Journal: bioRxiv

Article Title: DMBT1 promotes SARS-CoV-2 infection and its SRCR-derived peptide inhibits SARS-CoV-2 infection

doi: 10.1101/2025.03.06.641801

Figure Lengend Snippet: (A) Flow cytometry staining of cell lines over-expressing DMBT1. (B) Western blot of 293T and 293T-ACE2KO using anti-ACE2 mAb. Cell lines over-expressing DMBT1 were analyzed using anti-DMBT1 pAb. (C) Luminescence values (RLU) of 293T and 293T-ACE2KO over-expressing DMBT1 cells infected with VLP (MOI=0.03). (D) Relative infection changes of 293T and 293T-ACE2KO cells over-expressing DMBT1. Data were representative of three independent experiments. *, P<0.05; Statistic significance was assessed by one-way ANOVA.

Article Snippet: Full length cDNA of DMBT1 gene was purchased from R&D systems, USA (RDC3108).

Techniques: Flow Cytometry, Staining, Expressing, Western Blot, Infection

Journal: bioRxiv

Article Title: DMBT1 promotes SARS-CoV-2 infection and its SRCR-derived peptide inhibits SARS-CoV-2 infection

doi: 10.1101/2025.03.06.641801

Figure Lengend Snippet: (A) RNA expression of DMBT1 in airway epithelial cell on violin plot from scRNA-seq/snRNA-seq. (B) Section of human trachea stained with the anti-DMBT1 Rabbit Polyclonal antibody. Scale bar = 200 μm. DMBT1 expression was upregulated in ACE2+ AT2 cells of COVID group. (C) RNA expression of DMBT1 in airway epithelial cell of COVID (left blue bars) and control (right red bars) group on violin plot. (D) RNA expression of DMBT1 in ACE2-AT2 cells (left blue bars) and ACE2+ cells (right red bars) on violin plot.

Article Snippet: Full length cDNA of DMBT1 gene was purchased from R&D systems, USA (RDC3108).

Techniques: RNA Expression, Staining, Expressing, Control

Journal: bioRxiv

Article Title: DMBT1 promotes SARS-CoV-2 infection and its SRCR-derived peptide inhibits SARS-CoV-2 infection

doi: 10.1101/2025.03.06.641801

Figure Lengend Snippet: (A) Schematic diagram of DMBT1 protein structure. Full length amino acid sequence of SRCR domain of DMBT1 and overlapping peptide library of SRCR domain. (B) Infection rate at SARS-CoV-2 virus with MOI at 3. (C) Infection rate at SARS-CoV-2 virus with MOI at 0.6. (D) Inhibition of peptide of SARS-CoV-2 pseudovirus infection. (E-G) IC50 values were determined using logistic regression analysis. Relative change rate was calculated based on comparison to DMSO control. (E) 293T-DMBT1 was infected by SARS-CoV-2 original strain (SH01) after peptide treatment. Virus incubated with peptide 7 in a 1:2 gradient dilution from 800 μg/mL, and then added to cells. Detection of viral infection by immunofluorescence at 48 hpi. (F) 293T-DMBT1 was infected by SARS-CoV-2 Delta pseudovirus after peptide treatment. (G) HeLa and A549 cells were infected by SARS-CoV-2 pseudovirus 3 strains after peptide treatment. (F, G) Pseudovirus (MOI=5) was incubated with peptide 7 in a 1:2 gradient dilution from 100 μM, and then added to cells. Intracellular Fluc activity of cell lysates was determined at 48 hpi.

Article Snippet: Full length cDNA of DMBT1 gene was purchased from R&D systems, USA (RDC3108).

Techniques: Sequencing, Infection, Virus, Inhibition, Comparison, Control, Incubation, Immunofluorescence, Activity Assay

Journal: Experimental & Molecular Medicine

Article Title: Loss of complex O-glycosylation impairs exocrine pancreatic function and induces MODY8-like diabetes in mice

doi: 10.1038/s12276-018-0157-3

Figure Lengend Snippet: a Representative TEM and brightfield micrographs of pancreas sections from fasting WT and Cosmc -KO adult mice. Zymogen granules are depicted as electron dense vesicles. TEM and BF scale bars are 2 and 20 µm, respectively. b Quantification of zymogen granules in five randomly selected fields of pancreas sections from fasting WT and Cosmc- KO adult mice ( n = 5 each). Elevated numbers of zymogen granules in Cosmc- KO pancreata ( P = 0.0004). c WB of VVA pull-down from WT and Cosmc- KO pancreatic lysates and DMBT1-specific antibody for detection. d Body weight analysis of WT and Cosmc- KO mice at ages 2–48 weeks ( n = 10 each) displays reduced body weight gain at 2 and 4 weeks of age ( P = 0.0021 and P = 0.0002). e Assessment of pancreas organ weight of 20- ( n = 10) and 54-week-old WT ( n = 11) and Cosmc- KO ( n = 13) mice. Aged mice display reduced organ weight ( P = 0.0062)

Article Snippet: For Western blot, antibodies for GAPDH (sc-32233; Santa Cruz Biotechnology, Santa Cruz, CA, USA), Cosmc (sc-67480; Santa Cruz Biotechnology), CEL (ab79131; Abcam, Cambridge, UK; sc-34883; Santa Cruz Biotechnology), DMBT1 (MAB59151; R&D Systems, Minneapolis, MN, USA), elastase (ab21593; Abcam) and trypsin (ab166898; Abcam) were used.

Techniques:

Journal: Inflammatory bowel diseases

Article Title: High suppressor of cytokine signaling-3 expression impairs STAT3-dependent protective effects of interleukin-22 in ulcerative colitis in remission.

doi: 10.1097/MIB.0000000000000267

Figure Lengend Snippet: FIGURE 2. IL-22–treatment induced activation of STAT3 signaling and expression of downstream target genes. Expression of SOCS3 and DMBT1 were evaluated by real-time PCR analysis of SW480 cells treated with IL-22 (20 ng/mL) at different time points (A). Survivin, Bcl-2, Bcl-xL, and c-Myc were evaluated by Western blot in HCT116 cells treated with IL-22 (20 ng/mL). Beta-actin was used for control. Graphs represent quantification of target protein bands relative to b-actin (B). Activation of STAT3 signaling by IL-22 was analyzed in HCT116 cells with respect to different durations of treatment and concentrations of IL-22 (C). The error bar equals SEM.

Article Snippet: Specific antibodies were used for SOCS3 (Abcam), p-STAT3 (Cell Signaling Technology), STAT3 (Cell Signaling Technology), Bcl-2 (Cell Signaling Technology), Survivin (Cell Signaling Technology), Bcl-xL (Cell Signaling Technology), c-Myc (Cell Signaling Technology), DMBT1 (Santa Cruz Biotechnology, Santa Cruz, CA), and b-Actin (Santa Cruz Biotechnology).

Techniques: Activation Assay, Expressing, Real-time Polymerase Chain Reaction, Western Blot, Control

Journal: Inflammatory bowel diseases

Article Title: High suppressor of cytokine signaling-3 expression impairs STAT3-dependent protective effects of interleukin-22 in ulcerative colitis in remission.

doi: 10.1097/MIB.0000000000000267

Figure Lengend Snippet: FIGURE 3. IL-22–regulated gene expression in a STAT3-dependent manner. IEC cell lines were transfected with STAT3 siRNA or nonspecific siRNA for 24 hours, followed by stimulation with IL-22 (20 ng/mL) for 48 hours. Real-time PCR analysis showed that IL-22–induced expression of SOCS3 and DMBT1 were reduced by depletion of STAT3 in SW480 cells. Expression was normalized to GAPDH levels (A). Western blot analysis represented that STAT3 was efficiently depleted, and IL-22–induced STAT3 activation was inhibited. STAT3 depletion partly inhibited IL-22–promoted expression of Survivin, Bcl-2, and c-Myc in HCT116 cells. Graphs represent quantification of target protein bands relative to b-actin (B).

Article Snippet: Specific antibodies were used for SOCS3 (Abcam), p-STAT3 (Cell Signaling Technology), STAT3 (Cell Signaling Technology), Bcl-2 (Cell Signaling Technology), Survivin (Cell Signaling Technology), Bcl-xL (Cell Signaling Technology), c-Myc (Cell Signaling Technology), DMBT1 (Santa Cruz Biotechnology, Santa Cruz, CA), and b-Actin (Santa Cruz Biotechnology).

Techniques: Gene Expression, Transfection, Real-time Polymerase Chain Reaction, Expressing, Western Blot, Activation Assay

Journal: Inflammatory bowel diseases

Article Title: High suppressor of cytokine signaling-3 expression impairs STAT3-dependent protective effects of interleukin-22 in ulcerative colitis in remission.

doi: 10.1097/MIB.0000000000000267

Figure Lengend Snippet: FIGURE 4. Overexpression of SOCS3 nearly abolished IL-22–induced STAT3 activation and opposed STAT3-dependent regulation of downstream genes. 116-neo and HCT116 stably transfected with SOCS3 (116-SOCS3) were treated with IL-22 (20 ng/mL) for different time points as indicated. Cell extracts were prepared and subjected to Western blot (A). SW480 cells were transfected with SOCS3 or empty vector for 24 hours, followed by IL-22 treatment for 48 hours. Analysis of DMBT1 protein accumulation and mRNA expression was performed by Western blot or real-time PCR, respectively (B). Expression of Survivin, Bcl-2, Bcl-xL, and c-Myc after IL-22 stimulation for 48 hours were analyzed by Western blot. Graphs represent quantification of target protein bands relative to b-actin (C).

Article Snippet: Specific antibodies were used for SOCS3 (Abcam), p-STAT3 (Cell Signaling Technology), STAT3 (Cell Signaling Technology), Bcl-2 (Cell Signaling Technology), Survivin (Cell Signaling Technology), Bcl-xL (Cell Signaling Technology), c-Myc (Cell Signaling Technology), DMBT1 (Santa Cruz Biotechnology, Santa Cruz, CA), and b-Actin (Santa Cruz Biotechnology).

Techniques: Over Expression, Activation Assay, Stable Transfection, Transfection, Western Blot, Plasmid Preparation, Expressing, Real-time Polymerase Chain Reaction

Journal: The Journal of Experimental Medicine

Article Title: Squamous cell carcinoma subverts adjacent histologically normal epithelium to promote lateral invasion

doi: 10.1084/jem.20200944

Figure Lengend Snippet: DMBT1 is down-regulated in HNSCC, and overexpression of DMBT1 suppresses invasion and tumor progression. (A) Meta-analysis showing down-regulation of DMBT1 in HNSCC relative to normal tissue. The datasets and accession numbers are given in . (B) Down-regulation of DMBT1 is correlated with poor overall survival in patients with HNSCC. The analyses were performed with the Rickman Head-Neck dataset (reporter ID, 208250_s_at; Oncomine; n = 81; *, P < 0.05; log-rank test). (C) DMBT1 gene expression in HNSCC cell lines. Total RNA from immortalized (HOK16B), primary keratinocytes (HOK5973), and HNSCC cell lines UM-SCC-(1, 14A, 29, 47, 81B, 104) was used to generate cDNAs, and Q-RT-PCR was performed. Data were analyzed by the relative quantification method with normalization to GAPDH and then relative to keratinocytes (*, P < 0.001; one-way ANOVA; error bars represent SD). Each sample was analyzed in triplicate, and the average fold-change was determined. (D) DMBT1 was stably overexpressed in UM-SCC-29 as verified by immunoblot analysis ( n = 2). (E) Overexpression of DMBT1 suppresses invasion in vitro at 48 h. Each color represents an independent experiment with three replicates in each experiment (*, P < 0.05; t test). (F) Nuclear pleomorphism is significantly less in tumors with UM-SCC-29-DMBT1 cells than in control tumors with UM-SCC-29-pCMV6 cells (***, P < 0.001; t test; n = 9; error bars represent SD).

Article Snippet: UM-SCC-1 and UM-SCC-29 cells were transfected with empty vector (pCMV6) or DMBT1 plasmids (#RC215454; OriGene).

Techniques: Over Expression, Gene Expression, Reverse Transcription Polymerase Chain Reaction, Quantitative Proteomics, Stable Transfection, Western Blot, In Vitro, Control

Journal: The Journal of Experimental Medicine

Article Title: Squamous cell carcinoma subverts adjacent histologically normal epithelium to promote lateral invasion

doi: 10.1084/jem.20200944

Figure Lengend Snippet: DMBT1 inhibits invasion and metastasis. (A) Down-regulation of DMBT1 is associated with distant metastasis-free survival. The analysis was performed with the Rickman Head-Neck dataset (reporter ID, 208250_s_at; Oncomine; n = 81; *, P < 0.05; log-rank test). (B) Protein lysates from immortalized (HOK16B), primary keratinocytes (HOK5973), and HNSCC cell lines UM-SCC-(1, 14A, 29, 47, 81B, 104) were immunoblotted with anti-DMBT1 antibody. Signal intensity was quantified by densitometric analysis with normalization to actin (loading control) and then expressed as percent of the signal intensity in HOK16B ( n = 2). (C) Overexpression of DMBT1 inhibits tumor growth in the CAM in vivo model. UM-SCC-29-pCMV6 and UM-SCC-29-DMBT1 cells (1 × 10 6 ) were seeded on the chick CAM (*, P < 0.05; n = 6; t test). (D) Overexpression of DMBT1 suppresses invasion in the CAM assay (left scale bar = 1 mm; right scale bar = 500 µm). Tumor sections from the CAM were stained with H&E. Arrows point to invasive islands. (E) Invasive tumor islands in tumor sections were plotted as the total number of invasive islands per sample (*, P < 0.05; t test). (F) Metastases (Mets) to the lower CAM were quantified with quantitative Alu-PCR (*, P < 0.05; t test). (G) UM-SCC-29 overexpressing DMBT1 (UM-SCC-29-DMBT1) or empty vector (UM-SCC-29-pCMV6; 1 × 10 6 ) were injected subcutaneously in athymic nude mice. Days 0 and 7 denote the time of injection and the start of tumor measurements, respectively. (H) Tumor size for mice injected with UM-SCC-29-pCMV6 or UM-SCC-29-DMBT1 cells (****, P < 0.0001; n = 9/group; linear mixed model of tumor volume with random effect for mouse and fixed effects for time). (I) Quantification of mitoses from 10 high power fields (HPF) in each mouse tissue section (images at 40× magnification; *, P < 0.05; t test). (J) H&E-stained images for pCMV6 and DMBT1 groups. Representative images show the predominant pattern of invasion. Arrows denote tumor islands at the invasive front (outside scale bar = 200 µm; inside scale bar = 40 µm). (K) Predominant pattern of invasion analyzed in tissue sections from each mouse (**, P < 0.01; t test).

Article Snippet: UM-SCC-1 and UM-SCC-29 cells were transfected with empty vector (pCMV6) or DMBT1 plasmids (#RC215454; OriGene).

Techniques: Control, Over Expression, In Vivo, Chick Chorioallantoic Membrane Assay, Staining, Plasmid Preparation, Injection

Journal: The Journal of Experimental Medicine

Article Title: Squamous cell carcinoma subverts adjacent histologically normal epithelium to promote lateral invasion

doi: 10.1084/jem.20200944

Figure Lengend Snippet: DMBT1 regulates mRNA stability and transcription of MMP9 and E-cadherin via ZEB1. (A) Immunoblot for EMT markers in UM-SCC-29-pCMV6 and UM-SCC-29-DMBT1 cells ( n = 2). (B–E) DMBT1 inhibits invasion via up-regulation of E-cadherin (E-cad). UM-SCC-29-DMBT1 cells were transiently transfected with siNT or siE-cad-1 (B and C) or siE-cad-2 (D and E). (B and D) Immunoblots verify suppression of E-cadherin. (C and E) Invasion assays. Scatter plots show three independent experiments; each color represents one experiment with at least duplicates in each (**, P < 0.001; ***, P < 0.0001; one-way ANOVA; error bars represent SD). (F and G) Overexpression of MMP9 and ZEB1 rescue invasion. UM-SCC-29-DMBT1 cells were transduced with empty vector (pLX304) or MMP9 or ZEB1. UM-SCC-29-pCMV was transduced with pLX304 as a control for UM-SCC-29-DMBT1-pLX304. Lysates were immunoblotted with anti-MMP9, anti-ZEB1, and anti-GAPDH (F). Invasion was quantified at 48 h after seeding (G). Scatter plots show two independent experiments; each color represents an independent experiment with three replicates in each (****, P < 0.0001; one-way ANOVA; error bars represent SD). (H and I) UM-SCC-29-pCMV6 and UM-SCC-29-DMBT1 were incubated with actinomycin D (1 µg/ml), and RNA was isolated at the indicated time. MMP-9 (H) and E-cadherin (I) transcripts, quantified by Q-RT-PCR, were normalized to GAPDH. Results are presented as percent of corresponding transcript at time 0. Values are mean ± SEM ( n = 3). (J and K) Normalized luciferase activity of MMP9 (J) and CDH1 (K) promoters in UM-SCC-29-pCMV6 and UM-SCC-29-DMBT1. Scatter plots show three independent experiments; each color represents an independent experiment (***, P < 0.001; t test; error bars represent SD).

Article Snippet: UM-SCC-1 and UM-SCC-29 cells were transfected with empty vector (pCMV6) or DMBT1 plasmids (#RC215454; OriGene).

Techniques: Western Blot, Transfection, Over Expression, Transduction, Plasmid Preparation, Control, Incubation, Isolation, Reverse Transcription Polymerase Chain Reaction, Luciferase, Activity Assay

Journal: The Journal of Experimental Medicine

Article Title: Squamous cell carcinoma subverts adjacent histologically normal epithelium to promote lateral invasion

doi: 10.1084/jem.20200944

Figure Lengend Snippet: Overexpression of DMBT1 regulates mRNA stability and transcription of MMP9 and E-cadherin (E-cad). (A) Expression of E-cad and MMP9 in UM-SCC-1-pCMV6 and UM-SCC-1-DMBT1 cells ( n = 2). (B and C) UM-SCC-1-pCMV6 and UM-SCC-1-DMBT1 were incubated with actinomycin D (1 µg/ml), and RNA was isolated at different time points. MMP9 (B) and E-cad (C) transcripts were quantified by Q-RT-PCR. MMP9 and E-cad mRNA expression was normalized to GAPDH. Results are presented as percent of corresponding transcript at time 0. Values are mean ± SEM. (D and E) Normalized luciferase activity of MMP9 promoter (D) is reduced whereas activity of CDH1 promoter (E) is significantly higher in UM-SCC-1-DMBT1 compared with control UM-SCC-1-pCMV6 cells (*, P < 0.001; n = 2; t test; error bars represent SD). (F) Q-RT-PCR of UM-SCC-1-pCMV6, UM-SCC-1-DMBT1, UM-SCC-29-pCMV6, and UM-SCC-29-DMBT1. Primers for ZEB1, NRF2 (NFE2), β-catenin, VDR, YY1, c-Jun (AP1), c-Fos (AP1), SP1, EGR1, KLF4, NFATC1 (NFAT), HNF1 (HNF1A), STAT1, STAT3, and TP53 are listed in . Data are normalized to GAPDH. Relative expression of each transcription factor in cells overexpressing DMBT1 is shown as fold change with respect to control (pCMV6) cells (*, P < 0.05; t test; error bars represent SD).

Article Snippet: UM-SCC-1 and UM-SCC-29 cells were transfected with empty vector (pCMV6) or DMBT1 plasmids (#RC215454; OriGene).

Techniques: Over Expression, Expressing, Incubation, Isolation, Reverse Transcription Polymerase Chain Reaction, Luciferase, Activity Assay, Control

Journal: The Journal of Experimental Medicine

Article Title: Squamous cell carcinoma subverts adjacent histologically normal epithelium to promote lateral invasion

doi: 10.1084/jem.20200944

Figure Lengend Snippet: ZEB1 down-regulates DMBT1 by binding promoter regions of MMP9 and CDH1 . (A) Venn diagram showing transcription factors with binding sites in the promoter regions of MMP9 and CDH1 , including ZEB1, NRF2 (NFE2), VDR, YY1, c-Jun (AP1), SP1, EGR1, KLF4, NFATC1 (NFAT), HNF1 (HNF1A), STAT1, STAT3, and TP53. (B and C) Q-RT-PCR of UM-SCC-1-pCMV6, UM-SCC-1-DMBT1, UM-SCC-29-pCMV6, and UM-SCC-29-DMBT1. Data are normalized to GAPDH. Relative expression of ZEB1 transcription factor in cells overexpressing DMBT1 is shown as fold change with respect to control (pCMV6) cells (***, P < 0.001; ****, P < 0.0001; t test; n = 2; error bars represent SD). (D and E) Q-RT-PCR was performed with ChIP-eluted DNA from UM-SCC-1-pCMV6, UM-SCC-1-DMBT1, UM-SCC-29-pCMV6, and UM-SCC-29-DMBT1 with validated primers specific to the ZEB1-binding site in the promoter region of MMP9 (D) and CDH1 (E; *, P < 0.05; t test; n = 2; error bars represent SD). (F) Immunoblot validation of DMBT1 down-regulation in lysates from UM-SCC-29-shVSVG and -shEZH2 transfected with nontarget siRNA (NT) or siDMBT1 (-1 and -2), as indicated. (G and H) Q-RT-PCR with ChIP-eluted DNA from UM-SCC-29-shVSVG and UM-SCC-29-shEZH2 (NT, siDMBT1-1, and siDMBT1-2) for standardized primers targeting the ZEB1-binding site in the promoter region of MMP9 (G) and CDH1 (H). Scatter plots show two independent experiments; each color represents an independent experiment (**, P < 0.01; ****, P < 0.0001; one-way ANOVA; error bars represent SD).

Article Snippet: UM-SCC-1 and UM-SCC-29 cells were transfected with empty vector (pCMV6) or DMBT1 plasmids (#RC215454; OriGene).

Techniques: Binding Assay, Reverse Transcription Polymerase Chain Reaction, Expressing, Control, Western Blot, Biomarker Discovery, Transfection

Journal: Frontiers in Oncology

Article Title: Integrative Proteo-Genomic Analysis for Recurrent Survival Prognosis in Colon Adenocarcinoma

doi: 10.3389/fonc.2022.871568

Figure Lengend Snippet: The list of independent prognostic feature cDEGs.

Article Snippet: The membranes were blocked with 5% skim milk dissolved in phosphate-buffered saline (PBS) and Tween 20 (PBST) for 2 h at room temperature, followed by incubated with primary antibodies against CA12 (15180-1-AP, Proteintech Group, Inc., Chicago, Il, USA), AHNAK2 (ab164994, Abcam), MMAA (ab264418, Abcam), DMBT1 (ab276422), and GAPDH (10491-1-AP, Proteintech Group, Inc., Chicago, Il, USA) at 4°C overnight.

Techniques:

Journal: Frontiers in Oncology

Article Title: Integrative Proteo-Genomic Analysis for Recurrent Survival Prognosis in Colon Adenocarcinoma

doi: 10.3389/fonc.2022.871568

Figure Lengend Snippet: Validation of eight independent prognostic cDEGs. Quantitative real-time PCR analysis was performed to determine the mRNA expression levels of ADH4, AHNAK2, MMAA, and DMBT1 in tumor tissue and adjacent tissues (A) , and in recurrent tissues and non-recurrent tissues (B) . Western blot analysis was utilized to measure the protein levels of ADH4, AHNAK2, MMAA, and DMBT1 in tumor tissue and adjacent tissues (C) , and in recurrent tissues and non-recurrent tissues (D) . Data were expressed as mean ± SD of three independent repeats. ** p < 0.01, *** p < 0.001, compared with adjacent or non-recurrent tissues. A, adjacent tissues; T, tumor tissues; N, non-recurrent; R, recurrent.

Article Snippet: The membranes were blocked with 5% skim milk dissolved in phosphate-buffered saline (PBS) and Tween 20 (PBST) for 2 h at room temperature, followed by incubated with primary antibodies against CA12 (15180-1-AP, Proteintech Group, Inc., Chicago, Il, USA), AHNAK2 (ab164994, Abcam), MMAA (ab264418, Abcam), DMBT1 (ab276422), and GAPDH (10491-1-AP, Proteintech Group, Inc., Chicago, Il, USA) at 4°C overnight.

Techniques: Biomarker Discovery, Real-time Polymerase Chain Reaction, Expressing, Western Blot

Journal: The Kaohsiung journal of medical sciences

Article Title: The protective role of DMBT1 in cervical squamous cell carcinoma.

doi: 10.1002/kjm2.12117

Figure Lengend Snippet: FIGURE 1 DMBT1 expression in CSCC tissues and adjacent normal tissues detected by qRT-PCR (A) and immunohistochemical staining (B and C). CSCC, cervical squamous cell carcinoma; DMBT1, deleted in malignant brain tumor 1

Article Snippet: SiHa and CaSKi cells were divided into three groups, including Blank group, Vector group (cells transfected with control lentiviral activation particles, sc-437282, Santa Cruz Biotechnology, California), and DMBT1 group (cells transfected with DMBT1 lentiviral activation particles, sc-402615-LAC, Santa Cruz Biotechnology).

Techniques: Expressing, Quantitative RT-PCR, Immunohistochemical staining, Staining

Journal: The Kaohsiung journal of medical sciences

Article Title: The protective role of DMBT1 in cervical squamous cell carcinoma.

doi: 10.1002/kjm2.12117

Figure Lengend Snippet: FIGURE 2 Effects of DMBT1 expression and clinicopathological features on the prognosis of CSCC patients. A, DMBT1 expression; B, Age; C, FIGO stage; D, Tumor diameter; E, Lymph node metastasis; F, Tumor differentiation. CSCC, cervical squamous cell carcinoma; DMBT1, deleted in malignant brain tumor 1

Article Snippet: SiHa and CaSKi cells were divided into three groups, including Blank group, Vector group (cells transfected with control lentiviral activation particles, sc-437282, Santa Cruz Biotechnology, California), and DMBT1 group (cells transfected with DMBT1 lentiviral activation particles, sc-402615-LAC, Santa Cruz Biotechnology).

Techniques: Expressing

Journal: The Kaohsiung journal of medical sciences

Article Title: The protective role of DMBT1 in cervical squamous cell carcinoma.

doi: 10.1002/kjm2.12117

Figure Lengend Snippet: FIGURE 3 DMBT1 overexpression inhibited the proliferation of CSCC cells. A and B, The mRNA expression of DMBT1 in SiHa (A) and CaSKi (B) cells from each group detected by qRT-PCR; C-F, DMBT1 protein expression in SiHa (C, E) and CaSKi (D, F) cells from each group tested by Western blot; *P < .05 compared with the Blank group and the Vector group; G and H, The growth of SiHa (G) and CaSKi (H) cells detected by MTT assay; I-L, The proliferation of SiHa (I and J) and CaSKi (K and L) cells tested by Cell-Light EdU assay; *P < .05 compared with the Blank group and the Vector group. CSCC, cervical squamous cell carcinoma; DMBT1, deleted in malignant brain tumor 1

Article Snippet: SiHa and CaSKi cells were divided into three groups, including Blank group, Vector group (cells transfected with control lentiviral activation particles, sc-437282, Santa Cruz Biotechnology, California), and DMBT1 group (cells transfected with DMBT1 lentiviral activation particles, sc-402615-LAC, Santa Cruz Biotechnology).

Techniques: Over Expression, Expressing, Quantitative RT-PCR, Western Blot, Plasmid Preparation, MTT Assay, EdU Assay

Journal: The Kaohsiung journal of medical sciences

Article Title: The protective role of DMBT1 in cervical squamous cell carcinoma.

doi: 10.1002/kjm2.12117

Figure Lengend Snippet: FIGURE 4 DMBT1 overexpression promoted the apoptosis of CSCC cells. A-D, The apoptosis of SiHa (A and B) and CaSKi (C and D) cells examined by Annexin V-FITC/PI staining; E-G, The expression of apoptosis-related proteins (Bcl-2, Bax, and Cleaved caspase-3) in SiHa (E and F) and CaSKi (G and H) cells determined by Western blot; *P < .05 compared with the Blank group and the Vector group. CSCC, cervical squamous cell carcinoma; DMBT1, deleted in malignant brain tumor 1

Article Snippet: SiHa and CaSKi cells were divided into three groups, including Blank group, Vector group (cells transfected with control lentiviral activation particles, sc-437282, Santa Cruz Biotechnology, California), and DMBT1 group (cells transfected with DMBT1 lentiviral activation particles, sc-402615-LAC, Santa Cruz Biotechnology).

Techniques: Over Expression, Staining, Expressing, Western Blot, Plasmid Preparation

Journal: The Kaohsiung journal of medical sciences

Article Title: The protective role of DMBT1 in cervical squamous cell carcinoma.

doi: 10.1002/kjm2.12117

Figure Lengend Snippet: FIGURE 5 DMBT1 overexpression inhibited the migration and invasion of CSCC cells. A and B, The migration and invasion of SiHa (A) and CaSKi (B) cells detected by Wound-healing assay and Transwell invasion assay, respectively; C-F, The statistical analysis of cell migration and invasion ability; *P < .05 compared with the Blank group and the Vector group. CSCC, cervical squamous cell carcinoma; DMBT1, deleted in malignant brain tumor 1

Article Snippet: SiHa and CaSKi cells were divided into three groups, including Blank group, Vector group (cells transfected with control lentiviral activation particles, sc-437282, Santa Cruz Biotechnology, California), and DMBT1 group (cells transfected with DMBT1 lentiviral activation particles, sc-402615-LAC, Santa Cruz Biotechnology).

Techniques: Over Expression, Migration, Wound Healing Assay, Transwell Invasion Assay, Plasmid Preparation

Journal: The Kaohsiung journal of medical sciences

Article Title: The protective role of DMBT1 in cervical squamous cell carcinoma.

doi: 10.1002/kjm2.12117

Figure Lengend Snippet: FIGURE 6 DMBT1 overexpression inhibited the EMT formation of CSCC cells. A, The protein expressions of EMT makers (including E-cadherin, N-cadherin, and Vimentin) in SiHa and CaSKi cells examined by Western blot; B and C, The mRNA expression of EMT makers (including E-cadherin, N-cadherin, and Vimentin) in SiHa (B) and CaSKi (C) cells detected by qRT-PCR; D and E, The statistical analysis of Figure A;*, P < .05 compared with the Blank group and the Vector group. CSCC, cervical squamous cell carcinoma; DMBT1, deleted in malignant brain tumor 1

Article Snippet: SiHa and CaSKi cells were divided into three groups, including Blank group, Vector group (cells transfected with control lentiviral activation particles, sc-437282, Santa Cruz Biotechnology, California), and DMBT1 group (cells transfected with DMBT1 lentiviral activation particles, sc-402615-LAC, Santa Cruz Biotechnology).

Techniques: Over Expression, Western Blot, Expressing, Quantitative RT-PCR, Plasmid Preparation

Journal: bioRxiv

Article Title: DMBT1 promotes SARS-CoV-2 infection and its SRCR-derived peptide inhibits SARS-CoV-2 infection

doi: 10.1101/2025.03.06.641801

Figure Lengend Snippet: (A) Flow cytometry staining of cell lines over-expressing DMBT1. (B) Western blot of 293T and 293T-ACE2KO using anti-ACE2 mAb. Cell lines over-expressing DMBT1 were analyzed using anti-DMBT1 pAb. (C) Luminescence values (RLU) of 293T and 293T-ACE2KO over-expressing DMBT1 cells infected with VLP (MOI=0.03). (D) Relative infection changes of 293T and 293T-ACE2KO cells over-expressing DMBT1. Data were representative of three independent experiments. *, P<0.05; Statistic significance was assessed by one-way ANOVA.

Article Snippet: Incubation with Anti-DMBT1 rabbit pAb (Sino Biological, China) and anti-ACE2 rabbit mAb (ABclonal, China) was performed overnight at 4°C.

Techniques: Flow Cytometry, Staining, Expressing, Western Blot, Infection

Journal: bioRxiv

Article Title: DMBT1 promotes SARS-CoV-2 infection and its SRCR-derived peptide inhibits SARS-CoV-2 infection

doi: 10.1101/2025.03.06.641801

Figure Lengend Snippet: (A) RNA expression of DMBT1 in airway epithelial cell on violin plot from scRNA-seq/snRNA-seq. (B) Section of human trachea stained with the anti-DMBT1 Rabbit Polyclonal antibody. Scale bar = 200 μm. DMBT1 expression was upregulated in ACE2+ AT2 cells of COVID group. (C) RNA expression of DMBT1 in airway epithelial cell of COVID (left blue bars) and control (right red bars) group on violin plot. (D) RNA expression of DMBT1 in ACE2-AT2 cells (left blue bars) and ACE2+ cells (right red bars) on violin plot.

Article Snippet: Incubation with Anti-DMBT1 rabbit pAb (Sino Biological, China) and anti-ACE2 rabbit mAb (ABclonal, China) was performed overnight at 4°C.

Techniques: RNA Expression, Staining, Expressing, Control

Journal: bioRxiv

Article Title: DMBT1 promotes SARS-CoV-2 infection and its SRCR-derived peptide inhibits SARS-CoV-2 infection

doi: 10.1101/2025.03.06.641801

Figure Lengend Snippet: (A) Schematic diagram of DMBT1 protein structure. Full length amino acid sequence of SRCR domain of DMBT1 and overlapping peptide library of SRCR domain. (B) Infection rate at SARS-CoV-2 virus with MOI at 3. (C) Infection rate at SARS-CoV-2 virus with MOI at 0.6. (D) Inhibition of peptide of SARS-CoV-2 pseudovirus infection. (E-G) IC50 values were determined using logistic regression analysis. Relative change rate was calculated based on comparison to DMSO control. (E) 293T-DMBT1 was infected by SARS-CoV-2 original strain (SH01) after peptide treatment. Virus incubated with peptide 7 in a 1:2 gradient dilution from 800 μg/mL, and then added to cells. Detection of viral infection by immunofluorescence at 48 hpi. (F) 293T-DMBT1 was infected by SARS-CoV-2 Delta pseudovirus after peptide treatment. (G) HeLa and A549 cells were infected by SARS-CoV-2 pseudovirus 3 strains after peptide treatment. (F, G) Pseudovirus (MOI=5) was incubated with peptide 7 in a 1:2 gradient dilution from 100 μM, and then added to cells. Intracellular Fluc activity of cell lysates was determined at 48 hpi.

Article Snippet: Incubation with Anti-DMBT1 rabbit pAb (Sino Biological, China) and anti-ACE2 rabbit mAb (ABclonal, China) was performed overnight at 4°C.

Techniques: Sequencing, Infection, Virus, Inhibition, Comparison, Control, Incubation, Immunofluorescence, Activity Assay