.D. ( n = 3). ns, not significant. ( c ) Top Panel: Cells expressing OAT3 were treated with topotecan (1 µM, 12 h). OAT3 was immunoprecipitated (IP) first and immunoblotted (IB) with anti-SENP2 to detect SENP2 that bound to OAT3. Bottom panel: The same blot was re-probed with an anti-myc antibody to assess the total amount of OAT3 pulled down. ( d ) The densitometry of c and other repeats. Density values were normalized to total pulled-down OAT3. Values are mean ± S.D. ( n = 3). * p < 0.05.

Article Snippet: Rabbit anti-SUMO2/3, anti-Ubc9, and anti-SENP2 antibodies were purchased from Abcam (Cambridge, MA, USA).

Techniques: Expressing, Western Blot, Marker, Immunoprecipitation

CHK1 regulates L-flow-induced SENP2 S344 phosphorylation, subsequently suppresses ERK5 and p53 SUMOylation: ( A ) HUVECs transduced with Ad-SENP2 WT or Ad-SENP2 S344A were exposed to L-flow for 0 and 30 min, and the levels of SENP2 (p-S344 and total), ERK5 (p-T-E-Y and total), and actin (loading control) were determined using Wes. An increase in p-ERK5-T-E-Y indicated successful generation of L-flow, in addition to elongated cell shape ( , ). ( B ) HUVECs were exposed to D-flow for 0, 20, 40, and 60 min, and the levels of SENP2 (p-S344 and total) were determined using immunoblotting. ( C ) HUVECs pretreated with 250 nM GDC 0575 were exposed to L-flow for 0, 20, 40, and 60 min, and the levels of SENP2 (p-S344 and total), CHK1 (p-S280, p-S345, and total), and actin were determined using Wes. ( D , upper panel) The graphs present quantified data from 3 independent experiments from ( C ) ( n = 3) (* p < 0.05, ** p < 0.01, two-way ANOVA). (D , lower panel ) The graphs present quantified data from 3 independent experiments from ( B ) ( n = 3). N.S. indicates no significance. (E–G) The graphs present quantified data from 3 independent experiments from ( C ) ( n = 3) (* p < 0.05, ** p < 0.01, two-way ANOVA). (H) WT mouse lung ECs (WT MLECs) and SENP2 S344A KI MLECs were exposed to L-flow for 0 and 30 min, and the levels of SENP2 (p-S344 and total) were determined by immunoblotting. (I ) WT MLECs and SENP2 S344A KI MLECs were exposed to L-flow for 0 and 30 min. Lysates were immuno-precipitated with the SUMO2/3 antibody (Signal-Seeker TM SUMOylation 2/3 Detection Kit, #BK162; Cytoskeleton, Inc.), and ERK5 or p53 antibody was used to detect SUMOylated ERK5 or p53 using Wes, respectively. The SUMO2/3 antibody was also used to confirm equal immunoprecipitation across the samples. Control beads were used as the negative control. ERK5, SENP2, and p53antibodies were used to detect their expression in total cell lysates using Wes. ( J ) The graphs present quantified data from 4 (upper panel) and 5 (lower panel) independent experiments (* p < 0.05, two-way ANOVA).

Journal: Frontiers in Cardiovascular Medicine

Article Title: Endothelial activation and fibrotic changes are impeded by laminar flow-induced CHK1-SENP2 activity through mechanisms distinct from endothelial-to-mesenchymal cell transition

doi: 10.3389/fcvm.2023.1187490

Figure Lengend Snippet: CHK1 regulates L-flow-induced SENP2 S344 phosphorylation, subsequently suppresses ERK5 and p53 SUMOylation: ( A ) HUVECs transduced with Ad-SENP2 WT or Ad-SENP2 S344A were exposed to L-flow for 0 and 30 min, and the levels of SENP2 (p-S344 and total), ERK5 (p-T-E-Y and total), and actin (loading control) were determined using Wes. An increase in p-ERK5-T-E-Y indicated successful generation of L-flow, in addition to elongated cell shape ( , ). ( B ) HUVECs were exposed to D-flow for 0, 20, 40, and 60 min, and the levels of SENP2 (p-S344 and total) were determined using immunoblotting. ( C ) HUVECs pretreated with 250 nM GDC 0575 were exposed to L-flow for 0, 20, 40, and 60 min, and the levels of SENP2 (p-S344 and total), CHK1 (p-S280, p-S345, and total), and actin were determined using Wes. ( D , upper panel) The graphs present quantified data from 3 independent experiments from ( C ) ( n = 3) (* p < 0.05, ** p < 0.01, two-way ANOVA). (D , lower panel ) The graphs present quantified data from 3 independent experiments from ( B ) ( n = 3). N.S. indicates no significance. (E–G) The graphs present quantified data from 3 independent experiments from ( C ) ( n = 3) (* p < 0.05, ** p < 0.01, two-way ANOVA). (H) WT mouse lung ECs (WT MLECs) and SENP2 S344A KI MLECs were exposed to L-flow for 0 and 30 min, and the levels of SENP2 (p-S344 and total) were determined by immunoblotting. (I ) WT MLECs and SENP2 S344A KI MLECs were exposed to L-flow for 0 and 30 min. Lysates were immuno-precipitated with the SUMO2/3 antibody (Signal-Seeker TM SUMOylation 2/3 Detection Kit, #BK162; Cytoskeleton, Inc.), and ERK5 or p53 antibody was used to detect SUMOylated ERK5 or p53 using Wes, respectively. The SUMO2/3 antibody was also used to confirm equal immunoprecipitation across the samples. Control beads were used as the negative control. ERK5, SENP2, and p53antibodies were used to detect their expression in total cell lysates using Wes. ( J ) The graphs present quantified data from 4 (upper panel) and 5 (lower panel) independent experiments (* p < 0.05, two-way ANOVA).

Article Snippet: SENP2 antibody (NBP1-31217) and β-actin antibody (NB600-532) were purchased from Novus Biologicals (Briarwood Ave, CO, USA).

Techniques: Phospho-proteomics, Transduction, Control, Western Blot, Immunoprecipitation, Negative Control, Expressing

Increased EC inflammation and apoptosis in SENP2 S344A KI mice: ( A ) En face preparation of WT and SENP2 S344A KI aortas were immunofluorescence-stained with VCAM1 (red, EC inflammation) and VE-Cad (green, EC marker). ( B ) Aortic sections were stained with TUNEL (green, EC apoptosis ) and DAPI (blue, nucleus ). TUNEL-positive apoptotic nuclei were counted, indicating the colocalization between the TUNEL signal (representing fragmented DNA) and the DAPI signal (representing cell nuclei) . The graphs present quantified data from 5 independent samples ( n = 5) (* p < 0.05, ** p < 0.01, two-way ANOVA for ( A) ; unpaired t -test for ( B )).

Journal: Frontiers in Cardiovascular Medicine

Article Title: Endothelial activation and fibrotic changes are impeded by laminar flow-induced CHK1-SENP2 activity through mechanisms distinct from endothelial-to-mesenchymal cell transition

doi: 10.3389/fcvm.2023.1187490

Figure Lengend Snippet: Increased EC inflammation and apoptosis in SENP2 S344A KI mice: ( A ) En face preparation of WT and SENP2 S344A KI aortas were immunofluorescence-stained with VCAM1 (red, EC inflammation) and VE-Cad (green, EC marker). ( B ) Aortic sections were stained with TUNEL (green, EC apoptosis ) and DAPI (blue, nucleus ). TUNEL-positive apoptotic nuclei were counted, indicating the colocalization between the TUNEL signal (representing fragmented DNA) and the DAPI signal (representing cell nuclei) . The graphs present quantified data from 5 independent samples ( n = 5) (* p < 0.05, ** p < 0.01, two-way ANOVA for ( A) ; unpaired t -test for ( B )).

Article Snippet: SENP2 antibody (NBP1-31217) and β-actin antibody (NB600-532) were purchased from Novus Biologicals (Briarwood Ave, CO, USA).

Techniques: Immunofluorescence, Staining, Marker, TUNEL Assay

Increased lipid-laden lesions and fibrotic caps in SENP2 S344A KI mice: SENP2 S344A KI and WT mice were injected with a single dose of rAAV8-mPCSK9 and fed a high fat diet (HFD) for 16 weeks . ( A ) En face Oil Red O staining was performed to quantify lipid abundance and distribution. ( C ) The bone marrow transplantation (BMT) procedure was conducted . ( D ) Representative PCR data demonstrate the success of the BMT. ( E ) En face Oil Red O staining was performed on the BMT-generated models. ( G ) Aortic valve leaflet sections were stained with Masson's trichrome to evaluate changes in the aortic valves. ( B, F, H–K ) The graphs present quantified data from samples ( n = 7–10) (* p < 0.05, ** p < 0.01, unpaired t -test). N.S. indicates non-significant.

Journal: Frontiers in Cardiovascular Medicine

Article Title: Endothelial activation and fibrotic changes are impeded by laminar flow-induced CHK1-SENP2 activity through mechanisms distinct from endothelial-to-mesenchymal cell transition

doi: 10.3389/fcvm.2023.1187490

Figure Lengend Snippet: Increased lipid-laden lesions and fibrotic caps in SENP2 S344A KI mice: SENP2 S344A KI and WT mice were injected with a single dose of rAAV8-mPCSK9 and fed a high fat diet (HFD) for 16 weeks . ( A ) En face Oil Red O staining was performed to quantify lipid abundance and distribution. ( C ) The bone marrow transplantation (BMT) procedure was conducted . ( D ) Representative PCR data demonstrate the success of the BMT. ( E ) En face Oil Red O staining was performed on the BMT-generated models. ( G ) Aortic valve leaflet sections were stained with Masson's trichrome to evaluate changes in the aortic valves. ( B, F, H–K ) The graphs present quantified data from samples ( n = 7–10) (* p < 0.05, ** p < 0.01, unpaired t -test). N.S. indicates non-significant.

Article Snippet: SENP2 antibody (NBP1-31217) and β-actin antibody (NB600-532) were purchased from Novus Biologicals (Briarwood Ave, CO, USA).

Techniques: Injection, Staining, Transplantation Assay, Generated

Radiation-induced EC activation through CHK1 downregulation: ( A )there was no significant difference in lipid-laden lesions between female WT → WT and WT → SENP2 S344A KI mice ( n = 3–4). ( B ) Expression levels of CHK1, SENP2 (p-S344 and total), VCAM1, ICAM1, and actin were evaluated in HUVECs exposed to 0, 2, 4, 6, 8 Gy of ionizing radiation (IR) for 24 h. ( C ) The graphs present quantified data from 3 independent experiments (** p < 0.01, two-way ANOVA). ( D , left panel) SUMOylated ERK5 was assessed in siRNA-treated HUVECs, and the lysates were immuno-precipitated as described in . ( D , right panel) The graphs present quantified data from 3 independent experiments (** p < 0.01, t -test). ( E , left panel) siRNA-treated HUVECs were exposed to D-flow for 24 h, and the expression of ICAM1, CHK1, and actin were determined using immunoblotting. ( E , right panel) The graphs present quantified data from 3 independent experiments (* p < 0.05, two-way ANOVA). ( F ) Expression levels of ICAM1, VCAM1, CHK1, and actin were evaluated in siRNA-treated HUVECs exposed to L-flow for 24 h using immunoblotting. ( G ) The graphs present quantified data from 3 or 4 independent experiments (* p < 0.05, ** p < 0.01, two-way ANOVA).

Journal: Frontiers in Cardiovascular Medicine

Article Title: Endothelial activation and fibrotic changes are impeded by laminar flow-induced CHK1-SENP2 activity through mechanisms distinct from endothelial-to-mesenchymal cell transition

doi: 10.3389/fcvm.2023.1187490

Figure Lengend Snippet: Radiation-induced EC activation through CHK1 downregulation: ( A )there was no significant difference in lipid-laden lesions between female WT → WT and WT → SENP2 S344A KI mice ( n = 3–4). ( B ) Expression levels of CHK1, SENP2 (p-S344 and total), VCAM1, ICAM1, and actin were evaluated in HUVECs exposed to 0, 2, 4, 6, 8 Gy of ionizing radiation (IR) for 24 h. ( C ) The graphs present quantified data from 3 independent experiments (** p < 0.01, two-way ANOVA). ( D , left panel) SUMOylated ERK5 was assessed in siRNA-treated HUVECs, and the lysates were immuno-precipitated as described in . ( D , right panel) The graphs present quantified data from 3 independent experiments (** p < 0.01, t -test). ( E , left panel) siRNA-treated HUVECs were exposed to D-flow for 24 h, and the expression of ICAM1, CHK1, and actin were determined using immunoblotting. ( E , right panel) The graphs present quantified data from 3 independent experiments (* p < 0.05, two-way ANOVA). ( F ) Expression levels of ICAM1, VCAM1, CHK1, and actin were evaluated in siRNA-treated HUVECs exposed to L-flow for 24 h using immunoblotting. ( G ) The graphs present quantified data from 3 or 4 independent experiments (* p < 0.05, ** p < 0.01, two-way ANOVA).

Article Snippet: SENP2 antibody (NBP1-31217) and β-actin antibody (NB600-532) were purchased from Novus Biologicals (Briarwood Ave, CO, USA).

Techniques: Activation Assay, Expressing, Western Blot

Increased EC pathophysiological stress response in SENP2 S344A KI MLECs: ( A ) the volcano plot illustrates the differentially expressed genes (DEGs) in WT MLECs compared to SENP2 S344A KI MLECs after L-flow; “red” dots represent upregulated DEGs, and “blue” dots represent downregulated DEGs. ( B ) A heatmap displaying hierarchical clustering of DEGs between WT MLECs vs. SENP2 S344A KI MLECs after L-flow for 24 h. ( C ) A Venn diagram indicating the total number of DEGs in WT MLECs and SENP2 S344A KI MLECs. ( D ) Annotation of EC activation-related gene ontology (GO) pathways identified in quadruplicate between WT MLECs vs. SENP2 S344A KI MLECs. ( E ) A molecular function Chord plot illustrating the enriched GO biological process terms associated with EC activation in SENP2 S344A KI MLEC transcripts, along with the corresponding genes arranged by their expression levels. ( F ) HUVECs transduced with Ad-SENP2 WT or Ad-SENP2 S344A were subjected to a scratch assay and exposed to L-flow for 6 h. Representative images of cell migration are shown. The dashed line represents the initial or final migration areas. ( G ) The graphs present quantified data from 6 independent experiments (* p < 0.05, ** p < 0.01, two-way ANOVA).

Journal: Frontiers in Cardiovascular Medicine

Article Title: Endothelial activation and fibrotic changes are impeded by laminar flow-induced CHK1-SENP2 activity through mechanisms distinct from endothelial-to-mesenchymal cell transition

doi: 10.3389/fcvm.2023.1187490

Figure Lengend Snippet: Increased EC pathophysiological stress response in SENP2 S344A KI MLECs: ( A ) the volcano plot illustrates the differentially expressed genes (DEGs) in WT MLECs compared to SENP2 S344A KI MLECs after L-flow; “red” dots represent upregulated DEGs, and “blue” dots represent downregulated DEGs. ( B ) A heatmap displaying hierarchical clustering of DEGs between WT MLECs vs. SENP2 S344A KI MLECs after L-flow for 24 h. ( C ) A Venn diagram indicating the total number of DEGs in WT MLECs and SENP2 S344A KI MLECs. ( D ) Annotation of EC activation-related gene ontology (GO) pathways identified in quadruplicate between WT MLECs vs. SENP2 S344A KI MLECs. ( E ) A molecular function Chord plot illustrating the enriched GO biological process terms associated with EC activation in SENP2 S344A KI MLEC transcripts, along with the corresponding genes arranged by their expression levels. ( F ) HUVECs transduced with Ad-SENP2 WT or Ad-SENP2 S344A were subjected to a scratch assay and exposed to L-flow for 6 h. Representative images of cell migration are shown. The dashed line represents the initial or final migration areas. ( G ) The graphs present quantified data from 6 independent experiments (* p < 0.05, ** p < 0.01, two-way ANOVA).

Article Snippet: SENP2 antibody (NBP1-31217) and β-actin antibody (NB600-532) were purchased from Novus Biologicals (Briarwood Ave, CO, USA).

Techniques: Activation Assay, Expressing, Transduction, Wound Healing Assay, Migration

Increased EC activation-stimulated fibrosis in SENP2 S344A KI MLECs with upregulated expression of EC markers: ( A ) after L-flow, the Z -score of fibrosis-related processes is positively upregulated in SENP2 S344A KI MLECs, as determined by IPA analysis. ( B ) Under static condition, the Z -score of the pulmonary fibrosis idiopathic signaling pathway remains positive in SENP2 S344A KI MLECs. ( C , D ) Under static condition, the Z -score of EC activation-associated processes, including cell adhesion, angiogenesis, positive regulation of epithelial cell proliferation, and extracelular matrix organization, is positive in SENP2 S344A KI MLECs. ( E ) DNA synthesis is increased in HUVECs transduced with Ad-SENP2 S344A compared to HUVECs transduced with Ad-SENP2 WT, as demonstrated by data from 3 independent experiments. ( F , left panel) The expression of mesenchymal markers (TWIST1, αSMA) is increased in SENP2 S344A KI MLECs. ( F , right panel) The graphs present quantified data from 3 independent experiments (* p < 0.05, t -test). ( G , H ) The expression of both mesenchymal ( G ) and endothelial ( H ) markers is increased in SENP2 S344A KI MLECs.

Journal: Frontiers in Cardiovascular Medicine

Article Title: Endothelial activation and fibrotic changes are impeded by laminar flow-induced CHK1-SENP2 activity through mechanisms distinct from endothelial-to-mesenchymal cell transition

doi: 10.3389/fcvm.2023.1187490

Figure Lengend Snippet: Increased EC activation-stimulated fibrosis in SENP2 S344A KI MLECs with upregulated expression of EC markers: ( A ) after L-flow, the Z -score of fibrosis-related processes is positively upregulated in SENP2 S344A KI MLECs, as determined by IPA analysis. ( B ) Under static condition, the Z -score of the pulmonary fibrosis idiopathic signaling pathway remains positive in SENP2 S344A KI MLECs. ( C , D ) Under static condition, the Z -score of EC activation-associated processes, including cell adhesion, angiogenesis, positive regulation of epithelial cell proliferation, and extracelular matrix organization, is positive in SENP2 S344A KI MLECs. ( E ) DNA synthesis is increased in HUVECs transduced with Ad-SENP2 S344A compared to HUVECs transduced with Ad-SENP2 WT, as demonstrated by data from 3 independent experiments. ( F , left panel) The expression of mesenchymal markers (TWIST1, αSMA) is increased in SENP2 S344A KI MLECs. ( F , right panel) The graphs present quantified data from 3 independent experiments (* p < 0.05, t -test). ( G , H ) The expression of both mesenchymal ( G ) and endothelial ( H ) markers is increased in SENP2 S344A KI MLECs.

Article Snippet: SENP2 antibody (NBP1-31217) and β-actin antibody (NB600-532) were purchased from Novus Biologicals (Briarwood Ave, CO, USA).

Techniques: Activation Assay, Expressing, DNA Synthesis, Transduction

L-flow upregulates DDIAS expression via SENP2 S344 phosphorylation and ERK5 activation to suppress EC apoptosis: ( A ) the venn diagram illustrates the significant DEGs between the groups. ( B ) The heatmap displays the nine core genes, including DDIAS. ( C , left panel) Pretreatment with XMD8-92 (5 µM), an ERK5-specific inhibitor, suppresses L-flow-mediated upregulation of DDIAS expression in HUVECs after 24 h. ( C , right panel) The graphs present quantified data from 3 independent experiments (** p < 0.01, two-way ANOVA). ( D , left panel) HUVECs were overexpressed with DDIAS using the DDIAS plasmid or control plasmid, then exposed to IR for 24 h. The increased expression of cleaved caspase-3 induced by IR is reversed by DDIAS overexpression. ( D , right panel) The graphs present quantified data from 3 independent experiments (* p < 0.05, two-way ANOVA). “pCont” refers to the control plasmid, and “pDDIAS” refers to the DDIAS plasmid. ( E ) The scheme illustrates the mechanism of L-flow-induced SENP2 S344 phosphorylation in suppressing the EC pathophysiological stress response.

Journal: Frontiers in Cardiovascular Medicine

Article Title: Endothelial activation and fibrotic changes are impeded by laminar flow-induced CHK1-SENP2 activity through mechanisms distinct from endothelial-to-mesenchymal cell transition

doi: 10.3389/fcvm.2023.1187490

Figure Lengend Snippet: L-flow upregulates DDIAS expression via SENP2 S344 phosphorylation and ERK5 activation to suppress EC apoptosis: ( A ) the venn diagram illustrates the significant DEGs between the groups. ( B ) The heatmap displays the nine core genes, including DDIAS. ( C , left panel) Pretreatment with XMD8-92 (5 µM), an ERK5-specific inhibitor, suppresses L-flow-mediated upregulation of DDIAS expression in HUVECs after 24 h. ( C , right panel) The graphs present quantified data from 3 independent experiments (** p < 0.01, two-way ANOVA). ( D , left panel) HUVECs were overexpressed with DDIAS using the DDIAS plasmid or control plasmid, then exposed to IR for 24 h. The increased expression of cleaved caspase-3 induced by IR is reversed by DDIAS overexpression. ( D , right panel) The graphs present quantified data from 3 independent experiments (* p < 0.05, two-way ANOVA). “pCont” refers to the control plasmid, and “pDDIAS” refers to the DDIAS plasmid. ( E ) The scheme illustrates the mechanism of L-flow-induced SENP2 S344 phosphorylation in suppressing the EC pathophysiological stress response.

Article Snippet: SENP2 antibody (NBP1-31217) and β-actin antibody (NB600-532) were purchased from Novus Biologicals (Briarwood Ave, CO, USA).

Techniques: Expressing, Phospho-proteomics, Activation Assay, Plasmid Preparation, Control, Over Expression

Review

Structured Review

Images

Similar Products

Image Search Results