Journal: Nature Communications

Article Title: Improving erectile function in diabetic male mice by rescuing depalmitoylated FBP1 to reduce cavernosal lactate

doi: 10.1038/s41467-026-68443-y

Figure Lengend Snippet: a The interconversion between lactate and glucose. b , c Heatmap of transcriptome sequencing for key genes involved in glycolysis ( Hk2 , Pfkfb3 , Pklr , Ldha ) and gluconeogenesis ( Fbp1 , G6pc3 , Pck1 ) in mice and rats. n1, n2, n3 and N1, N2, N3 denote three independent samples from the control mouse and rat groups, respectively; t1, t2, t3 and T1, T2, T3 represent the corresponding three independent samples from the DMED mouse and rat groups, respectively. d The expression of FBP1 in each group based on single-cell data analysis of the human corpus cavernosum. e Fbp1 mRNA levels in the corpus cavernosum of normal and DMED mice ( n = 3). f , g Representational results and quantification of FBP1 immunohistochemical staining among Fbp1 +/+ , DMED- Fbp1 +/+ , Fbp1 −/+ and DMED- Fbp1 −/+ mice. Scale bars, 200 µm, n = 3. h The cavernosal lactate concentrations ( n = 3). i , j Representative images and quantification of ICP ( n = 3). k , l Morphology and quantification of the corpus cavernosum assessed by H&E staining ( n = 3). m , n Representative images and quantification of α -SMA (green) immunofluorescence staining. Scale bars, 200 µm, n = 3. o Cell viability of primary mouse CCSMCs in the low-concentration lactate and Fbp1 knockout groups ( n = 3). p Representative images of motility evaluated by Transwell migration assays. Scale bars, 100 µm. q The protein expressions of SM22 α , CALPONIN, VIMENTIN, and OSTEOPONTIN were detected by Western blot. r Cell viability in the high-concentration lactate and Fbp1 overexpression groups ( n = 3). s Transwell migration assays. Scale bars, 100 µm. t The protein expressions of SM22 α , CALPONIN, VIMENTIN, and OSTEOPONTIN in the high-concentration lactate and Fbp1 overexpression groups. Bar charts are presented as mean ± SD. All experiments were performed with at least three biologically independent replicates with consistent results, and the points represent individual biological samples. Unpaired two-sided Student’s t -test ( e ) and one-way ANOVA with Tukey’s post hoc test ( g , h , j , l , n , o , r ) were performed. Source data are provided as a Source Data file. DMED: diabetes mellitus-induced erectile dysfunction, NC normal control, ICP intracavernous pressure, CCSMC corpus cavernosum smooth muscle cell, FBP1 fructose-1,6-bisphosphatase 1.

Article Snippet: The primary antibodies used were as follows: α -SMA (# GB111364 , Servicebio, 1:1000), SM22 α (#60213, Proteintech, 1:5000), CALPONIN (#13938, Proteintech, 1:5000), VIMENTIN (#60330, Proteintech, 1:20,000), OSTEOPONIN (#83341, Proteintech, 1:1000), FBP1 (#12842, Proteintech, 1:500), H3K9me3 (#ab8898, Abcam, 1:1000), H3K27me3 (#ab6002, Abcam, 1:1000), SUV39H1 (#10574, Proteintech, 1:2000), SUV39H2 (#11338, Proteintech, 1:1000), SETDB1 (#66293, Proteintech, 1:20,000), SETDB2 (#ab13712, Abcam, 1:500), EZH1 (#ab263961, Abcam, 1:1000), EZH2 (#66476, Proteintech, 1:5000), β -ACTIN (#60008, Proteintech, 1:5000), CBX3 (#66446, Proteintech, 1:2000), CBX5 (#11831, Proteintech, 1:500), CBX1(#10241, Proteintech, 1:1000), ZDHHC13 (#24759, Proteintech, 1:500), FLAG (#66008, Proteintech, 1:5000), HA-tag (#51064, Proteintech, 1:5000), HIS-tag (#66005, Proteintech, 1:5000), AGK (#ab137616, Abcam, 1:1000), GST(#2622, Cell Signaling Technology,1:500), Histone H3 (#17168, Proteintech, 1:1000), LC3 (#14600, Proteintech, 1:1000), P62 (#18420, Proteintech, 1:1000), G6PC (#A21168, ABclonal, 1:2000), PCK1 (#GB11966, Servicebio, 1:500), Phospho-RPB1(Ser2) (#13499, Cell Signaling Technology,1:500), H3K4me3 (#39915, Proteintech, 1:1000), H3K27ac (#A22264, ABclonal, 1:5000), H2AK119ub (#8240, Cell Signaling Technology, 1:500), CRBN (#28494, Proteintech, 1:2000), Phospho-AKT (#66444, Proteintech, 1:1000), AKT (#10176, Proteintech, 1:1000), SOX9 (#67439, Proteintech, 1:5000), vWF (# GB120019 , Servicebio, 1:500), and Collagen I (#GB11022, Servicebio, 1:1000).

Techniques: Sequencing, Control, Expressing, Single Cell, Immunohistochemical staining, Staining, Immunofluorescence, Concentration Assay, Knock-Out, Migration, Western Blot, Over Expression

Journal: Nature Communications

Article Title: Improving erectile function in diabetic male mice by rescuing depalmitoylated FBP1 to reduce cavernosal lactate

doi: 10.1038/s41467-026-68443-y

Figure Lengend Snippet: a Histone methylation modifiers binding to the FBP1 promoter sequence identified from the ChIP-Atlas public database. b , c The ChIP-qPCR assay confirming the interaction between H3K9me3/H3K27me3 and Fbp1 in MOVAS cells ( n = 3). d , e The protein expressions of H3K9me3 and H3K27me3 in mice ( n = 3). f , g The protein expressions of methyltransferases related to H3K9me3 and H3K27me3 in mice ( n = 3). h , i Effects of Suv39h1 overexpression on H3K9me3 as well as on FBP1 protein and Fbp1 mRNA levels in MOVAS cells ( n = 3). j , k Effects of siRNA-mediated knockdown of Suv39h1 on H3K9me3 as well as on FBP1 protein and Fbp1 mRNA levels in MOVAS cells ( n = 3). l , m Effects of a Suv39h1 inhibitor (chaetocin, 25, 50 nM) on FBP1 protein and Fbp1 mRNA levels in MOVAS cells ( n = 3). n CBX3 binding to the Fbp1 promoter sequence identified from the ChIP-Atlas public database. o The ChIP-qPCR assay confirming the interaction between CBX3 and Fbp1 in MOVAS cells ( n = 3). p , q The protein expressions of CBX3 in mice ( n = 3). r , s Effects of Cbx3 overexpression on FBP1 protein and Fbp1 mRNA levels in MOVAS cells ( n = 3). t , u Effects of siRNA-mediated knockdown of Cbx3 on FBP1 protein and Fbp1 mRNA levels in MOVAS cells ( n = 3). v , w Effects of the H-PROTAC (1 μM, 2 μM) on FBP1 protein and Fbp1 mRNA levels in MOVAS cells ( n = 3). x The effects of exogenous CBX3 on FBP1 protein level in MOVAS cells. y Mechanism diagram. Bar charts are presented as mean ± SD. All experiments were performed with at least three biologically independent replicates with consistent results, and the points represent individual biological samples. Unpaired two-sided Student’s t -test ( b , c , e , g , i , q , s ) and one-way ANOVA with Tukey’s post hoc test ( k , m , o , u , w ) were performed. Source data are provided as a Source Data file. NC normal control, DMED diabetes mellitus-induced erectile dysfunction, FBP1 fructose-1,6- bisphosphatase 1, H3K9me3 histone H3 lysine 9 trimethylation, H3K27me3 histone H3 lysine 27 trimethylation, SUV39H1 suppressor of variegation 3-9 homolog 1, EZH2 enhancer of zeste homolog 2, EV empty vector, CBX3 chromobox protein homolog 3.

Article Snippet: The primary antibodies used were as follows: α -SMA (# GB111364 , Servicebio, 1:1000), SM22 α (#60213, Proteintech, 1:5000), CALPONIN (#13938, Proteintech, 1:5000), VIMENTIN (#60330, Proteintech, 1:20,000), OSTEOPONIN (#83341, Proteintech, 1:1000), FBP1 (#12842, Proteintech, 1:500), H3K9me3 (#ab8898, Abcam, 1:1000), H3K27me3 (#ab6002, Abcam, 1:1000), SUV39H1 (#10574, Proteintech, 1:2000), SUV39H2 (#11338, Proteintech, 1:1000), SETDB1 (#66293, Proteintech, 1:20,000), SETDB2 (#ab13712, Abcam, 1:500), EZH1 (#ab263961, Abcam, 1:1000), EZH2 (#66476, Proteintech, 1:5000), β -ACTIN (#60008, Proteintech, 1:5000), CBX3 (#66446, Proteintech, 1:2000), CBX5 (#11831, Proteintech, 1:500), CBX1(#10241, Proteintech, 1:1000), ZDHHC13 (#24759, Proteintech, 1:500), FLAG (#66008, Proteintech, 1:5000), HA-tag (#51064, Proteintech, 1:5000), HIS-tag (#66005, Proteintech, 1:5000), AGK (#ab137616, Abcam, 1:1000), GST(#2622, Cell Signaling Technology,1:500), Histone H3 (#17168, Proteintech, 1:1000), LC3 (#14600, Proteintech, 1:1000), P62 (#18420, Proteintech, 1:1000), G6PC (#A21168, ABclonal, 1:2000), PCK1 (#GB11966, Servicebio, 1:500), Phospho-RPB1(Ser2) (#13499, Cell Signaling Technology,1:500), H3K4me3 (#39915, Proteintech, 1:1000), H3K27ac (#A22264, ABclonal, 1:5000), H2AK119ub (#8240, Cell Signaling Technology, 1:500), CRBN (#28494, Proteintech, 1:2000), Phospho-AKT (#66444, Proteintech, 1:1000), AKT (#10176, Proteintech, 1:1000), SOX9 (#67439, Proteintech, 1:5000), vWF (# GB120019 , Servicebio, 1:500), and Collagen I (#GB11022, Servicebio, 1:1000).

Techniques: Methylation, Binding Assay, Sequencing, ChIP-qPCR, Over Expression, Knockdown, Control, Plasmid Preparation

Journal: Nature Communications

Article Title: Improving erectile function in diabetic male mice by rescuing depalmitoylated FBP1 to reduce cavernosal lactate

doi: 10.1038/s41467-026-68443-y

Figure Lengend Snippet: a – l The results of glucose consumption in MOVAS cells ( n = 3). m Effects of the H-PROTAC on FBP1 expression in MOVAS cells with Fbp1 knockout. n Effects of the chaetocin on FBP1 expression in MOVAS cells with Fbp1 knockout. o Effects of the EPZ6438 on FBP1 expression in MOVAS cells with Fbp1 knockout. p The cavernosal lactate concentrations ( n = 3). q , r Representative images and quantification of ICP ( n = 3). s , t Morphology and quantification of the corpus cavernosum assessed by H&E staining. Scale bars, 200 µm, n = 3. u Representative images of α -SMA (green) immunofluorescence staining. Scale bars, 200 µm. Bar charts are presented as mean ± SD. All experiments were performed with at least three biologically independent replicates with consistent results, and the points represent individual biological samples. Unpaired two-sided Student’s t -test ( a – l ) and one-way ANOVA with Tukey’s post hoc test ( p , r , t ) were performed. Source data are provided as a Source Data file. DMED diabetes mellitus-induced erectile dysfunction, ICP intracavernous pressure, FBP1 fructose-1,6-bisphosphatase 1, SUV39H1 suppressor of variegation 3-9 homolog 1, EZH2 enhancer of zeste homolog 2, CBX3 chromobox protein homolog 3.

Article Snippet: The primary antibodies used were as follows: α -SMA (# GB111364 , Servicebio, 1:1000), SM22 α (#60213, Proteintech, 1:5000), CALPONIN (#13938, Proteintech, 1:5000), VIMENTIN (#60330, Proteintech, 1:20,000), OSTEOPONIN (#83341, Proteintech, 1:1000), FBP1 (#12842, Proteintech, 1:500), H3K9me3 (#ab8898, Abcam, 1:1000), H3K27me3 (#ab6002, Abcam, 1:1000), SUV39H1 (#10574, Proteintech, 1:2000), SUV39H2 (#11338, Proteintech, 1:1000), SETDB1 (#66293, Proteintech, 1:20,000), SETDB2 (#ab13712, Abcam, 1:500), EZH1 (#ab263961, Abcam, 1:1000), EZH2 (#66476, Proteintech, 1:5000), β -ACTIN (#60008, Proteintech, 1:5000), CBX3 (#66446, Proteintech, 1:2000), CBX5 (#11831, Proteintech, 1:500), CBX1(#10241, Proteintech, 1:1000), ZDHHC13 (#24759, Proteintech, 1:500), FLAG (#66008, Proteintech, 1:5000), HA-tag (#51064, Proteintech, 1:5000), HIS-tag (#66005, Proteintech, 1:5000), AGK (#ab137616, Abcam, 1:1000), GST(#2622, Cell Signaling Technology,1:500), Histone H3 (#17168, Proteintech, 1:1000), LC3 (#14600, Proteintech, 1:1000), P62 (#18420, Proteintech, 1:1000), G6PC (#A21168, ABclonal, 1:2000), PCK1 (#GB11966, Servicebio, 1:500), Phospho-RPB1(Ser2) (#13499, Cell Signaling Technology,1:500), H3K4me3 (#39915, Proteintech, 1:1000), H3K27ac (#A22264, ABclonal, 1:5000), H2AK119ub (#8240, Cell Signaling Technology, 1:500), CRBN (#28494, Proteintech, 1:2000), Phospho-AKT (#66444, Proteintech, 1:1000), AKT (#10176, Proteintech, 1:1000), SOX9 (#67439, Proteintech, 1:5000), vWF (# GB120019 , Servicebio, 1:500), and Collagen I (#GB11022, Servicebio, 1:1000).

Techniques: Expressing, Knock-Out, Staining, Immunofluorescence

Journal: Nature Communications

Article Title: Improving erectile function in diabetic male mice by rescuing depalmitoylated FBP1 to reduce cavernosal lactate

doi: 10.1038/s41467-026-68443-y

Figure Lengend Snippet: a Analysis of all PTMs within ±25 amino acids around the G260 of FBP1. b , c ABE and Click-iT pull-down assay detecting the palmitoylation of FBP1 in MOVAS cells. d Prediction of potential FBP1 palmitoylation sites using CSS-Palm 4.0 software. e MOVAS cells were infected with lentiviruses containing expression cassettes of guide RNAs targeting different Zdhhc s. The ABE assay was used for detecting the palmitoylation status of FBP1. f Alphafold and PyMOL3 was used to conduct a visualization study of the molecular docking between ZDHHC13 and FBP1. g Antibodies to ZDHHC13 or FBP1 were used to perform co-immunoprecipitation experiments in MOVAS cells. h Confocal microscopy analysis of co-localization between ZDHHC13 (green) and FBP1 (red) in MOVAS cells. Scale bars, 15 µm. i Schematic diagram. j Western blotting analysis of ZDHHC13 GST-pulled down by FBP1 recombinant. k Heatmap of transcriptome sequencing of Zdhhc13 in normal and DMED mice. l Representational results of FBP1 immunohistochemical image. Scale bars, 100 µm. m , n FBP1 palmitoylation was examined in MOVAS or CCSMCs with Zdhhc 13 knockdown or overexpression. o MOVAS cells were transfected with the indicated plasmids for 48 h. The ABE assay was used to detect the palmitoylation level of FBP1. p The effect of ZDHHC13 C456S on FBP1 palmitoylation in MOVAS cells. q Endogenous Fbp1 were knocked out in MOVAS cells by CRISPR/Cas9. The ABE assay was used to detect the palmitoylation level of FBP1. r The palmitoylation analysis was performed by mixing purified His-FBP1-WT and His-FBP-C282S with purified GST-ZDHHC13-WT or GST-ZDHHC13-C456S in the presence of palmitoyl-alkyne-CoA. All experiments were performed with at least three biologically independent replicates with consistent results. Source data are provided as a Source Data file. PTM post-translational modification, FBP1 fructose-1,6-bisphosphatase 1, ABE acyl-biotinyl exchange, ZDHHC13 zinc finger DHHC-type containing 13, CCSMC corpus cavernosum smooth muscle cells.

Article Snippet: The primary antibodies used were as follows: α -SMA (# GB111364 , Servicebio, 1:1000), SM22 α (#60213, Proteintech, 1:5000), CALPONIN (#13938, Proteintech, 1:5000), VIMENTIN (#60330, Proteintech, 1:20,000), OSTEOPONIN (#83341, Proteintech, 1:1000), FBP1 (#12842, Proteintech, 1:500), H3K9me3 (#ab8898, Abcam, 1:1000), H3K27me3 (#ab6002, Abcam, 1:1000), SUV39H1 (#10574, Proteintech, 1:2000), SUV39H2 (#11338, Proteintech, 1:1000), SETDB1 (#66293, Proteintech, 1:20,000), SETDB2 (#ab13712, Abcam, 1:500), EZH1 (#ab263961, Abcam, 1:1000), EZH2 (#66476, Proteintech, 1:5000), β -ACTIN (#60008, Proteintech, 1:5000), CBX3 (#66446, Proteintech, 1:2000), CBX5 (#11831, Proteintech, 1:500), CBX1(#10241, Proteintech, 1:1000), ZDHHC13 (#24759, Proteintech, 1:500), FLAG (#66008, Proteintech, 1:5000), HA-tag (#51064, Proteintech, 1:5000), HIS-tag (#66005, Proteintech, 1:5000), AGK (#ab137616, Abcam, 1:1000), GST(#2622, Cell Signaling Technology,1:500), Histone H3 (#17168, Proteintech, 1:1000), LC3 (#14600, Proteintech, 1:1000), P62 (#18420, Proteintech, 1:1000), G6PC (#A21168, ABclonal, 1:2000), PCK1 (#GB11966, Servicebio, 1:500), Phospho-RPB1(Ser2) (#13499, Cell Signaling Technology,1:500), H3K4me3 (#39915, Proteintech, 1:1000), H3K27ac (#A22264, ABclonal, 1:5000), H2AK119ub (#8240, Cell Signaling Technology, 1:500), CRBN (#28494, Proteintech, 1:2000), Phospho-AKT (#66444, Proteintech, 1:1000), AKT (#10176, Proteintech, 1:1000), SOX9 (#67439, Proteintech, 1:5000), vWF (# GB120019 , Servicebio, 1:500), and Collagen I (#GB11022, Servicebio, 1:1000).

Techniques: Pull Down Assay, Software, Infection, Expressing, Immunoprecipitation, Confocal Microscopy, Western Blot, Recombinant, Sequencing, Immunohistochemical staining, Knockdown, Over Expression, Transfection, CRISPR, Purification, Modification

Journal: Nature Communications

Article Title: Improving erectile function in diabetic male mice by rescuing depalmitoylated FBP1 to reduce cavernosal lactate

doi: 10.1038/s41467-026-68443-y

Figure Lengend Snippet: a The cycloheximide (50 µg/ml) chase assay with protein extraction at 0, 2, 4, and 8 h, and then analyzed by Western blot. b Western blot analysis of cytoplasmic and nuclear proteins. c – n The glucose consumption, lactate production, ECAR and OCR of MOVAS cells in groups ( n = 3). o The cavernosal lactate concentrations ( n = 3). p , q Representative images and quantification of ICP ( n = 3). r , s Morphology and quantification of the corpus cavernosum assessed by H&E staining. Scale bars, 200 µm, n = 3. t Representative images of α -SMA (green) immunofluorescence staining. Scale bars, 100 µm. Bar charts are presented as mean ± SD. All experiments were performed with at least three biologically independent replicates with consistent results, and the points represent individual biological samples. Unpaired two-sided Student’s t -test were performed. Source data are provided as a Source Data file. CHX cycloheximide, FBP1 fructose-1,6-bisphosphatase 1, ZDHHC13 zinc finger DHHC-type containing 13, DMED diabetes mellitus-induced erectile dysfunction, ICP intracavernous pressure. ECAR extracellular acidification rate, OCR oxygen consumption rate, AAV adeno-associated virus.

Article Snippet: The primary antibodies used were as follows: α -SMA (# GB111364 , Servicebio, 1:1000), SM22 α (#60213, Proteintech, 1:5000), CALPONIN (#13938, Proteintech, 1:5000), VIMENTIN (#60330, Proteintech, 1:20,000), OSTEOPONIN (#83341, Proteintech, 1:1000), FBP1 (#12842, Proteintech, 1:500), H3K9me3 (#ab8898, Abcam, 1:1000), H3K27me3 (#ab6002, Abcam, 1:1000), SUV39H1 (#10574, Proteintech, 1:2000), SUV39H2 (#11338, Proteintech, 1:1000), SETDB1 (#66293, Proteintech, 1:20,000), SETDB2 (#ab13712, Abcam, 1:500), EZH1 (#ab263961, Abcam, 1:1000), EZH2 (#66476, Proteintech, 1:5000), β -ACTIN (#60008, Proteintech, 1:5000), CBX3 (#66446, Proteintech, 1:2000), CBX5 (#11831, Proteintech, 1:500), CBX1(#10241, Proteintech, 1:1000), ZDHHC13 (#24759, Proteintech, 1:500), FLAG (#66008, Proteintech, 1:5000), HA-tag (#51064, Proteintech, 1:5000), HIS-tag (#66005, Proteintech, 1:5000), AGK (#ab137616, Abcam, 1:1000), GST(#2622, Cell Signaling Technology,1:500), Histone H3 (#17168, Proteintech, 1:1000), LC3 (#14600, Proteintech, 1:1000), P62 (#18420, Proteintech, 1:1000), G6PC (#A21168, ABclonal, 1:2000), PCK1 (#GB11966, Servicebio, 1:500), Phospho-RPB1(Ser2) (#13499, Cell Signaling Technology,1:500), H3K4me3 (#39915, Proteintech, 1:1000), H3K27ac (#A22264, ABclonal, 1:5000), H2AK119ub (#8240, Cell Signaling Technology, 1:500), CRBN (#28494, Proteintech, 1:2000), Phospho-AKT (#66444, Proteintech, 1:1000), AKT (#10176, Proteintech, 1:1000), SOX9 (#67439, Proteintech, 1:5000), vWF (# GB120019 , Servicebio, 1:500), and Collagen I (#GB11022, Servicebio, 1:1000).

Techniques: Protein Extraction, Western Blot, Staining, Immunofluorescence, Virus

Journal: Nature Communications

Article Title: Improving erectile function in diabetic male mice by rescuing depalmitoylated FBP1 to reduce cavernosal lactate

doi: 10.1038/s41467-026-68443-y

Figure Lengend Snippet: a Schematic diagram of Fbp1 -C282S-LNP. b The average particle size, PDI encapsulation efficiency and zeta potential ( n = 3). c The representative images of canning electron microscopy. Scale bars, 50 nm. d , e FBP1 expression in CCSMCs assessed by Western blot ( n = 3). f Cell viability in CCSMCs ( n = 5). g – n The glucose consumption, lactate production, ECAR, and OCR of MOVAS cells in groups ( n = 3). o The cavernosal lactate concentrations ( n = 3). p , q Representative images and quantification of ICP ( n = 3). r , s Morphology and quantification of the corpus cavernosum assessed by H&E staining. Scale bars, 200 µm, n = 3. t , u Representative images and quantification of α -SMA (green) immunofluorescence staining. Scale bars, 100 µm, n = 3. v , w Representative images and quantification of Collagen I (red) immunofluorescence staining. Scale bars, 100 µm, n = 3. x , y The FBP1 protein expression and quantification ( n = 3). Bar charts are presented as mean ± SD. All experiments were performed with at least three biologically independent replicates with consistent results, and the points represent individual biological samples. The one-way ANOVA with Tukey’s post hoc test were performed. Source data are provided as a Source Data file. FBP1 fructose-1,6-bisphosphatase 1, PDI polydispersity index, LNP lipid nanoparticle, Col I Collagen I, DMED diabetes mellitus-induced erectile dysfunction, ICP intracavernous pressure, ECAR extracellular acidification rate, OCR oxygen consumption rate.

Article Snippet: The primary antibodies used were as follows: α -SMA (# GB111364 , Servicebio, 1:1000), SM22 α (#60213, Proteintech, 1:5000), CALPONIN (#13938, Proteintech, 1:5000), VIMENTIN (#60330, Proteintech, 1:20,000), OSTEOPONIN (#83341, Proteintech, 1:1000), FBP1 (#12842, Proteintech, 1:500), H3K9me3 (#ab8898, Abcam, 1:1000), H3K27me3 (#ab6002, Abcam, 1:1000), SUV39H1 (#10574, Proteintech, 1:2000), SUV39H2 (#11338, Proteintech, 1:1000), SETDB1 (#66293, Proteintech, 1:20,000), SETDB2 (#ab13712, Abcam, 1:500), EZH1 (#ab263961, Abcam, 1:1000), EZH2 (#66476, Proteintech, 1:5000), β -ACTIN (#60008, Proteintech, 1:5000), CBX3 (#66446, Proteintech, 1:2000), CBX5 (#11831, Proteintech, 1:500), CBX1(#10241, Proteintech, 1:1000), ZDHHC13 (#24759, Proteintech, 1:500), FLAG (#66008, Proteintech, 1:5000), HA-tag (#51064, Proteintech, 1:5000), HIS-tag (#66005, Proteintech, 1:5000), AGK (#ab137616, Abcam, 1:1000), GST(#2622, Cell Signaling Technology,1:500), Histone H3 (#17168, Proteintech, 1:1000), LC3 (#14600, Proteintech, 1:1000), P62 (#18420, Proteintech, 1:1000), G6PC (#A21168, ABclonal, 1:2000), PCK1 (#GB11966, Servicebio, 1:500), Phospho-RPB1(Ser2) (#13499, Cell Signaling Technology,1:500), H3K4me3 (#39915, Proteintech, 1:1000), H3K27ac (#A22264, ABclonal, 1:5000), H2AK119ub (#8240, Cell Signaling Technology, 1:500), CRBN (#28494, Proteintech, 1:2000), Phospho-AKT (#66444, Proteintech, 1:1000), AKT (#10176, Proteintech, 1:1000), SOX9 (#67439, Proteintech, 1:5000), vWF (# GB120019 , Servicebio, 1:500), and Collagen I (#GB11022, Servicebio, 1:1000).

Techniques: Encapsulation, Zeta Potential Analyzer, Electron Microscopy, Expressing, Western Blot, Staining, Immunofluorescence

Journal: Nature Communications

Article Title: Improving erectile function in diabetic male mice by rescuing depalmitoylated FBP1 to reduce cavernosal lactate

doi: 10.1038/s41467-026-68443-y

Figure Lengend Snippet: a Mechanisms of FBP1 dysfunction and lactate accumulation in DMED. H3K9me3-mediated repression of Fbp 1 transcription by SUV39H1/CBX3 (targeted by Chaetocin and H-PROTAC), H3K9me3-mediated repression of Fbp1 transcription by EZH2 (inhibited by EPZ6438), and ZDHHC13-mediated palmitoylation impairing FBP1 enzymatic function. b Production and intracavernosal administration of Fbp1 C282S-LNP reduces cavernous lactate levels and rescues erectile function in DMED mice. SUV39H1 suppressor of variegation 3-9 homolog 1, CBX3 chromobox protein homolog 3, FBP1 fructose-1,6-bisphosphatase 1, EZH2 enhancer of zeste homolog 2, ZDHHC13 zinc finger DHHC-type containing 13, LNP Lipid nanoparticle, DMED diabetes mellitus-induced erectile dysfunction, H3K9me3 histone H3 lysine 9 trimethylation, H3K27me3 histone H3 lysine 27 trimethylation.

Article Snippet: The primary antibodies used were as follows: α -SMA (# GB111364 , Servicebio, 1:1000), SM22 α (#60213, Proteintech, 1:5000), CALPONIN (#13938, Proteintech, 1:5000), VIMENTIN (#60330, Proteintech, 1:20,000), OSTEOPONIN (#83341, Proteintech, 1:1000), FBP1 (#12842, Proteintech, 1:500), H3K9me3 (#ab8898, Abcam, 1:1000), H3K27me3 (#ab6002, Abcam, 1:1000), SUV39H1 (#10574, Proteintech, 1:2000), SUV39H2 (#11338, Proteintech, 1:1000), SETDB1 (#66293, Proteintech, 1:20,000), SETDB2 (#ab13712, Abcam, 1:500), EZH1 (#ab263961, Abcam, 1:1000), EZH2 (#66476, Proteintech, 1:5000), β -ACTIN (#60008, Proteintech, 1:5000), CBX3 (#66446, Proteintech, 1:2000), CBX5 (#11831, Proteintech, 1:500), CBX1(#10241, Proteintech, 1:1000), ZDHHC13 (#24759, Proteintech, 1:500), FLAG (#66008, Proteintech, 1:5000), HA-tag (#51064, Proteintech, 1:5000), HIS-tag (#66005, Proteintech, 1:5000), AGK (#ab137616, Abcam, 1:1000), GST(#2622, Cell Signaling Technology,1:500), Histone H3 (#17168, Proteintech, 1:1000), LC3 (#14600, Proteintech, 1:1000), P62 (#18420, Proteintech, 1:1000), G6PC (#A21168, ABclonal, 1:2000), PCK1 (#GB11966, Servicebio, 1:500), Phospho-RPB1(Ser2) (#13499, Cell Signaling Technology,1:500), H3K4me3 (#39915, Proteintech, 1:1000), H3K27ac (#A22264, ABclonal, 1:5000), H2AK119ub (#8240, Cell Signaling Technology, 1:500), CRBN (#28494, Proteintech, 1:2000), Phospho-AKT (#66444, Proteintech, 1:1000), AKT (#10176, Proteintech, 1:1000), SOX9 (#67439, Proteintech, 1:5000), vWF (# GB120019 , Servicebio, 1:500), and Collagen I (#GB11022, Servicebio, 1:1000).

Techniques:

Journal: Journal of Virology

Article Title: FUSE Binding Protein 1 Facilitates Persistent Hepatitis C Virus Replication in Hepatoma Cells by Regulating Tumor Suppressor p53

doi: 10.1128/jvi.00729-15

Figure Lengend Snippet: Figure 1. FBP1 is specifically overexpressed in human HCC tumors with CHC background. (A). 677

Article Snippet: FBP1 shRNA lentiviral particles and P53 siRNA sense (GCA UGA ACC GGA 121 GGC CCA Utt) and antisense (5’-AUG GGC CUC CGG UUC AUG Ctt-3’) were purchased from Santa 122 Cruz Biotechnology Lentiviral particles expressing shRNAs targeting FBP1, p53, or BCCIP were 123 purchased from Santa Cruz Biotechnology (CA).

Techniques:

Journal: Journal of Virology

Article Title: FUSE Binding Protein 1 Facilitates Persistent Hepatitis C Virus Replication in Hepatoma Cells by Regulating Tumor Suppressor p53

doi: 10.1128/jvi.00729-15

Figure Lengend Snippet: Fig. 4. The downregulation of p53 and FBP1 have the opposite effect on p21-expression and HCV 716

Article Snippet: FBP1 shRNA lentiviral particles and P53 siRNA sense (GCA UGA ACC GGA 121 GGC CCA Utt) and antisense (5’-AUG GGC CUC CGG UUC AUG Ctt-3’) were purchased from Santa 122 Cruz Biotechnology Lentiviral particles expressing shRNAs targeting FBP1, p53, or BCCIP were 123 purchased from Santa Cruz Biotechnology (CA).

Techniques: Expressing

Journal: Journal of Virology

Article Title: FUSE Binding Protein 1 Facilitates Persistent Hepatitis C Virus Replication in Hepatoma Cells by Regulating Tumor Suppressor p53

doi: 10.1128/jvi.00729-15

Figure Lengend Snippet: Figure 7. FBP1 promotes HCV replication by regulating p53 and its regulatory proteins, TCTP, and 810

Article Snippet: FBP1 shRNA lentiviral particles and P53 siRNA sense (GCA UGA ACC GGA 121 GGC CCA Utt) and antisense (5’-AUG GGC CUC CGG UUC AUG Ctt-3’) were purchased from Santa 122 Cruz Biotechnology Lentiviral particles expressing shRNAs targeting FBP1, p53, or BCCIP were 123 purchased from Santa Cruz Biotechnology (CA).

Techniques:

Journal: Journal of Virology

Article Title: FUSE Binding Protein 1 Facilitates Persistent Hepatitis C Virus Replication in Hepatoma Cells by Regulating Tumor Suppressor p53

doi: 10.1128/jvi.00729-15

Figure Lengend Snippet: Fig. 8. The migration of FBP1-kd Huh7.5 cells is drastically reduced. 849

Article Snippet: FBP1 shRNA lentiviral particles and P53 siRNA sense (GCA UGA ACC GGA 121 GGC CCA Utt) and antisense (5’-AUG GGC CUC CGG UUC AUG Ctt-3’) were purchased from Santa 122 Cruz Biotechnology Lentiviral particles expressing shRNAs targeting FBP1, p53, or BCCIP were 123 purchased from Santa Cruz Biotechnology (CA).

Techniques: Migration

Journal: PLoS ONE

Article Title: Effects of intravenous AICAR (5-aminoimidazole-4-carboximide riboside) administration on insulin signaling and resistance in premature baboons, Papio sp .

doi: 10.1371/journal.pone.0208757

Figure Lengend Snippet: Summary of RT-PCR primers.

Article Snippet: FBP1 , Human , 80 , Life Technologies, Hs00983323_m1.

Techniques: Amplification

Journal: PLoS ONE

Article Title: Effects of intravenous AICAR (5-aminoimidazole-4-carboximide riboside) administration on insulin signaling and resistance in premature baboons, Papio sp .

doi: 10.1371/journal.pone.0208757

Figure Lengend Snippet: Relative mRNA content of (A) PPARGC1A , (B) INSR , (C) IRS1 , (D) G6PC3 , (E) AKT , (F) PCK1 , (G) FOXO1 , and (H) FBP1 in the liver of preterm baboons is shown for placebo and AICAR treated animals. Error bars represent ± standard error of the mean. *, p < .05, placebo vs AICAR, independent samples T-Test.

Article Snippet: FBP1 , Human , 80 , Life Technologies, Hs00983323_m1.

Techniques:

Journal: Redox Biology

Article Title: Far Upstream Binding Protein 1 (FUBP1) participates in translational regulation of Nrf2 protein under oxidative stress

doi: 10.1016/j.redox.2021.101906

Figure Lengend Snippet: FUBP1 peptides detected by LC-MS/MS.

Article Snippet: FUBP1 siRNA and control were purchased from Santa Cruz Biotechnology, Inc (sc-43760 and sc-37007) or were designed and synthesized as described [ ].

Techniques:

Journal: Redox Biology

Article Title: Far Upstream Binding Protein 1 (FUBP1) participates in translational regulation of Nrf2 protein under oxidative stress

doi: 10.1016/j.redox.2021.101906

Figure Lengend Snippet: Time Dependent FUBP1 Binding to Nrf2 mRNA. HeLa cells were treated with 100 μM H 2 O 2 for 10 min and harvested at indicated time point for in vitro binding using Nrf2 5′UTR as a probe (A), or for immunoprecipitation using antibodies against FUBP1 for detection of associated Nrf2 mRNA (B). The proteins bound to Nrf2 5′UTR probe were pull down for Western blot to detect FUBP1, with FUBP1 levels in total cell lysates serving as an input (A). The immunoprecipitates of FUBP1 were used for real time RT-PCR to detect Nrf2 mRNA, and the abundance of Nrf2 mRNA was calculated with ΔCT by comparing the copy number from the immunoprecipitates of FUBP1 group or IgG group to that of the average of IgG group at 0 time point. The results are from one experiment representative of three independent experiments. * indicates statistically significant difference between control versus the H 2 O 2 treated group (p < 0.05).

Article Snippet: FUBP1 siRNA and control were purchased from Santa Cruz Biotechnology, Inc (sc-43760 and sc-37007) or were designed and synthesized as described [ ].

Techniques: Binding Assay, In Vitro, Immunoprecipitation, Western Blot, Quantitative RT-PCR, Control

Journal: Redox Biology

Article Title: Far Upstream Binding Protein 1 (FUBP1) participates in translational regulation of Nrf2 protein under oxidative stress

doi: 10.1016/j.redox.2021.101906

Figure Lengend Snippet: H 2 O 2 Dose Dependent FUBP1 Binding to Nrf2 mRNA. HeLa cells were treated with H 2 O 2 for 10 mins at the indicated dose and harvested at 1 hour after for in vitro binding using Nrf2 5′UTR as a probe (A) or for immunoprecipitation using antibodies against FUBP1 for detection of associated Nrf2 mRNA (B), as described in .

Article Snippet: FUBP1 siRNA and control were purchased from Santa Cruz Biotechnology, Inc (sc-43760 and sc-37007) or were designed and synthesized as described [ ].

Techniques: Binding Assay, In Vitro, Immunoprecipitation

Journal: Redox Biology

Article Title: Far Upstream Binding Protein 1 (FUBP1) participates in translational regulation of Nrf2 protein under oxidative stress

doi: 10.1016/j.redox.2021.101906

Figure Lengend Snippet: Recombinant FUBP1 Is Capable of Nrf2 5′UTR Binding. EMSA was performed using in vitro transcribed Nrf2 5′UTR probe and recombinant FUBP1 protein as described in the Methods.

Article Snippet: FUBP1 siRNA and control were purchased from Santa Cruz Biotechnology, Inc (sc-43760 and sc-37007) or were designed and synthesized as described [ ].

Techniques: Recombinant, Binding Assay, In Vitro

Journal: Redox Biology

Article Title: Far Upstream Binding Protein 1 (FUBP1) participates in translational regulation of Nrf2 protein under oxidative stress

doi: 10.1016/j.redox.2021.101906

Figure Lengend Snippet: FUBP1 Is Required for Nrf2 Protein Induction and Nrf2 5′UTR Activation. FUBP1 siRNA or negative control was introduced to HeLa cells at 72 hours prior to H 2 O 2 treatment. Cells were harvested at 1 hour after 10 min of 100 μM H 2 O 2 treatment, for Western blot to detect FUBP1 or Nrf2 protein from total cell lysates using GAPDH as a loading control (A, B). FUBP1 siRNA or negative control was cotransfected with pRF bicistronic vector of Nrf2 5′UTR in HeLa cells. At 72 hours after, cells were treated with H 2 O 2 for measurements of luciferases at 1 hour after (C). The results of one experiment representative of three are shown (A, C), or are summarized as average ± SD of Nrf2 band intensity over that of GAPDH from three experiments (B). * indicates significant difference between control versus the H 2 O 2 treated group (p < 0.05), whereas # indicates significant difference between two H 2 O 2 treated groups with FUBP1 siRNA versus with control siRNA (p < 0.05).

Article Snippet: FUBP1 siRNA and control were purchased from Santa Cruz Biotechnology, Inc (sc-43760 and sc-37007) or were designed and synthesized as described [ ].

Techniques: Activation Assay, Negative Control, Western Blot, Control, Plasmid Preparation

Journal: Redox Biology

Article Title: Far Upstream Binding Protein 1 (FUBP1) participates in translational regulation of Nrf2 protein under oxidative stress

doi: 10.1016/j.redox.2021.101906

Figure Lengend Snippet: Lack of Time Dependent Nuclear to Cytoplasmic Translocation of FUBP1. Hela cells were treated with 100 μM H 2 O 2 for 10 minutes and subsequently cultured in fresh DMEM containing 0.5% FBS for indicated time point before harvesting for total cell lysates or fractionation into cytosolic and nuclear extracts. The level of FUBP1 protein was determined by Western Blot. Lamin B1 was used as a loading control for nuclear fraction, whereas GAPDH was used as a loading control for cytosolic or total proteins. The bar graphs represent average ± SD of FUBP1 band intensity over that of corresponding loading control from three independent experiments. * indicates statistically significant difference between control versus the H 2 O 2 treated group (p < 0.05).

Article Snippet: FUBP1 siRNA and control were purchased from Santa Cruz Biotechnology, Inc (sc-43760 and sc-37007) or were designed and synthesized as described [ ].

Techniques: Translocation Assay, Cell Culture, Fractionation, Western Blot, Control

Journal: Redox Biology

Article Title: Far Upstream Binding Protein 1 (FUBP1) participates in translational regulation of Nrf2 protein under oxidative stress

doi: 10.1016/j.redox.2021.101906

Figure Lengend Snippet: Lack of Dose Dependent Nuclear to Cytoplasmic Translocation of FUBP1. Hela cells were treated with 0, 100, 200 or 300 μM H 2 O 2 for 10 minutes and cultured in freshly changed DMEM containing 0.5% FBS for another 1 hour. Cells were harvested for total cell lysates or fractionated into cytosolic and nuclear extracts for Western blot as described in .

Article Snippet: FUBP1 siRNA and control were purchased from Santa Cruz Biotechnology, Inc (sc-43760 and sc-37007) or were designed and synthesized as described [ ].

Techniques: Translocation Assay, Cell Culture, Western Blot

Journal: Redox Biology

Article Title: Far Upstream Binding Protein 1 (FUBP1) participates in translational regulation of Nrf2 protein under oxidative stress

doi: 10.1016/j.redox.2021.101906

Figure Lengend Snippet: Immunocytochemistry Confirmation of the Lack of Nuclear to Cytoplasmic Translocation of FUBP1. Hela cells were treated with 0, 100 or 200 μM H 2 O 2 for 10 minutes and incubated 1 hour in fresh DMEM containing 0.5% FBS. Cells were then processed for immunocytochemistry to stain for FUBP1 protein using Alexa Fluor 488 conjugated secondary antibody for visualization with a 63× lens (A). The bar graphs showed the mean fluorescence intensity (MFI) of cytosolic versus whole cell area (B), or nuclear versus whole cell area (C) as average ± SD from 12 different fields chosen randomly for quantification using Image J. * indicates significant different between Control versus H 2 O 2 treated group by student's t -test (p < 0.05).

Article Snippet: FUBP1 siRNA and control were purchased from Santa Cruz Biotechnology, Inc (sc-43760 and sc-37007) or were designed and synthesized as described [ ].

Techniques: Immunocytochemistry, Translocation Assay, Incubation, Staining, Fluorescence, Control

Journal: Redox Biology

Article Title: Far Upstream Binding Protein 1 (FUBP1) participates in translational regulation of Nrf2 protein under oxidative stress

doi: 10.1016/j.redox.2021.101906

Figure Lengend Snippet: Time and Dose Dependent Increase of FUBP1 Association with Ribosomes. Hela cells were treated with 100 μM H 2 O 2 for 10 min before harvesting at indicate time points (A) or were treated with various doses of H 2 O 2 for 10 min before harvesting at 60 min after (B). Cells were lysed for total ribosome isolation using sucrose cushion and ultracentrifugation as described in the methods. Ribosomal proteins were resolved by SDS-PAGE for Western blot to detect FUBP1 protein using S6 as a loading control. The bar graphs showed average ± SD of FUBP1 band intensity over that of corresponding loading control from three independent experiments. * indicates significant different between control versus the H 2 O 2 treated group (p < 0.05).

Article Snippet: FUBP1 siRNA and control were purchased from Santa Cruz Biotechnology, Inc (sc-43760 and sc-37007) or were designed and synthesized as described [ ].

Techniques: Isolation, SDS Page, Western Blot, Control

Journal: Redox Biology

Article Title: Far Upstream Binding Protein 1 (FUBP1) participates in translational regulation of Nrf2 protein under oxidative stress

doi: 10.1016/j.redox.2021.101906

Figure Lengend Snippet: Presence of FUBP1 in the 40/43S Ribosomal Fraction. Hela cells were treated with 100 μM H 2 O 2 for 10 min and harvested 1 hour after for isolation of ribosomes and separation of ribosomal subunits using a fractionator as described in the Methods. The proteins collected in the fractions between 8 and 21 min were used for Western blot to detect indicated proteins.

Article Snippet: FUBP1 siRNA and control were purchased from Santa Cruz Biotechnology, Inc (sc-43760 and sc-37007) or were designed and synthesized as described [ ].

Techniques: Isolation, Western Blot

Journal: Redox Biology

Article Title: Far Upstream Binding Protein 1 (FUBP1) participates in translational regulation of Nrf2 protein under oxidative stress

doi: 10.1016/j.redox.2021.101906

Figure Lengend Snippet: Immunoprecipitation of FUBP1 for Detection of eIFs. Hela cells were treated with 100 μM H 2 O 2 for 10 minutes and lysed in RIPA buffer 1 hour after for immunoprecipitation. FUBP1 was captured and pulled down from cell lysate by anti-FUBP1 antibody and agarose-protein A/G beads. Mouse IgG was used as a control for immunoprecipitation. Protein aliquots from total cell lysates were used as input or loading control. Immunoprecipitated proteins and input were resolved by SDS-PAGE gel for detection of binding proteins as indicated.

Article Snippet: FUBP1 siRNA and control were purchased from Santa Cruz Biotechnology, Inc (sc-43760 and sc-37007) or were designed and synthesized as described [ ].

Techniques: Immunoprecipitation, Control, SDS Page, Binding Assay

Journal: Journal of Virology

Article Title: FUSE Binding Protein 1 Facilitates Persistent Hepatitis C Virus Replication in Hepatoma Cells by Regulating Tumor Suppressor p53

doi: 10.1128/jvi.00729-15

Figure Lengend Snippet: Figure 1. FBP1 is specifically overexpressed in human HCC tumors with CHC background. (A). 677

Article Snippet: FBP1 shRNA lentiviral particles and P53 siRNA sense (GCA UGA ACC GGA 121 GGC CCA Utt) and antisense (5’-AUG GGC CUC CGG UUC AUG Ctt-3’) were purchased from Santa 122 Cruz Biotechnology Lentiviral particles expressing shRNAs targeting FBP1, p53, or BCCIP were 123 purchased from Santa Cruz Biotechnology (CA).

Techniques:

Journal: Journal of Virology

Article Title: FUSE Binding Protein 1 Facilitates Persistent Hepatitis C Virus Replication in Hepatoma Cells by Regulating Tumor Suppressor p53

doi: 10.1128/jvi.00729-15

Figure Lengend Snippet: Fig. 4. The downregulation of p53 and FBP1 have the opposite effect on p21-expression and HCV 716

Article Snippet: FBP1 shRNA lentiviral particles and P53 siRNA sense (GCA UGA ACC GGA 121 GGC CCA Utt) and antisense (5’-AUG GGC CUC CGG UUC AUG Ctt-3’) were purchased from Santa 122 Cruz Biotechnology Lentiviral particles expressing shRNAs targeting FBP1, p53, or BCCIP were 123 purchased from Santa Cruz Biotechnology (CA).

Techniques: Expressing

Journal: Journal of Virology

Article Title: FUSE Binding Protein 1 Facilitates Persistent Hepatitis C Virus Replication in Hepatoma Cells by Regulating Tumor Suppressor p53

doi: 10.1128/jvi.00729-15

Figure Lengend Snippet: Figure 7. FBP1 promotes HCV replication by regulating p53 and its regulatory proteins, TCTP, and 810

Article Snippet: FBP1 shRNA lentiviral particles and P53 siRNA sense (GCA UGA ACC GGA 121 GGC CCA Utt) and antisense (5’-AUG GGC CUC CGG UUC AUG Ctt-3’) were purchased from Santa 122 Cruz Biotechnology Lentiviral particles expressing shRNAs targeting FBP1, p53, or BCCIP were 123 purchased from Santa Cruz Biotechnology (CA).

Techniques:

Journal: Journal of Virology

Article Title: FUSE Binding Protein 1 Facilitates Persistent Hepatitis C Virus Replication in Hepatoma Cells by Regulating Tumor Suppressor p53

doi: 10.1128/jvi.00729-15

Figure Lengend Snippet: Fig. 8. The migration of FBP1-kd Huh7.5 cells is drastically reduced. 849

Article Snippet: FBP1 shRNA lentiviral particles and P53 siRNA sense (GCA UGA ACC GGA 121 GGC CCA Utt) and antisense (5’-AUG GGC CUC CGG UUC AUG Ctt-3’) were purchased from Santa 122 Cruz Biotechnology Lentiviral particles expressing shRNAs targeting FBP1, p53, or BCCIP were 123 purchased from Santa Cruz Biotechnology (CA).

Techniques: Migration