v atpase Search Results


94
Proteintech tcirg1
<t>TCIRG1</t> expression in different tumors and their cancerous tissues. ( A ) TCIRG1 expression levels in TCGA tumor tissues and TCGA and GTEX normal tissues. ( B ) Comparison of TCIRG1 expression between TCGA tumor data and the corresponding TCGA normal data. ( C ) RNA expression levels of TCIRG1 in tumor and normal tissues in renal clear cell carcinoma (KIRC) samples from the UALCAN database. GEO database series, including TCIRG1 expression levels in GSE66272 ( D ) and GSE53757 ( E ), and GSE15641 ( F – H ) immunohistochemistry staining statistics results for normal kidney tissues and KIRC tissues. Scale bar: 50 μm. (* p < 0.05, ** p < 0.01, *** p < 0.001, ns indicates no statistical significance).
Tcirg1, supplied by Proteintech, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/v+atpase/TCIRG1+Antibody/pmc09558535-136-51-53
Average 94 stars, based on 1 article reviews
tcirg1 - by Bioz Stars, 2026-10
94/100 stars
  Buy from Supplier

94
Proteintech ldhb
Fig. 6. NaHS inhibited the interaction between <t>LDHB</t> and ATP6V1A and reduced ATP6V1A-dependent lysosomal acidification. A, B. MOVAs were treated with NaHS (200 μM) and PDGF (20 ng/mL) for 24 h. Whole-cell lysates were immunoprecipitated and then immunoblotted <t>with</t> <t>antibodies</t> against the indicated proteins. C. PLA was performed to detect the interaction of LDHB and ATP6V1A. Data were quantified in the lower panel. ***p < 0.001.Scale bar = 50 μm. D. Co-localization of LDHB and ATP6V1A in MOVAs was examined by immunofluorescence. Data were quantified in the lower panel. n = 6, ***p < 0.001. Scale bars = 50 μm. E. LDHB- GFP plasmid was transfected into MOVAs for 24 h and then stimulated with PDGF in the presence or absence of NaHS. Lyso-Tracker Red was used to label lysosomes. Data were quantified in the lower panel. n = 6, ***p < 0.001.Scale bars = 20 μm. F. Lysosomal pH of MOVAs was measured by FITC-dextran staining (0.5 mg/mL). Data were quantified in the right panel. n = 6, ***p < 0.001. Scale bars = 50 μm.
Ldhb, supplied by Proteintech, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/v+atpase/ATP6V1A+Antibody/pm39647238-146-3-4
Average 94 stars, based on 1 article reviews
ldhb - by Bioz Stars, 2026-10
94/100 stars
  Buy from Supplier

93
Proteintech atp6v1b2
Fig. 6. NaHS inhibited the interaction between <t>LDHB</t> and ATP6V1A and reduced ATP6V1A-dependent lysosomal acidification. A, B. MOVAs were treated with NaHS (200 μM) and PDGF (20 ng/mL) for 24 h. Whole-cell lysates were immunoprecipitated and then immunoblotted <t>with</t> <t>antibodies</t> against the indicated proteins. C. PLA was performed to detect the interaction of LDHB and ATP6V1A. Data were quantified in the lower panel. ***p < 0.001.Scale bar = 50 μm. D. Co-localization of LDHB and ATP6V1A in MOVAs was examined by immunofluorescence. Data were quantified in the lower panel. n = 6, ***p < 0.001. Scale bars = 50 μm. E. LDHB- GFP plasmid was transfected into MOVAs for 24 h and then stimulated with PDGF in the presence or absence of NaHS. Lyso-Tracker Red was used to label lysosomes. Data were quantified in the lower panel. n = 6, ***p < 0.001.Scale bars = 20 μm. F. Lysosomal pH of MOVAs was measured by FITC-dextran staining (0.5 mg/mL). Data were quantified in the right panel. n = 6, ***p < 0.001. Scale bars = 50 μm.
Atp6v1b2, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/v+atpase/ATP6V1B2+Antibody/bio_rxiv__2025__01__21__634145-256-59-61
Average 93 stars, based on 1 article reviews
atp6v1b2 - by Bioz Stars, 2026-10
93/100 stars
  Buy from Supplier

94
Proteintech anti calsarcin2
Fig. 6. NaHS inhibited the interaction between <t>LDHB</t> and ATP6V1A and reduced ATP6V1A-dependent lysosomal acidification. A, B. MOVAs were treated with NaHS (200 μM) and PDGF (20 ng/mL) for 24 h. Whole-cell lysates were immunoprecipitated and then immunoblotted <t>with</t> <t>antibodies</t> against the indicated proteins. C. PLA was performed to detect the interaction of LDHB and ATP6V1A. Data were quantified in the lower panel. ***p < 0.001.Scale bar = 50 μm. D. Co-localization of LDHB and ATP6V1A in MOVAs was examined by immunofluorescence. Data were quantified in the lower panel. n = 6, ***p < 0.001. Scale bars = 50 μm. E. LDHB- GFP plasmid was transfected into MOVAs for 24 h and then stimulated with PDGF in the presence or absence of NaHS. Lyso-Tracker Red was used to label lysosomes. Data were quantified in the lower panel. n = 6, ***p < 0.001.Scale bars = 20 μm. F. Lysosomal pH of MOVAs was measured by FITC-dextran staining (0.5 mg/mL). Data were quantified in the right panel. n = 6, ***p < 0.001. Scale bars = 50 μm.
Anti Calsarcin2, supplied by Proteintech, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/v+atpase/ATP6V1H+Antibody/pm28369518-252-44-72
Average 94 stars, based on 1 article reviews
anti calsarcin2 - by Bioz Stars, 2026-10
94/100 stars
  Buy from Supplier

94
Synaptic Systems rabbit polyclonal anti v0a1

Rabbit Polyclonal Anti V0a1, supplied by Synaptic Systems, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/v+atpase/109+002/pmc05959719-1-2-6
Average 94 stars, based on 1 article reviews
rabbit polyclonal anti v0a1 - by Bioz Stars, 2026-10
94/100 stars
  Buy from Supplier

93
Proteintech anti atp6v0a1

Anti Atp6v0a1, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/v+atpase/ATP6V0A1+Antibody/pm39680136-425-5-7
Average 93 stars, based on 1 article reviews
anti atp6v0a1 - by Bioz Stars, 2026-10
93/100 stars
  Buy from Supplier

93
Proteintech atp6v0d1 antibody

Atp6v0d1 Antibody, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/v+atpase/ATP6V0D1+Antibody/pm37936170-72-0-4
Average 93 stars, based on 1 article reviews
atp6v0d1 antibody - by Bioz Stars, 2026-10
93/100 stars
  Buy from Supplier

93
Proteintech atp6v1e1

Atp6v1e1, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/v+atpase/ATP6V1E1+Antibody/bio_rxiv__2025__04__28__650675-290-84-87
Average 93 stars, based on 1 article reviews
atp6v1e1 - by Bioz Stars, 2026-10
93/100 stars
  Buy from Supplier

93
Proteintech atp6v1g1
Figure 3. NEO214 has an adverse effect on lysosomal function and blocked autophagic flux in glioma cells dependent on MTOR signaling. (A-B) Expression analysis of the autophagy-lysosome relevant genes in 100 μmol/L NEO214-treated U251 and T98G cells. (C) WB analysis of <t>ATP6V1G1,</t> ATP6V1D, ATP6V1H and ATP6V1C1 in U251 and T98G cells were treated with NEO214(100 μmol/L) in full-medium 24 h. (D) NEO214 does not affect the autophagosome formation process in glioma cells. Western blot analysis of the protein expression of BECN1, ATG3, ATG5, ATG9A, LC3, and SQSTM1 in U251 and T98G cells treated by 100 μmol/L NEO214 for 24 h. (E) Western blot analysis of MTOR signaling proteins expressions in U251 and T98G cells treated by 100 μmol/L NEO214 24 h. (n = 3; *, P < 0.05; **, P < 0.01; ***, P < 0.001).
Atp6v1g1, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/v+atpase/ATP6V1G1+Antibody/pm37545052-330-149-150
Average 93 stars, based on 1 article reviews
atp6v1g1 - by Bioz Stars, 2026-10
93/100 stars
  Buy from Supplier

93
Proteintech atp6v1d
Figure 3. NEO214 has an adverse effect on lysosomal function and blocked autophagic flux in glioma cells dependent on MTOR signaling. (A-B) Expression analysis of the autophagy-lysosome relevant genes in 100 μmol/L NEO214-treated U251 and T98G cells. (C) WB analysis of <t>ATP6V1G1,</t> ATP6V1D, ATP6V1H and ATP6V1C1 in U251 and T98G cells were treated with NEO214(100 μmol/L) in full-medium 24 h. (D) NEO214 does not affect the autophagosome formation process in glioma cells. Western blot analysis of the protein expression of BECN1, ATG3, ATG5, ATG9A, LC3, and SQSTM1 in U251 and T98G cells treated by 100 μmol/L NEO214 for 24 h. (E) Western blot analysis of MTOR signaling proteins expressions in U251 and T98G cells treated by 100 μmol/L NEO214 24 h. (n = 3; *, P < 0.05; **, P < 0.01; ***, P < 0.001).
Atp6v1d, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/v+atpase/ATP6V1D+Antibody/pm36791992-149-62-66
Average 93 stars, based on 1 article reviews
atp6v1d - by Bioz Stars, 2026-10
93/100 stars
  Buy from Supplier

90
ProSci Incorporated sars cov2 specific antibodies against nucleocapsid
Viral findings in mild versus severe <t>SARS-CoV2</t> infection. The control lungs showed no viral protein or RNA (panel A) whereas the lung tissue from someone who died of COVID-19 showed high viral RNA (panel B) and the spike protein subunit 2 (panel C) in the same alveolar wall distribution. Similarly, note the absence of the viral spike protein in the uninfected nasopharynx swab (panel D) and the strong signal for spike subunit 1 (panel E) and spike subunit 2 proteins (panel F) in glandular cells from a person with mild disease. NP – nasopharyngeal, NL – normal control, and the signal is brown due to DAB with hematoxylin counterstain. (For interpretation of the references to color in this figure legend, the reader is referred to the web version of this article.)
Sars Cov2 Specific Antibodies Against Nucleocapsid, supplied by ProSci Incorporated, 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/v+atpase/ATP6AP1+Antibody/pmc09436872-32-0-18
Average 90 stars, based on 1 article reviews
sars cov2 specific antibodies against nucleocapsid - by Bioz Stars, 2026-10
90/100 stars
  Buy from Supplier

93
Proteintech rabbit anti atp6v1f
Viral findings in mild versus severe <t>SARS-CoV2</t> infection. The control lungs showed no viral protein or RNA (panel A) whereas the lung tissue from someone who died of COVID-19 showed high viral RNA (panel B) and the spike protein subunit 2 (panel C) in the same alveolar wall distribution. Similarly, note the absence of the viral spike protein in the uninfected nasopharynx swab (panel D) and the strong signal for spike subunit 1 (panel E) and spike subunit 2 proteins (panel F) in glandular cells from a person with mild disease. NP – nasopharyngeal, NL – normal control, and the signal is brown due to DAB with hematoxylin counterstain. (For interpretation of the references to color in this figure legend, the reader is referred to the web version of this article.)
Rabbit Anti Atp6v1f, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/v+atpase/ATP6V1F+Antibody/pmc12527914-447-70-72
Average 93 stars, based on 1 article reviews
rabbit anti atp6v1f - by Bioz Stars, 2026-10
93/100 stars
  Buy from Supplier

Image Search Results


TCIRG1 expression in different tumors and their cancerous tissues. ( A ) TCIRG1 expression levels in TCGA tumor tissues and TCGA and GTEX normal tissues. ( B ) Comparison of TCIRG1 expression between TCGA tumor data and the corresponding TCGA normal data. ( C ) RNA expression levels of TCIRG1 in tumor and normal tissues in renal clear cell carcinoma (KIRC) samples from the UALCAN database. GEO database series, including TCIRG1 expression levels in GSE66272 ( D ) and GSE53757 ( E ), and GSE15641 ( F – H ) immunohistochemistry staining statistics results for normal kidney tissues and KIRC tissues. Scale bar: 50 μm. (* p < 0.05, ** p < 0.01, *** p < 0.001, ns indicates no statistical significance).

Journal: Cancers

Article Title: Integrative Analysis Identifies TCIRG1 as a Potential Prognostic and Immunotherapy-Relevant Biomarker Associated with Malignant Cell Migration in Clear Cell Renal Cell Carcinoma

doi: 10.3390/cancers14194583

Figure Lengend Snippet: TCIRG1 expression in different tumors and their cancerous tissues. ( A ) TCIRG1 expression levels in TCGA tumor tissues and TCGA and GTEX normal tissues. ( B ) Comparison of TCIRG1 expression between TCGA tumor data and the corresponding TCGA normal data. ( C ) RNA expression levels of TCIRG1 in tumor and normal tissues in renal clear cell carcinoma (KIRC) samples from the UALCAN database. GEO database series, including TCIRG1 expression levels in GSE66272 ( D ) and GSE53757 ( E ), and GSE15641 ( F – H ) immunohistochemistry staining statistics results for normal kidney tissues and KIRC tissues. Scale bar: 50 μm. (* p < 0.05, ** p < 0.01, *** p < 0.001, ns indicates no statistical significance).

Article Snippet: Total proteins were then extracted, measured, and semi-dry transferred to PVDF (Millipore, Billerica, MA, USA) membranes after separation by 8–12% SDS-PAGE electrophoresis; PVDF membranes were first closed with TBS + Tween (TBST) solution containing 5% skim milk powder for 2 h, washed, and incubated with primary antibody at 4 °C overnight (TCIRG1, 12649-1-AP, Proteintech, 1:50); they were then rewashed and incubated for 2 h with a secondary antibody that was colored by horseradish peroxidase.

Techniques: Expressing, Comparison, RNA Expression, Immunohistochemistry, Staining

Correlation between the expression of TCIRG1 and tumor prognosis ( A , C , E ). Kaplan–Meier curves demonstrating OS, PFI, and DSS of patients in the high- and low-TCIRG1 expression groups in KIRC samples. Forest plots demonstrate the prognostic HR of TCIRG1 in different cancer subgroups in OS ( B ), PFI ( D ), and DSS ( F ).

Journal: Cancers

Article Title: Integrative Analysis Identifies TCIRG1 as a Potential Prognostic and Immunotherapy-Relevant Biomarker Associated with Malignant Cell Migration in Clear Cell Renal Cell Carcinoma

doi: 10.3390/cancers14194583

Figure Lengend Snippet: Correlation between the expression of TCIRG1 and tumor prognosis ( A , C , E ). Kaplan–Meier curves demonstrating OS, PFI, and DSS of patients in the high- and low-TCIRG1 expression groups in KIRC samples. Forest plots demonstrate the prognostic HR of TCIRG1 in different cancer subgroups in OS ( B ), PFI ( D ), and DSS ( F ).

Article Snippet: Total proteins were then extracted, measured, and semi-dry transferred to PVDF (Millipore, Billerica, MA, USA) membranes after separation by 8–12% SDS-PAGE electrophoresis; PVDF membranes were first closed with TBS + Tween (TBST) solution containing 5% skim milk powder for 2 h, washed, and incubated with primary antibody at 4 °C overnight (TCIRG1, 12649-1-AP, Proteintech, 1:50); they were then rewashed and incubated for 2 h with a secondary antibody that was colored by horseradish peroxidase.

Techniques: Expressing

Correlation between high TCIRG1 expression and clinical traits. ( A ) Grade, ( B ) Stage, ( C ) T, ( D ) M, and ( E ) N correlation with TCIRG1 expression. ( F ) Heat map of correlation between clinical traits and TCIRG1 expression. ( G ) ROC curve to predict the diagnostic value of elevated TCIRG1. Nomogram for KIRC samples ( H ) and the calibration curve of the nomogram ( I ) for predicting OS at 1, 3, and 5 years. (* p < 0.05, ** p < 0.01, *** p < 0.001).

Journal: Cancers

Article Title: Integrative Analysis Identifies TCIRG1 as a Potential Prognostic and Immunotherapy-Relevant Biomarker Associated with Malignant Cell Migration in Clear Cell Renal Cell Carcinoma

doi: 10.3390/cancers14194583

Figure Lengend Snippet: Correlation between high TCIRG1 expression and clinical traits. ( A ) Grade, ( B ) Stage, ( C ) T, ( D ) M, and ( E ) N correlation with TCIRG1 expression. ( F ) Heat map of correlation between clinical traits and TCIRG1 expression. ( G ) ROC curve to predict the diagnostic value of elevated TCIRG1. Nomogram for KIRC samples ( H ) and the calibration curve of the nomogram ( I ) for predicting OS at 1, 3, and 5 years. (* p < 0.05, ** p < 0.01, *** p < 0.001).

Article Snippet: Total proteins were then extracted, measured, and semi-dry transferred to PVDF (Millipore, Billerica, MA, USA) membranes after separation by 8–12% SDS-PAGE electrophoresis; PVDF membranes were first closed with TBS + Tween (TBST) solution containing 5% skim milk powder for 2 h, washed, and incubated with primary antibody at 4 °C overnight (TCIRG1, 12649-1-AP, Proteintech, 1:50); they were then rewashed and incubated for 2 h with a secondary antibody that was colored by horseradish peroxidase.

Techniques: Expressing, Diagnostic Assay

Analysis of OS using the Cox proportional hazards regression model.

Journal: Cancers

Article Title: Integrative Analysis Identifies TCIRG1 as a Potential Prognostic and Immunotherapy-Relevant Biomarker Associated with Malignant Cell Migration in Clear Cell Renal Cell Carcinoma

doi: 10.3390/cancers14194583

Figure Lengend Snippet: Analysis of OS using the Cox proportional hazards regression model.

Article Snippet: Total proteins were then extracted, measured, and semi-dry transferred to PVDF (Millipore, Billerica, MA, USA) membranes after separation by 8–12% SDS-PAGE electrophoresis; PVDF membranes were first closed with TBS + Tween (TBST) solution containing 5% skim milk powder for 2 h, washed, and incubated with primary antibody at 4 °C overnight (TCIRG1, 12649-1-AP, Proteintech, 1:50); they were then rewashed and incubated for 2 h with a secondary antibody that was colored by horseradish peroxidase.

Techniques:

Molecular characterization of high- and low-TCIRG1 expression subgroups. ( A , B ) Distribution of the ten most commonly mutated genes in the high-TCIRG1 TCGA-KIRC subgroup. The top bar shows the TMB of each patient, and the right bar shows the different types of mutations. Differences in TCIRG1 expression between ( C ) wild-type and PBRM1 mutant subgroups and ( D ) BAP1 mutant subgroups. ( E ) Correlation analysis of TCIRG1 expression with TMB. ( F ) Relationship between TCIRG1 expression and DNA methylation. ( G ) Relationship between DNA methylation levels and OS. ( H,I ) Correlation analysis of TCIRG1 expression with cancer stemness DNAss and RNAss. ( J ) Correlation analysis of RNAss levels with OS.

Journal: Cancers

Article Title: Integrative Analysis Identifies TCIRG1 as a Potential Prognostic and Immunotherapy-Relevant Biomarker Associated with Malignant Cell Migration in Clear Cell Renal Cell Carcinoma

doi: 10.3390/cancers14194583

Figure Lengend Snippet: Molecular characterization of high- and low-TCIRG1 expression subgroups. ( A , B ) Distribution of the ten most commonly mutated genes in the high-TCIRG1 TCGA-KIRC subgroup. The top bar shows the TMB of each patient, and the right bar shows the different types of mutations. Differences in TCIRG1 expression between ( C ) wild-type and PBRM1 mutant subgroups and ( D ) BAP1 mutant subgroups. ( E ) Correlation analysis of TCIRG1 expression with TMB. ( F ) Relationship between TCIRG1 expression and DNA methylation. ( G ) Relationship between DNA methylation levels and OS. ( H,I ) Correlation analysis of TCIRG1 expression with cancer stemness DNAss and RNAss. ( J ) Correlation analysis of RNAss levels with OS.

Article Snippet: Total proteins were then extracted, measured, and semi-dry transferred to PVDF (Millipore, Billerica, MA, USA) membranes after separation by 8–12% SDS-PAGE electrophoresis; PVDF membranes were first closed with TBS + Tween (TBST) solution containing 5% skim milk powder for 2 h, washed, and incubated with primary antibody at 4 °C overnight (TCIRG1, 12649-1-AP, Proteintech, 1:50); they were then rewashed and incubated for 2 h with a secondary antibody that was colored by horseradish peroxidase.

Techniques: Expressing, Mutagenesis, DNA Methylation Assay

Enrichment analysis of co-expressed genes of TCIRG1 in TCGA-KIRC. ( A ) Volcano maps showing the co-expression of TCIRG1 genes (FDR < 0.01, COR > 0.4). ( B ) The top fifty genes with the strongest correlation are shown in the heat map. ( C ) GO pathway analysis of TCIRG1 co-expressed genes in KIRC. ( D ) KEGG pathway analysis of TCIRG1 co-expressed gene in KIRC.

Journal: Cancers

Article Title: Integrative Analysis Identifies TCIRG1 as a Potential Prognostic and Immunotherapy-Relevant Biomarker Associated with Malignant Cell Migration in Clear Cell Renal Cell Carcinoma

doi: 10.3390/cancers14194583

Figure Lengend Snippet: Enrichment analysis of co-expressed genes of TCIRG1 in TCGA-KIRC. ( A ) Volcano maps showing the co-expression of TCIRG1 genes (FDR < 0.01, COR > 0.4). ( B ) The top fifty genes with the strongest correlation are shown in the heat map. ( C ) GO pathway analysis of TCIRG1 co-expressed genes in KIRC. ( D ) KEGG pathway analysis of TCIRG1 co-expressed gene in KIRC.

Article Snippet: Total proteins were then extracted, measured, and semi-dry transferred to PVDF (Millipore, Billerica, MA, USA) membranes after separation by 8–12% SDS-PAGE electrophoresis; PVDF membranes were first closed with TBS + Tween (TBST) solution containing 5% skim milk powder for 2 h, washed, and incubated with primary antibody at 4 °C overnight (TCIRG1, 12649-1-AP, Proteintech, 1:50); they were then rewashed and incubated for 2 h with a secondary antibody that was colored by horseradish peroxidase.

Techniques: Expressing

Correlation between TCIRG1 expression and tumor microenvironment score in KIRC. ( A ) BGN expression is associated with estimate score, Immunescore, and Stromalscore in renal cancer based on Pearson correlation analysis. ( B , C ) Relationship between OS of KIRC and Estimatedscore and Immunescore.(*** p < 0.001).

Journal: Cancers

Article Title: Integrative Analysis Identifies TCIRG1 as a Potential Prognostic and Immunotherapy-Relevant Biomarker Associated with Malignant Cell Migration in Clear Cell Renal Cell Carcinoma

doi: 10.3390/cancers14194583

Figure Lengend Snippet: Correlation between TCIRG1 expression and tumor microenvironment score in KIRC. ( A ) BGN expression is associated with estimate score, Immunescore, and Stromalscore in renal cancer based on Pearson correlation analysis. ( B , C ) Relationship between OS of KIRC and Estimatedscore and Immunescore.(*** p < 0.001).

Article Snippet: Total proteins were then extracted, measured, and semi-dry transferred to PVDF (Millipore, Billerica, MA, USA) membranes after separation by 8–12% SDS-PAGE electrophoresis; PVDF membranes were first closed with TBS + Tween (TBST) solution containing 5% skim milk powder for 2 h, washed, and incubated with primary antibody at 4 °C overnight (TCIRG1, 12649-1-AP, Proteintech, 1:50); they were then rewashed and incubated for 2 h with a secondary antibody that was colored by horseradish peroxidase.

Techniques: Expressing

TIIC profile and correlation analysis in kidney cancer samples. Pie charts showing the estimated proportions of different types of TIICs in renal tumor samples predicted by ( A ) quanTIseq and ( B ) CIBERSOR. Pearson correlation matrix of the proportions of different TIICs in the microenvironment of renal cancer quantified by ( C ) quanTIseq and ( D ) CIBERSORT. The size of each bubble and the shading of each small colored box represents the corresponding correlation value between two cells. ( E , F ) Lollipop plots showing the correlation between TCIRG1 expression and different TIIC ratios analyzed by quanTIseq and CIBERSORT.

Journal: Cancers

Article Title: Integrative Analysis Identifies TCIRG1 as a Potential Prognostic and Immunotherapy-Relevant Biomarker Associated with Malignant Cell Migration in Clear Cell Renal Cell Carcinoma

doi: 10.3390/cancers14194583

Figure Lengend Snippet: TIIC profile and correlation analysis in kidney cancer samples. Pie charts showing the estimated proportions of different types of TIICs in renal tumor samples predicted by ( A ) quanTIseq and ( B ) CIBERSOR. Pearson correlation matrix of the proportions of different TIICs in the microenvironment of renal cancer quantified by ( C ) quanTIseq and ( D ) CIBERSORT. The size of each bubble and the shading of each small colored box represents the corresponding correlation value between two cells. ( E , F ) Lollipop plots showing the correlation between TCIRG1 expression and different TIIC ratios analyzed by quanTIseq and CIBERSORT.

Article Snippet: Total proteins were then extracted, measured, and semi-dry transferred to PVDF (Millipore, Billerica, MA, USA) membranes after separation by 8–12% SDS-PAGE electrophoresis; PVDF membranes were first closed with TBS + Tween (TBST) solution containing 5% skim milk powder for 2 h, washed, and incubated with primary antibody at 4 °C overnight (TCIRG1, 12649-1-AP, Proteintech, 1:50); they were then rewashed and incubated for 2 h with a secondary antibody that was colored by horseradish peroxidase.

Techniques: Expressing

 TCIRG1  and immune cell biomarkers in RCC were correlated using GEPIA2 and Timer2.0.

Journal: Cancers

Article Title: Integrative Analysis Identifies TCIRG1 as a Potential Prognostic and Immunotherapy-Relevant Biomarker Associated with Malignant Cell Migration in Clear Cell Renal Cell Carcinoma

doi: 10.3390/cancers14194583

Figure Lengend Snippet: TCIRG1 and immune cell biomarkers in RCC were correlated using GEPIA2 and Timer2.0.

Article Snippet: Total proteins were then extracted, measured, and semi-dry transferred to PVDF (Millipore, Billerica, MA, USA) membranes after separation by 8–12% SDS-PAGE electrophoresis; PVDF membranes were first closed with TBS + Tween (TBST) solution containing 5% skim milk powder for 2 h, washed, and incubated with primary antibody at 4 °C overnight (TCIRG1, 12649-1-AP, Proteintech, 1:50); they were then rewashed and incubated for 2 h with a secondary antibody that was colored by horseradish peroxidase.

Techniques:

Division of subgroups according to TCIRG1 expression levels to predict potential immunotherapeutic responses in kidney cancer. ( A ) Immune checkpoint-associated genes are expressed in high- and low-TCIRG1 subpopulations. The Wilcoxon rank-sum test was used as a statistical significance test. ( B ) Tumor Immune Dysfunction and Exclusion (TIDE) score. ( C ) TCIRG1 expression differences between GSE67501-responding and non-responding groups. ( D – M ) IC50 differences between high- and low-TCIRG1 expression groups. (* p < 0.05, ** p < 0.01. *** p < 0.001).

Journal: Cancers

Article Title: Integrative Analysis Identifies TCIRG1 as a Potential Prognostic and Immunotherapy-Relevant Biomarker Associated with Malignant Cell Migration in Clear Cell Renal Cell Carcinoma

doi: 10.3390/cancers14194583

Figure Lengend Snippet: Division of subgroups according to TCIRG1 expression levels to predict potential immunotherapeutic responses in kidney cancer. ( A ) Immune checkpoint-associated genes are expressed in high- and low-TCIRG1 subpopulations. The Wilcoxon rank-sum test was used as a statistical significance test. ( B ) Tumor Immune Dysfunction and Exclusion (TIDE) score. ( C ) TCIRG1 expression differences between GSE67501-responding and non-responding groups. ( D – M ) IC50 differences between high- and low-TCIRG1 expression groups. (* p < 0.05, ** p < 0.01. *** p < 0.001).

Article Snippet: Total proteins were then extracted, measured, and semi-dry transferred to PVDF (Millipore, Billerica, MA, USA) membranes after separation by 8–12% SDS-PAGE electrophoresis; PVDF membranes were first closed with TBS + Tween (TBST) solution containing 5% skim milk powder for 2 h, washed, and incubated with primary antibody at 4 °C overnight (TCIRG1, 12649-1-AP, Proteintech, 1:50); they were then rewashed and incubated for 2 h with a secondary antibody that was colored by horseradish peroxidase.

Techniques: Expressing

( A ) Expression of TCIRG1 in different kidney cancer cell lines. TCIRG1 promotes the migratory ability of RCC cells. ( B , C ) qPCR Western Blot and ( D ) Western blotting showed that the expression of TCIRG1 was silenced by siRNA in 769P and caki1, respectively. Scratch wound-healing ( E , F , I , J ) and ( G , H , K , L ) transwell migration healing assays demonstrated TCIRG1-regulated migration ability. The scale bar of (E and I) is 250 μm, and the scale bar of (G and K) is 100 μm (* p < 0.05, *** p < 0.001).

Journal: Cancers

Article Title: Integrative Analysis Identifies TCIRG1 as a Potential Prognostic and Immunotherapy-Relevant Biomarker Associated with Malignant Cell Migration in Clear Cell Renal Cell Carcinoma

doi: 10.3390/cancers14194583

Figure Lengend Snippet: ( A ) Expression of TCIRG1 in different kidney cancer cell lines. TCIRG1 promotes the migratory ability of RCC cells. ( B , C ) qPCR Western Blot and ( D ) Western blotting showed that the expression of TCIRG1 was silenced by siRNA in 769P and caki1, respectively. Scratch wound-healing ( E , F , I , J ) and ( G , H , K , L ) transwell migration healing assays demonstrated TCIRG1-regulated migration ability. The scale bar of (E and I) is 250 μm, and the scale bar of (G and K) is 100 μm (* p < 0.05, *** p < 0.001).

Article Snippet: Total proteins were then extracted, measured, and semi-dry transferred to PVDF (Millipore, Billerica, MA, USA) membranes after separation by 8–12% SDS-PAGE electrophoresis; PVDF membranes were first closed with TBS + Tween (TBST) solution containing 5% skim milk powder for 2 h, washed, and incubated with primary antibody at 4 °C overnight (TCIRG1, 12649-1-AP, Proteintech, 1:50); they were then rewashed and incubated for 2 h with a secondary antibody that was colored by horseradish peroxidase.

Techniques: Expressing, Western Blot, Migration

Fig. 6. NaHS inhibited the interaction between LDHB and ATP6V1A and reduced ATP6V1A-dependent lysosomal acidification. A, B. MOVAs were treated with NaHS (200 μM) and PDGF (20 ng/mL) for 24 h. Whole-cell lysates were immunoprecipitated and then immunoblotted with antibodies against the indicated proteins. C. PLA was performed to detect the interaction of LDHB and ATP6V1A. Data were quantified in the lower panel. ***p < 0.001.Scale bar = 50 μm. D. Co-localization of LDHB and ATP6V1A in MOVAs was examined by immunofluorescence. Data were quantified in the lower panel. n = 6, ***p < 0.001. Scale bars = 50 μm. E. LDHB- GFP plasmid was transfected into MOVAs for 24 h and then stimulated with PDGF in the presence or absence of NaHS. Lyso-Tracker Red was used to label lysosomes. Data were quantified in the lower panel. n = 6, ***p < 0.001.Scale bars = 20 μm. F. Lysosomal pH of MOVAs was measured by FITC-dextran staining (0.5 mg/mL). Data were quantified in the right panel. n = 6, ***p < 0.001. Scale bars = 50 μm.

Journal: Redox biology

Article Title: Hydrogen sulfide attenuates disturbed flow-induced vascular remodeling by inhibiting LDHB-mediated autophagic flux.

doi: 10.1016/j.redox.2024.103456

Figure Lengend Snippet: Fig. 6. NaHS inhibited the interaction between LDHB and ATP6V1A and reduced ATP6V1A-dependent lysosomal acidification. A, B. MOVAs were treated with NaHS (200 μM) and PDGF (20 ng/mL) for 24 h. Whole-cell lysates were immunoprecipitated and then immunoblotted with antibodies against the indicated proteins. C. PLA was performed to detect the interaction of LDHB and ATP6V1A. Data were quantified in the lower panel. ***p < 0.001.Scale bar = 50 μm. D. Co-localization of LDHB and ATP6V1A in MOVAs was examined by immunofluorescence. Data were quantified in the lower panel. n = 6, ***p < 0.001. Scale bars = 50 μm. E. LDHB- GFP plasmid was transfected into MOVAs for 24 h and then stimulated with PDGF in the presence or absence of NaHS. Lyso-Tracker Red was used to label lysosomes. Data were quantified in the lower panel. n = 6, ***p < 0.001.Scale bars = 20 μm. F. Lysosomal pH of MOVAs was measured by FITC-dextran staining (0.5 mg/mL). Data were quantified in the right panel. n = 6, ***p < 0.001. Scale bars = 50 μm.

Article Snippet: Primary antibodies were: LDHB (Proteintech, 14824) and ATP6V1A (Santa Cruz, sc293336).

Techniques: Immunoprecipitation, Immunofluorescence, Plasmid Preparation, Transfection, Staining

Fig. 7. Identification of the domains of ATP6V1A and LDHB involved in their interaction. A. Schematic diagram illustrating the design of full-length HA-tagged ATP6V1A and the ATP6V1A truncates tagged with HA. B. HEK293T cells were co-transfected with these constructs, followed by IP assay using anti-Flag beads. Subsequent immunoblotting was performed with both anti-Flag and anti-HA antibodies to detect the expression of the constructs. C. The predicted structures of ATP6V1A and LDHB were generated using Alphafold. D. The conserved sequences containing L57 of ATP6V1A and S269 of LDHB were shown. E, F HEK293T cells were co-transfected with corresponding constructs and the cell lysates were collected for IP assays using beads conjugated with anti-Flag and anti-HA antibodies.

Journal: Redox biology

Article Title: Hydrogen sulfide attenuates disturbed flow-induced vascular remodeling by inhibiting LDHB-mediated autophagic flux.

doi: 10.1016/j.redox.2024.103456

Figure Lengend Snippet: Fig. 7. Identification of the domains of ATP6V1A and LDHB involved in their interaction. A. Schematic diagram illustrating the design of full-length HA-tagged ATP6V1A and the ATP6V1A truncates tagged with HA. B. HEK293T cells were co-transfected with these constructs, followed by IP assay using anti-Flag beads. Subsequent immunoblotting was performed with both anti-Flag and anti-HA antibodies to detect the expression of the constructs. C. The predicted structures of ATP6V1A and LDHB were generated using Alphafold. D. The conserved sequences containing L57 of ATP6V1A and S269 of LDHB were shown. E, F HEK293T cells were co-transfected with corresponding constructs and the cell lysates were collected for IP assays using beads conjugated with anti-Flag and anti-HA antibodies.

Article Snippet: Primary antibodies were: LDHB (Proteintech, 14824) and ATP6V1A (Santa Cruz, sc293336).

Techniques: Transfection, Construct, Western Blot, Expressing, Generated

Fig. 8. The expression of LDHB was up-regulated in VSMCs of human TAA and AAA. A. Co-localization of LDHB and ACTA2 in human TAA and AAA were analyzed by immunofluorescence staining. Data were quantified in the right panel. n = 6, ***p < 0.001. Scale bars = 50 μm. B. The mRNA level of LDHB in aortic tissues was detected by RT-PCR. n = 5, ***p < 0.001. C. Schematic diagram of this study. H2S attenuates DF-induced vascular remodeling by inhibiting the interaction between LDHB and ATP6V1A. The disruption of this interaction prevents lysosomal acidification and autophagic flux, thereby suppressing VSMC proliferation and migration.

Journal: Redox biology

Article Title: Hydrogen sulfide attenuates disturbed flow-induced vascular remodeling by inhibiting LDHB-mediated autophagic flux.

doi: 10.1016/j.redox.2024.103456

Figure Lengend Snippet: Fig. 8. The expression of LDHB was up-regulated in VSMCs of human TAA and AAA. A. Co-localization of LDHB and ACTA2 in human TAA and AAA were analyzed by immunofluorescence staining. Data were quantified in the right panel. n = 6, ***p < 0.001. Scale bars = 50 μm. B. The mRNA level of LDHB in aortic tissues was detected by RT-PCR. n = 5, ***p < 0.001. C. Schematic diagram of this study. H2S attenuates DF-induced vascular remodeling by inhibiting the interaction between LDHB and ATP6V1A. The disruption of this interaction prevents lysosomal acidification and autophagic flux, thereby suppressing VSMC proliferation and migration.

Article Snippet: Primary antibodies were: LDHB (Proteintech, 14824) and ATP6V1A (Santa Cruz, sc293336).

Techniques: Expressing, Immunofluorescence, Staining, Reverse Transcription Polymerase Chain Reaction, Disruption, Migration

Journal: eLife

Article Title: Optical detection of three modes of endocytosis at hippocampal synapses

doi: 10.7554/eLife.36097

Figure Lengend Snippet:

Article Snippet: Antibody , Rabbit polyclonal anti-V0a1 , Synaptic Systems , Catalog # 109 002 , dil. 1:100.

Techniques: Plasmid Preparation, Software

Figure 3. NEO214 has an adverse effect on lysosomal function and blocked autophagic flux in glioma cells dependent on MTOR signaling. (A-B) Expression analysis of the autophagy-lysosome relevant genes in 100 μmol/L NEO214-treated U251 and T98G cells. (C) WB analysis of ATP6V1G1, ATP6V1D, ATP6V1H and ATP6V1C1 in U251 and T98G cells were treated with NEO214(100 μmol/L) in full-medium 24 h. (D) NEO214 does not affect the autophagosome formation process in glioma cells. Western blot analysis of the protein expression of BECN1, ATG3, ATG5, ATG9A, LC3, and SQSTM1 in U251 and T98G cells treated by 100 μmol/L NEO214 for 24 h. (E) Western blot analysis of MTOR signaling proteins expressions in U251 and T98G cells treated by 100 μmol/L NEO214 24 h. (n = 3; *, P < 0.05; **, P < 0.01; ***, P < 0.001).

Journal: Autophagy

Article Title: Inhibition of autophagy and induction of glioblastoma cell death by NEO214, a perillyl alcohol-rolipram conjugate.

doi: 10.1080/15548627.2023.2242696

Figure Lengend Snippet: Figure 3. NEO214 has an adverse effect on lysosomal function and blocked autophagic flux in glioma cells dependent on MTOR signaling. (A-B) Expression analysis of the autophagy-lysosome relevant genes in 100 μmol/L NEO214-treated U251 and T98G cells. (C) WB analysis of ATP6V1G1, ATP6V1D, ATP6V1H and ATP6V1C1 in U251 and T98G cells were treated with NEO214(100 μmol/L) in full-medium 24 h. (D) NEO214 does not affect the autophagosome formation process in glioma cells. Western blot analysis of the protein expression of BECN1, ATG3, ATG5, ATG9A, LC3, and SQSTM1 in U251 and T98G cells treated by 100 μmol/L NEO214 for 24 h. (E) Western blot analysis of MTOR signaling proteins expressions in U251 and T98G cells treated by 100 μmol/L NEO214 24 h. (n = 3; *, P < 0.05; **, P < 0.01; ***, P < 0.001).

Article Snippet: Immunoblotting was performed with PARP (Cell Signaling Technology, CS9542), LC3B (Cell Signaling Technology, CS-2775), SQSTM1/ p62 (Cell Signaling Technology, CS-5114), BECN1/beclin 1 (Cell Signaling Technology, CS-3738), RPTOR/raptor (Cell Signaling Technology, CS-48648), RICTOR (Cell Signaling Technology, CS-2140), p-AKT (Cell Signaling Technology, CS-4058), p-RPS6KB/p70S6K (Cell Signaling Technology, CS-9206), RPS6KB/p70S6K (Cell Signaling Technology, CS9202), p-MTOR (Cell Signaling Technology, CS-2971), p-EIF4EBP1 (Cell Signaling Technology, CS-9456), EIF4EBP1 (Cell Signaling Technology, CS-9452), MGMT (Cell Signaling Technology, CS-2739S), CTSD/cathepsin D (Cell Signaling Technology, CS-2284), ATG3 (Cell Signaling Technology, CS-3415), ATG5 (Cell Signaling Technology, CS-12994), TP53 (Cell Signaling Technology, CS-9282), cleaved CASP7/caspase 7 (Cell Signaling Technology, CS-9491), TUBA1B/α-Tubulin (Cell Signaling Technology, CS-2125), LMNB1/Lamin B1 (Cell Signaling Technology, CS-13435), ATP6V1A (Abcam, ab -199,326), ATP6V1B2 (Abcam, ab -73,404), MTOR (Abcam, ab-2732), and CTSB/cathepsin B (Abcam, ab58802), TFEB (ThermoFisher Scientific, PAS-34360; 1:100 for IP, 1:200 for IF, 1:1000 for WB), TSC2 (Proteintech, 24601–1-AP), TSC1 (Proteintech, 20988–1-AP), ATP6V1D (Proteintech, 14920– 1-AP), ATP6V1G1 (Proteintech, 16143–1-AP), ATP6V1H (Proteintech, 26683–1-AP), ATP6V1C1 (Proteintech, 16054– 1-AP), AKT (GeneTex, GTX-121937), ATG9A (GeneTex, EPR-5973), CCND1/cyclin D1 (Santa Cruz Biotechnology, SC-753), CCND2/cyclin D2 (Santa Cruz Biotechnology, SC754), CCNDE1/cyclin E1 (Santa Cruz Biotechnology, SC377100), ACTB/actin (Santa Cruz Biotechnology, SC-8432), CTSB/capthepsin D (Santa Cruz Biotechnology, sc -377,124).

Techniques: Expressing, Western Blot

Viral findings in mild versus severe SARS-CoV2 infection. The control lungs showed no viral protein or RNA (panel A) whereas the lung tissue from someone who died of COVID-19 showed high viral RNA (panel B) and the spike protein subunit 2 (panel C) in the same alveolar wall distribution. Similarly, note the absence of the viral spike protein in the uninfected nasopharynx swab (panel D) and the strong signal for spike subunit 1 (panel E) and spike subunit 2 proteins (panel F) in glandular cells from a person with mild disease. NP – nasopharyngeal, NL – normal control, and the signal is brown due to DAB with hematoxylin counterstain. (For interpretation of the references to color in this figure legend, the reader is referred to the web version of this article.)

Journal: Annals of Diagnostic Pathology

Article Title: The differential immune response in mild versus fatal SARS-CoV2 infection ☆

doi: 10.1016/j.anndiagpath.2022.152032

Figure Lengend Snippet: Viral findings in mild versus severe SARS-CoV2 infection. The control lungs showed no viral protein or RNA (panel A) whereas the lung tissue from someone who died of COVID-19 showed high viral RNA (panel B) and the spike protein subunit 2 (panel C) in the same alveolar wall distribution. Similarly, note the absence of the viral spike protein in the uninfected nasopharynx swab (panel D) and the strong signal for spike subunit 1 (panel E) and spike subunit 2 proteins (panel F) in glandular cells from a person with mild disease. NP – nasopharyngeal, NL – normal control, and the signal is brown due to DAB with hematoxylin counterstain. (For interpretation of the references to color in this figure legend, the reader is referred to the web version of this article.)

Article Snippet: SARS-CoV2 specific antibodies against nucleocapsid (catalogue #9099), spike subunit 1 (#9083), and spike subunit 2 (#9123) were from ProSci (Poway, CA).

Techniques: Infection, Control

Compilation of the immune response to mild infection in the nasopharyngeal swabs. <xref ref-type= a " width="100%" height="100%">

Journal: Annals of Diagnostic Pathology

Article Title: The differential immune response in mild versus fatal SARS-CoV2 infection ☆

doi: 10.1016/j.anndiagpath.2022.152032

Figure Lengend Snippet: Compilation of the immune response to mild infection in the nasopharyngeal swabs. a

Article Snippet: SARS-CoV2 specific antibodies against nucleocapsid (catalogue #9099), spike subunit 1 (#9083), and spike subunit 2 (#9123) were from ProSci (Poway, CA).

Techniques: Infection

Compilation of the immune response to fatal infection in the COVID-lungs. <xref ref-type= a " width="100%" height="100%">

Journal: Annals of Diagnostic Pathology

Article Title: The differential immune response in mild versus fatal SARS-CoV2 infection ☆

doi: 10.1016/j.anndiagpath.2022.152032

Figure Lengend Snippet: Compilation of the immune response to fatal infection in the COVID-lungs. a

Article Snippet: SARS-CoV2 specific antibodies against nucleocapsid (catalogue #9099), spike subunit 1 (#9083), and spike subunit 2 (#9123) were from ProSci (Poway, CA).

Techniques: Infection, Virus

Immune response in mild versus fatal SARS-CoV2 infection. The figure shows a graphic representation of the fold changes from baseline in the nasopharyngeal swabs positive for SARS-CoV2 (blue columns) as well as the lung tissues from fatal COVID-19 that either had very high copy SARS-CoV2 (orange columns) or were not associated with SARS-CoV2 infection (gray columns). (For interpretation of the references to color in this figure legend, the reader is referred to the web version of this article.)

Journal: Annals of Diagnostic Pathology

Article Title: The differential immune response in mild versus fatal SARS-CoV2 infection ☆

doi: 10.1016/j.anndiagpath.2022.152032

Figure Lengend Snippet: Immune response in mild versus fatal SARS-CoV2 infection. The figure shows a graphic representation of the fold changes from baseline in the nasopharyngeal swabs positive for SARS-CoV2 (blue columns) as well as the lung tissues from fatal COVID-19 that either had very high copy SARS-CoV2 (orange columns) or were not associated with SARS-CoV2 infection (gray columns). (For interpretation of the references to color in this figure legend, the reader is referred to the web version of this article.)

Article Snippet: SARS-CoV2 specific antibodies against nucleocapsid (catalogue #9099), spike subunit 1 (#9083), and spike subunit 2 (#9123) were from ProSci (Poway, CA).

Techniques: Infection

In situ demonstration of the immune response in mild versus fatal SARS-CoV2 infection. Note the absence of a CD3 response in the uninfected nasopharynx swab (panel A) and the strong infiltration by these cells in an infected swab from a person with mild disease (panel B). Similarly, the control nasopharynx sample shows no PDL1 expression (panel C) whereas the infected nasopharynx shows a strong PDL1 response (panel D). Note that the lung from a fatal COVID-19 case not associated with viral infection did show a strong CD8 response (panel E) whereas this lung tissue from someone who died of COVID-19 that was strongly positive for SARS-CoV2 did not show a CD8 response (panel F). The control lungs showed a very weak PDL1 signal (panel G) whereas the COVID-19 lungs with high viral copy number did show strong PDL1 expression (panel H). NP – nasopharyngeal, NL – normal control, and the signal is brown due to DAB with hematoxylin counterstain. (For interpretation of the references to color in this figure legend, the reader is referred to the web version of this article.)

Journal: Annals of Diagnostic Pathology

Article Title: The differential immune response in mild versus fatal SARS-CoV2 infection ☆

doi: 10.1016/j.anndiagpath.2022.152032

Figure Lengend Snippet: In situ demonstration of the immune response in mild versus fatal SARS-CoV2 infection. Note the absence of a CD3 response in the uninfected nasopharynx swab (panel A) and the strong infiltration by these cells in an infected swab from a person with mild disease (panel B). Similarly, the control nasopharynx sample shows no PDL1 expression (panel C) whereas the infected nasopharynx shows a strong PDL1 response (panel D). Note that the lung from a fatal COVID-19 case not associated with viral infection did show a strong CD8 response (panel E) whereas this lung tissue from someone who died of COVID-19 that was strongly positive for SARS-CoV2 did not show a CD8 response (panel F). The control lungs showed a very weak PDL1 signal (panel G) whereas the COVID-19 lungs with high viral copy number did show strong PDL1 expression (panel H). NP – nasopharyngeal, NL – normal control, and the signal is brown due to DAB with hematoxylin counterstain. (For interpretation of the references to color in this figure legend, the reader is referred to the web version of this article.)

Article Snippet: SARS-CoV2 specific antibodies against nucleocapsid (catalogue #9099), spike subunit 1 (#9083), and spike subunit 2 (#9123) were from ProSci (Poway, CA).

Techniques: In Situ, Infection, Control, Expressing

In situ demonstration of the clotting and complement activation in the fatal COVID-19 lungs. Note the absence of complement component 6 in the normal lung (panel A) as well as the lung from a fatal COVID-19 case that did not contain detectable SARS-CoV2 RNA (panel B). Panel C shows that the signal for complement component 6 in the COVID-19 lung tissue associated with high SARS-CoV2 copy number localizes only to the alveolar septa (arrows) which also shows a strong signal for fibrinogen (panel D); no signal is evident in the small vessels (oval). Panel E shows the lack of signal for CD41 in the normal lung controls. In comparison, note the CD41+ platelet aggregates in the small vessels in a lung from a person who died of COVID-19 associated with high viral copy number (panel F) as well as from the same lung that was not associated with SARS-CoV2 infection (panel G). However, note that the CD41 signal localizes only to the alveolar septa in the lung with high copy SARS-CoV2 (arrow, panel F). Co-localization of CD41 (fluorescent red) with SARS-CoV2 RNA (fluorescent green) documents that CD41 strongly co-expressed with the viral RNA in the lung samples with high copy viral RNA (seen as fluorescent yellow, panel H). NL – normal control, and the signal in panels A–D is brown due to DAB and fast red in panels E–G with hematoxylin counterstain. (For interpretation of the references to color in this figure legend, the reader is referred to the web version of this article.)

Journal: Annals of Diagnostic Pathology

Article Title: The differential immune response in mild versus fatal SARS-CoV2 infection ☆

doi: 10.1016/j.anndiagpath.2022.152032

Figure Lengend Snippet: In situ demonstration of the clotting and complement activation in the fatal COVID-19 lungs. Note the absence of complement component 6 in the normal lung (panel A) as well as the lung from a fatal COVID-19 case that did not contain detectable SARS-CoV2 RNA (panel B). Panel C shows that the signal for complement component 6 in the COVID-19 lung tissue associated with high SARS-CoV2 copy number localizes only to the alveolar septa (arrows) which also shows a strong signal for fibrinogen (panel D); no signal is evident in the small vessels (oval). Panel E shows the lack of signal for CD41 in the normal lung controls. In comparison, note the CD41+ platelet aggregates in the small vessels in a lung from a person who died of COVID-19 associated with high viral copy number (panel F) as well as from the same lung that was not associated with SARS-CoV2 infection (panel G). However, note that the CD41 signal localizes only to the alveolar septa in the lung with high copy SARS-CoV2 (arrow, panel F). Co-localization of CD41 (fluorescent red) with SARS-CoV2 RNA (fluorescent green) documents that CD41 strongly co-expressed with the viral RNA in the lung samples with high copy viral RNA (seen as fluorescent yellow, panel H). NL – normal control, and the signal in panels A–D is brown due to DAB and fast red in panels E–G with hematoxylin counterstain. (For interpretation of the references to color in this figure legend, the reader is referred to the web version of this article.)

Article Snippet: SARS-CoV2 specific antibodies against nucleocapsid (catalogue #9099), spike subunit 1 (#9083), and spike subunit 2 (#9123) were from ProSci (Poway, CA).

Techniques: In Situ, Coagulation, Activation Assay, Comparison, Infection, Control

Correlation of the H&E findings with the viral load in fatal COVID-19. The figure shows a graphic representation of the histologic findings in the lung tissues from people who died of COVID-19 where there was high viral copy number (orange columns) and those not associated with direct SARS-CoV2 infection (blue columns). (For interpretation of the references to color in this figure legend, the reader is referred to the web version of this article.)

Journal: Annals of Diagnostic Pathology

Article Title: The differential immune response in mild versus fatal SARS-CoV2 infection ☆

doi: 10.1016/j.anndiagpath.2022.152032

Figure Lengend Snippet: Correlation of the H&E findings with the viral load in fatal COVID-19. The figure shows a graphic representation of the histologic findings in the lung tissues from people who died of COVID-19 where there was high viral copy number (orange columns) and those not associated with direct SARS-CoV2 infection (blue columns). (For interpretation of the references to color in this figure legend, the reader is referred to the web version of this article.)

Article Snippet: SARS-CoV2 specific antibodies against nucleocapsid (catalogue #9099), spike subunit 1 (#9083), and spike subunit 2 (#9123) were from ProSci (Poway, CA).

Techniques: Infection

H&E findings of mild versus fatal SARS-CoV2 infection. Panels A–C compare the cytologic findings in the normal nasopharynx (panel A) and mild infection (panel B); note that the glandular cells show degenerative changes that is highlighted with the EMA immunohistochemistry test (panel C). Panels D–F show successively high magnifications in a lung from a person who died of COVID-19 in which viral RNA was not evident; note the presence of extensive organizing pneumonia with scattered chronic inflammatory infiltrates. Panels G-I show successively high magnifications in a lung from a person who died of COVID-19 with high copy viral RNA; note the diffuse alveolar damage characterized by hyaline membrane formation, hemorrhage, and destruction of lining pneumocytes.

Journal: Annals of Diagnostic Pathology

Article Title: The differential immune response in mild versus fatal SARS-CoV2 infection ☆

doi: 10.1016/j.anndiagpath.2022.152032

Figure Lengend Snippet: H&E findings of mild versus fatal SARS-CoV2 infection. Panels A–C compare the cytologic findings in the normal nasopharynx (panel A) and mild infection (panel B); note that the glandular cells show degenerative changes that is highlighted with the EMA immunohistochemistry test (panel C). Panels D–F show successively high magnifications in a lung from a person who died of COVID-19 in which viral RNA was not evident; note the presence of extensive organizing pneumonia with scattered chronic inflammatory infiltrates. Panels G-I show successively high magnifications in a lung from a person who died of COVID-19 with high copy viral RNA; note the diffuse alveolar damage characterized by hyaline membrane formation, hemorrhage, and destruction of lining pneumocytes.

Article Snippet: SARS-CoV2 specific antibodies against nucleocapsid (catalogue #9099), spike subunit 1 (#9083), and spike subunit 2 (#9123) were from ProSci (Poway, CA).

Techniques: Infection, Immunohistochemistry, Membrane