Journal: Cells

Article Title: Silencing Heat Shock Protein 27 Inhibits the Progression and Metastasis of Colorectal Cancer (CRC) by Maintaining the Stability of Stromal Interaction Molecule 1 (STIM1) Proteins

doi: 10.3390/cells7120262

Figure Lengend Snippet: Primer sequences used QPCR analysis with gene name.

Article Snippet: For determination of the association of HSP27 and STIM1 expression levels, two consecutive formalin-fixed paraffin-embedded tissue microarray sections purchased from SuperBioChips Laboratories (catalog no. CDA3, Seoul, Korea) were stained with HSP27 and STIM1 (catalog no. HPA012123, 1:200, Atlas Antibodies AB, AlbaNova University Center, Stockholm, Sweden) by immunohistochemistry using the aforementioned protocol.

Techniques: Sequencing

Journal: Cells

Article Title: Silencing Heat Shock Protein 27 Inhibits the Progression and Metastasis of Colorectal Cancer (CRC) by Maintaining the Stability of Stromal Interaction Molecule 1 (STIM1) Proteins

doi: 10.3390/cells7120262

Figure Lengend Snippet: HSP27 increased the STIM1 protein levels in CRC cells. ( a ) QPCR was used to determine the STIM1 mRNA levels, and the levels were normalized to the GAPDH level. ( b , c and d ) Protein extracts prepared from the indicated cell lines were subjected to western blot analysis for STIM1 or Orai1. GAPDH was used as an internal control. Data are representative of three independent experiments. Values are the mean ± SD of three independent experiments. ** p < 0.01.

Article Snippet: For determination of the association of HSP27 and STIM1 expression levels, two consecutive formalin-fixed paraffin-embedded tissue microarray sections purchased from SuperBioChips Laboratories (catalog no. CDA3, Seoul, Korea) were stained with HSP27 and STIM1 (catalog no. HPA012123, 1:200, Atlas Antibodies AB, AlbaNova University Center, Stockholm, Sweden) by immunohistochemistry using the aforementioned protocol.

Techniques: Western Blot, Control

Journal: Cells

Article Title: Silencing Heat Shock Protein 27 Inhibits the Progression and Metastasis of Colorectal Cancer (CRC) by Maintaining the Stability of Stromal Interaction Molecule 1 (STIM1) Proteins

doi: 10.3390/cells7120262

Figure Lengend Snippet: HSP27 prevented STIM1 degradation by directly binding to STIM1. ( a , b ) Scrambled control or HSP27KD cells were treated with cycloheximide (CHX), MG132 or PYR-41. Whole cell lysates were immunoblotted for STIM1 and HSP27. GAPDH was used as an internal control. ( c ) The possibility of direct protein-protein interactions was examined by immunoprecipitation (IP). All the experiments were independently performed at least 3 times.

Article Snippet: For determination of the association of HSP27 and STIM1 expression levels, two consecutive formalin-fixed paraffin-embedded tissue microarray sections purchased from SuperBioChips Laboratories (catalog no. CDA3, Seoul, Korea) were stained with HSP27 and STIM1 (catalog no. HPA012123, 1:200, Atlas Antibodies AB, AlbaNova University Center, Stockholm, Sweden) by immunohistochemistry using the aforementioned protocol.

Techniques: Binding Assay, Control, Protein-Protein interactions, Immunoprecipitation

Journal: Cells

Article Title: Silencing Heat Shock Protein 27 Inhibits the Progression and Metastasis of Colorectal Cancer (CRC) by Maintaining the Stability of Stromal Interaction Molecule 1 (STIM1) Proteins

doi: 10.3390/cells7120262

Figure Lengend Snippet: HSP27 promoted STIM1 oligomerization in DLD-1 cells. Scrambled control or HSP27KD DLD cells were seeded into coverslips and then treated with vehicle or TG for 15 min. Cells were fixed, and the distribution of STIM1 was detected by immunocytochemical staining. Confocal microscopy was applied to observe the distribution of STIM1 (green). Nuclei were identified by DAPI. All experiments were independently performed at least 3 times.

Article Snippet: For determination of the association of HSP27 and STIM1 expression levels, two consecutive formalin-fixed paraffin-embedded tissue microarray sections purchased from SuperBioChips Laboratories (catalog no. CDA3, Seoul, Korea) were stained with HSP27 and STIM1 (catalog no. HPA012123, 1:200, Atlas Antibodies AB, AlbaNova University Center, Stockholm, Sweden) by immunohistochemistry using the aforementioned protocol.

Techniques: Control, Staining, Confocal Microscopy

Journal: Cells

Article Title: Silencing Heat Shock Protein 27 Inhibits the Progression and Metastasis of Colorectal Cancer (CRC) by Maintaining the Stability of Stromal Interaction Molecule 1 (STIM1) Proteins

doi: 10.3390/cells7120262

Figure Lengend Snippet: The association between HSP27 and STIM1 expression. ( a ) The scatterplot of H-scores of HSP27 and the corresponding STIM1 expression displayed a positive correlation (correlation coefficient = 0.416, p = 0.003). ( b ) A case of colon adenocarcinoma with a high HSP27 H-score displayed a high STIM1 H-score. ( c ) A case of colon adenocarcinoma with a low HSP27 H-score displayed a low STIM1 H-score.

Article Snippet: For determination of the association of HSP27 and STIM1 expression levels, two consecutive formalin-fixed paraffin-embedded tissue microarray sections purchased from SuperBioChips Laboratories (catalog no. CDA3, Seoul, Korea) were stained with HSP27 and STIM1 (catalog no. HPA012123, 1:200, Atlas Antibodies AB, AlbaNova University Center, Stockholm, Sweden) by immunohistochemistry using the aforementioned protocol.

Techniques: Expressing

Journal: Cells

Article Title: Silencing Heat Shock Protein 27 Inhibits the Progression and Metastasis of Colorectal Cancer (CRC) by Maintaining the Stability of Stromal Interaction Molecule 1 (STIM1) Proteins

doi: 10.3390/cells7120262

Figure Lengend Snippet: The proposed model for the role of HSP27 in CRC progression. HSP27 may interact with STIM1 to maintain the stability of STIM1. Silencing HSP27 caused a reduction of STIM1 to regulate the growth activity and metastasis ability on CRC.

Article Snippet: For determination of the association of HSP27 and STIM1 expression levels, two consecutive formalin-fixed paraffin-embedded tissue microarray sections purchased from SuperBioChips Laboratories (catalog no. CDA3, Seoul, Korea) were stained with HSP27 and STIM1 (catalog no. HPA012123, 1:200, Atlas Antibodies AB, AlbaNova University Center, Stockholm, Sweden) by immunohistochemistry using the aforementioned protocol.

Techniques: Activity Assay

Journal: Frontiers in Cellular Neuroscience

Article Title: Huntingtin-Associated Protein 1A Regulates Store-Operated Calcium Entry in Medium Spiny Neurons From Transgenic YAC128 Mice, a Model of Huntington’s Disease

doi: 10.3389/fncel.2018.00381

Figure Lengend Snippet: Expression levels of proteins that are involved in SOCE in SK-N-SH Htt138Q HAP1A. (A–D) Expression levels of transient receptor potential channel type 1 (TRPC1) (A) , Orai1 (B) , STIM1 (C) and STIM2 (D) proteins (normalized to α-tubulin) in SK-N-SH Htt138Q cotransfected with GFP (black bars) or HAP1A (red bars). On the top of each panel, the representative Western blots are shown. On the bottom of each panel, the expression levels of proteins are plotted as mean ± SEM. * p < 0.05, significant difference in expression level. ns, not significant. The number of tested lysates is shown above the bars.

Article Snippet: For STIM1 detection, the PVDF membrane was treated with the primary monoclonal anti-STIM1 antibody (1:250; catalog no. 610954, BD Bioscience) and peroxidase-conjugated goat anti-mouse IgG heavy-chain constant region secondary antibody (1:30,000; catalog no. A0168, Sigma).

Techniques: Expressing, Western Blot

Journal: Poultry Science

Article Title: Mechanism of Scutellaria baicalensis extracellular vesicles in attenuating Mycoplasma gallisepticum -induced inflammation via TRPC1 - STIM1/ORAI1 channel inhibition

doi: 10.1016/j.psj.2026.106773

Figure Lengend Snippet: Effects of STIM1 expression inhibition on MG-induced inflammatory damage, endoplasmic reticulum stress, calcium channel-associated proteins, and calcium ion accumulation in HD-11 cells. (A) Fluorescence microscopy images of HD-11 cells transfected with FAM-labelled siRNA. (B) Knockdown efficiency of three siRNAs at the mRNA level. (C) Knockdown efficiency of three siRNAs at the protein level. (D) Calcium channel-associated protein expression levels markedly decreased following siRNA transfection in HD-11 cells. (E) Validation results via quantitative real-time PCR (qRT-PCR). (F) Western blot analysis. (G) Reactive oxygen species (ROS) levels in HD11 cells across treatment groups. (H) Fluorescence microscopy images of calcium-sensitive dye Fluo-4-AM in each group.

Article Snippet: The antibodies used in this study were as follows: TRPC1 (HuaBio, China), NLRP3 (Wanleibio, China), STIM1 (Wanleibio, China), NF-κB (Abmart, China), ORAI1 (Abclonal, China), CHOP (Bioss, China), and GAPDH (Abmart, China).

Techniques: Expressing, Inhibition, Fluorescence, Microscopy, Transfection, Knockdown, Biomarker Discovery, Real-time Polymerase Chain Reaction, Quantitative RT-PCR, Western Blot

Journal: Poultry Science

Article Title: Mechanism of Scutellaria baicalensis extracellular vesicles in attenuating Mycoplasma gallisepticum -induced inflammation via TRPC1 - STIM1/ORAI1 channel inhibition

doi: 10.1016/j.psj.2026.106773

Figure Lengend Snippet: Effects of STIM1 overexpression on MG-induced inflammatory damage, endoplasmic reticulum stress, calcium channel-associated proteins, and calcium ion accumulation in HD-11 cells. (A) Fluorescence microscopy images of HD-11 cells transfected with an EGFP-tagged overexpression plasmid. (B) Transfection of HD-11 cells with STIM1 overexpression plasmid resulted in markedly elevated STIM1 protein expression levels. (C) Western blot analysis. (D) Quantitative real-time PCR (qRT-PCR) validation results. (E) Reactive oxygen species (ROS) levels in HD-11 cells across groups. (F) Fluorescence microscopy images of calcium-sensitive dye Fluo-4-AM in cells across groups.

Article Snippet: The antibodies used in this study were as follows: TRPC1 (HuaBio, China), NLRP3 (Wanleibio, China), STIM1 (Wanleibio, China), NF-κB (Abmart, China), ORAI1 (Abclonal, China), CHOP (Bioss, China), and GAPDH (Abmart, China).

Techniques: Over Expression, Fluorescence, Microscopy, Transfection, Plasmid Preparation, Expressing, Western Blot, Real-time Polymerase Chain Reaction, Quantitative RT-PCR, Biomarker Discovery