Journal: The EMBO Journal

Article Title: The disulfide catalyst QSOX1 maintains the colon mucosal barrier by regulating Golgi glycosyltransferases

doi: 10.15252/embj.2022111869

Figure Lengend Snippet:

Article Snippet: Rabbit anti St3Gal1 , Aviva Systems Biology , Cat# ARP45410_P050.

Techniques: Plasmid Preparation, Recombinant, Expressing, Cell Culture, DNA Extraction

Journal: International Journal of Gynaecology and Obstetrics

Article Title: Targeting the ST3 beta‐galactoside alpha‐2,3‐sialyltransferase 1 ( ST3Gal1 ) as a potential therapeutic strategy to overcome anti‐ VEGF resistance in endometrial cancer

doi: 10.1002/ijgo.70292

Figure Lengend Snippet: Functional impact of ST3 beta‐galactoside alpha‐2,3‐sialyltransferase 1 (ST3Gal1) knockdown (KD) on vascular endothelial growth factor‐A (VEGF‐A) Signaling and epithelial–mesenchymal transition (EMT) in endometrial cancer (EC). (a) ST3Gal1 mRNA expression in RL95‐2 and HEC‐1B cells following ST3Gal1 KD (KD#1, KD#2) compared with scrambled control (SC). Protein expression levels of ST3Gal1 and VEGF‐A are shown using Western blot. (b) Western blot analysis of EMT markers (E‐cadherin, N‐cadherin, vimentin, α‐SMA) in RL95‐2 and HEC‐1B cells following ST3Gal1 KD. Bottom panels: Representative Transwell invasion assays of control (SC) and ST3Gal1‐KD cells. (c) Duolink proximity ligation assay (PLA) demonstrating ST3Gal1 and VEGF‐A co‐expression in EC cells following ST3Gal1 KD (KD#1, KD#2) compared with scrambled control (SC). Red spots indicate protein–protein interactions, and DAPI (blue) marks nuclei. Quantification of interactions is shown on the right. (d) Duolink PLA demonstrating ST3Gal1 and VEGF‐A interactions in EC tissues, with increased interaction in tumors with >1/2 myometrial invasion compared with those with <1/2 myometrial invasion. Quantification of ST3Gal1/VEGF‐A co‐expression is shown on the right. Relative quantification is performed using ImageJ software. (e) Immunoprecipitation (IP) of VEGF‐A in RL95‐2 cells. ST3Gal1 KD reduces the VEGF‐A–ST3Gal1 interaction, as shown by decreased VEGF‐A levels in IP products compared with SC shRNA. Co‐immunoprecipitation (Co‐IP) of VEGF‐A. ST3Gal1‐KD reduces ST3Gal1 binding in VEGF‐A immunoprecipitates, indicating disruption of their interaction. (f) Peanut agglutinin (PNA) pull‐down assays in RL95‐2 and HEC‐1B cells demonstrated that ST3Gal1 KD reduced VEGF‐A sialylation, as evidenced by increased PNA binding in KD cells versus SC controls.

Article Snippet: Primary antibodies including ST3Gal1, VEGF‐A, E‐cadherin, N‐cadherin, vimentin, and α‐SMA (iREAL, ProteinTech, ABclonal, Hsinchu City, Taiwan) were utilized to assess EMT.

Techniques: Functional Assay, Knockdown, Expressing, Control, Western Blot, Proximity Ligation Assay, Protein-Protein interactions, Quantitative Proteomics, Software, Immunoprecipitation, shRNA, Co-Immunoprecipitation Assay, Binding Assay, Disruption

Journal: International Journal of Gynaecology and Obstetrics

Article Title: Targeting the ST3 beta‐galactoside alpha‐2,3‐sialyltransferase 1 ( ST3Gal1 ) as a potential therapeutic strategy to overcome anti‐ VEGF resistance in endometrial cancer

doi: 10.1002/ijgo.70292

Figure Lengend Snippet: In vitro evaluation of the effect of soyasaponin I (SsaI), bevacizumab, and their combination on endometrial cancer (EC) cells. (a) Colony formation assay showing the effect of increasing concentrations of SsaI (dimethyl sulfoxide [DMSO], 25, 50, and 100 μM) on RL95‐2 and HEC‐1B cell proliferation. Quantification of colony number is presented on the right ( P < 0.05). (b) Western blot analysis of ST3 beta‐galactoside alpha‐2,3‐sialyltransferase 1 (ST3Gal1), vascular endothelial growth factor‐A (VEGF‐A), and epithelial–mesenchymal transition (EMT) markers (E‐cadherin, N‐cadherin, vimentin, and α‐SMA) in RL95‐2 and HEC‐1B cells treated with increasing concentrations of SsaI. glyceraldehyde‐3‐phosphate dehydrogenase (GAPDH) served as a loading control. (c) Duolink proximity ligation assay demonstrating ST3Gal1 and VEGF‐A co‐expression in EC cells. Red spots indicate protein–protein interactions, and DAPI (blue) marks the nucleus. Quantification of ST3Gal1/VEGF‐A interactions is shown on the top ( P < 0.001). (d) Transwell invasion assay of RL95‐2 and HEC‐1B cells treated with DMSO, SsaI, bevacizumab, or SsaI + bevacizumab. Cells were stained with crystal violet. Quantification of relative invasion is shown on the right. ( P < 0.05, * P < 0.01, ** P < 0.001). (e) Wound‐healing assay performed on RL95‐2 and HEC‐1B cells treated with DMSO, SsaI, bevacizumab, or SsaI + bevacizumab. Representative images of wound closure at 48 hours are shown. Quantification of wound closure rate is presented on the right ( P < 0.05, * P < 0.01, ** P < 0.001).

Article Snippet: Primary antibodies including ST3Gal1, VEGF‐A, E‐cadherin, N‐cadherin, vimentin, and α‐SMA (iREAL, ProteinTech, ABclonal, Hsinchu City, Taiwan) were utilized to assess EMT.

Techniques: In Vitro, Colony Assay, Western Blot, Control, Proximity Ligation Assay, Expressing, Protein-Protein interactions, Transwell Invasion Assay, Staining, Wound Healing Assay

Journal: International Journal of Gynaecology and Obstetrics

Article Title: Targeting the ST3 beta‐galactoside alpha‐2,3‐sialyltransferase 1 ( ST3Gal1 ) as a potential therapeutic strategy to overcome anti‐ VEGF resistance in endometrial cancer

doi: 10.1002/ijgo.70292

Figure Lengend Snippet: In vivo evaluation of soyasaponin I (SsaI) and bevacizumab treatment on endometrial cancer (EC) using RL95‐2 and HEC‐1B xenografts. (a) Schematic representation of the xenograft study. Created using BioRender.com . (b) Tumor volume growth curves over time for RL95‐2 and HEC‐1B xenografts in mice treated with control (black), SsaI (red), bevacizumab (BEV; blue), or the combination of SsaI and bevacizumab (SsaI + BEV; green) over the course of the experiment. (c) Body weight measurement of RL95‐2 and HEC‐1B xenograft‐bearing nude mice treated with control (black), SsaI (red), bevacizumab (BEV; blue), or the combination of SsaI and bevacizumab (green) over the course of the experiment. (d) Gross images of the harvested RL95‐2 and HEC‐1B xenograft tumors. (e) Tumor weights at the time of harvest. (f) Immunohistochemistry (IHC) analysis of ST3 beta‐galactoside alpha‐2,3‐sialyltransferase 1 (ST3Gal1), vascular endothelial growth factor‐A (VEGF‐A), and CD31 expression, along with ST3Gal1/VEGF‐A dual staining and Duolink proximity ligation assay (PLA) assays, was performed to compare the combination treatment with the control group. (f) Western blot analysis of ST3Gal1, VEGF‐A, and epithelial–mesenchymal transition (EMT) markers (E‐cadherin, N‐cadherin, vimentin, and α‐SMA) in RL95‐2 and HEC‐1B xenografts tumor cells after sacrifice.

Article Snippet: Primary antibodies including ST3Gal1, VEGF‐A, E‐cadherin, N‐cadherin, vimentin, and α‐SMA (iREAL, ProteinTech, ABclonal, Hsinchu City, Taiwan) were utilized to assess EMT.

Techniques: In Vivo, Control, Immunohistochemistry, Expressing, Staining, Proximity Ligation Assay, Western Blot

Journal: Cancer cell international

Article Title: Comprehensive analysis of α2,3-sialyltransferases as prognostic biomarkers and immunotherapy targets in kidney renal clear cell carcinoma.

doi: 10.1186/s12935-025-03640-1

Figure Lengend Snippet: Fig. 6 ST3Gal5 knockdown inhibits the tumor growth of KIRC cells in vivo. (A) Morphological observation of tumor formation. (B) The tumor weight of the NC group and ST3Gal5-KD group, n = 5 per group. (C) The tumor volumes of the NC group and ST3Gal5-KD group. (D) The protein expression of ST3Gal5 in tumor tissues of NC and ST3Gal5 groups. (E) The mRNA level of ST3Gal5 in tumor tissues of NC and ST3Gal5 groups. (F) The H&E staining and the protein expression of ST3Gal5, PCNA and Ki67 were analyzed by IHC staining. *p < 0.05, **p < 0.01, ****p < 0.0001

Article Snippet: The antibodies were used for IHC, such as ST3Gal5 (Proteintech, 14614-1-AP, 1:200), ST3Gal1 (Abcam, ab96129, 1:100), PCNA (Proteintech, 10205-2-AP, 1:200) and Ki67 (Cell Signaling Technology, 12202S, 1:200).

Techniques: Knockdown, In Vivo, Expressing, Staining, Immunohistochemistry