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Galectin Therapeutics galectin-3 puncta formation
Galectin 3 Puncta Formation, supplied by Galectin Therapeutics, 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/galectin-3+puncta+formation/galectin+3/bio_rxiv__2025__05__06__652401-133-5-5
Average 90 stars, based on 1 article reviews
galectin-3 puncta formation - by Bioz Stars, 2026-09
90/100 stars

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Related Articles

Marker:

Article Title: VirPorters: Insights into the action of cationic and histidine-rich cell-penetrating peptides.
Article Snippet: The utilization of nanoparticles for the intracellular delivery of theranostic agents faces one substantial limitation.. Sequestration in intracellular vesicles prevents them from reaching the desired location in the cytoplasm or nucleus to deliver their cargo.. We investigated whether three different cell-penetrating peptides (CPPs), namely, octa-arginine R8, polyhistidine KH27K and histidine-rich LAH4, could promote cytosolic and/or nuclear transfer of unique model nanoparticles—pseudovirions derived from murine polyomavirus.

Article Title: LAMP3 transfer via extracellular particles induces apoptosis in Sjögren’s disease
Article Snippet: Galectin-3 puncta formation indicates a loss of lysosomal membrane integrity as a marker of LMP, which may imply release of lysosomal digestive enzymes into the cell cytoplasm .

Article Title: FASN Inactivation-Induced Progranulin (GRN) Expression Promotes Lysosome-Dependent Cell Death to Suppress Leukemogenesis
Article Snippet: In our study, we observed that the marker of LMP, Galectin-3 puncta formation, was significantly increased in FASN-depleted cells ( ).

Article Title: FASN Inactivation-Induced Progranulin (GRN) Expression Promotes Lysosome-Dependent Cell Death to Suppress Leukemogenesis
Article Snippet: In support of this hypothesis, Galectin-3 puncta formation, a marker of LMP , was accumulated in FASN-depleted MOLM-13 cells ( and fig. S12C).

Article Title: Lysosome-Associated Membrane Protein 3 Induces Lysosome-Dependent Cell Death by Impairing Autophagic Caspase 8 Degradation in the Salivary Glands of Individuals With Sjögren's Disease.
Article Snippet: Objective.. Lysosome-associated membrane protein 3 (LAMP3) overexpression is implicated in the development and progression of Sjögren’s disease (SjD) by inducing lysosomal membrane permeabilization (LMP) and apoptotic cell death in salivary gland epithelium.. The aim of this study was to clarify the molecular details of LAMP3-induced lysosome-dependent cell death and to test lysosomal biogenesis as a therapeutic intervention.

Inhibition:

Article Title: VirPorters: Insights into the action of cationic and histidine-rich cell-penetrating peptides.
Article Snippet: The utilization of nanoparticles for the intracellular delivery of theranostic agents faces one substantial limitation.. Sequestration in intracellular vesicles prevents them from reaching the desired location in the cytoplasm or nucleus to deliver their cargo.. We investigated whether three different cell-penetrating peptides (CPPs), namely, octa-arginine R8, polyhistidine KH27K and histidine-rich LAH4, could promote cytosolic and/or nuclear transfer of unique model nanoparticles—pseudovirions derived from murine polyomavirus.

Article Title: LAMP3 transfer via extracellular particles induces apoptosis in Sjögren’s disease
Article Snippet: Galectin-3 puncta formation indicates a loss of lysosomal membrane integrity as a marker of LMP, which may imply release of lysosomal digestive enzymes into the cell cytoplasm .

Article Title: FASN Inactivation-Induced Progranulin (GRN) Expression Promotes Lysosome-Dependent Cell Death to Suppress Leukemogenesis
Article Snippet: In our study, we observed that the marker of LMP, Galectin-3 puncta formation, was significantly increased in FASN-depleted cells ( ).

Article Title: FASN Inactivation-Induced Progranulin (GRN) Expression Promotes Lysosome-Dependent Cell Death to Suppress Leukemogenesis
Article Snippet: In support of this hypothesis, Galectin-3 puncta formation, a marker of LMP , was accumulated in FASN-depleted MOLM-13 cells ( and fig. S12C).

Article Title: Lysosome-Associated Membrane Protein 3 Induces Lysosome-Dependent Cell Death by Impairing Autophagic Caspase 8 Degradation in the Salivary Glands of Individuals With Sjögren's Disease.
Article Snippet: Objective.. Lysosome-associated membrane protein 3 (LAMP3) overexpression is implicated in the development and progression of Sjögren’s disease (SjD) by inducing lysosomal membrane permeabilization (LMP) and apoptotic cell death in salivary gland epithelium.. The aim of this study was to clarify the molecular details of LAMP3-induced lysosome-dependent cell death and to test lysosomal biogenesis as a therapeutic intervention.

Staining:

Article Title: VirPorters: Insights into the action of cationic and histidine-rich cell-penetrating peptides.
Article Snippet: The utilization of nanoparticles for the intracellular delivery of theranostic agents faces one substantial limitation.. Sequestration in intracellular vesicles prevents them from reaching the desired location in the cytoplasm or nucleus to deliver their cargo.. We investigated whether three different cell-penetrating peptides (CPPs), namely, octa-arginine R8, polyhistidine KH27K and histidine-rich LAH4, could promote cytosolic and/or nuclear transfer of unique model nanoparticles—pseudovirions derived from murine polyomavirus.

Article Title: LAMP3 transfer via extracellular particles induces apoptosis in Sjögren’s disease
Article Snippet: Galectin-3 puncta formation indicates a loss of lysosomal membrane integrity as a marker of LMP, which may imply release of lysosomal digestive enzymes into the cell cytoplasm .

Article Title: FASN Inactivation-Induced Progranulin (GRN) Expression Promotes Lysosome-Dependent Cell Death to Suppress Leukemogenesis
Article Snippet: In our study, we observed that the marker of LMP, Galectin-3 puncta formation, was significantly increased in FASN-depleted cells ( ).

Article Title: FASN Inactivation-Induced Progranulin (GRN) Expression Promotes Lysosome-Dependent Cell Death to Suppress Leukemogenesis
Article Snippet: In support of this hypothesis, Galectin-3 puncta formation, a marker of LMP , was accumulated in FASN-depleted MOLM-13 cells ( and fig. S12C).

Article Title: Lysosome-Associated Membrane Protein 3 Induces Lysosome-Dependent Cell Death by Impairing Autophagic Caspase 8 Degradation in the Salivary Glands of Individuals With Sjögren's Disease.
Article Snippet: Objective.. Lysosome-associated membrane protein 3 (LAMP3) overexpression is implicated in the development and progression of Sjögren’s disease (SjD) by inducing lysosomal membrane permeabilization (LMP) and apoptotic cell death in salivary gland epithelium.. The aim of this study was to clarify the molecular details of LAMP3-induced lysosome-dependent cell death and to test lysosomal biogenesis as a therapeutic intervention.

Fluorescence:

Article Title: VirPorters: Insights into the action of cationic and histidine-rich cell-penetrating peptides.
Article Snippet: The utilization of nanoparticles for the intracellular delivery of theranostic agents faces one substantial limitation.. Sequestration in intracellular vesicles prevents them from reaching the desired location in the cytoplasm or nucleus to deliver their cargo.. We investigated whether three different cell-penetrating peptides (CPPs), namely, octa-arginine R8, polyhistidine KH27K and histidine-rich LAH4, could promote cytosolic and/or nuclear transfer of unique model nanoparticles—pseudovirions derived from murine polyomavirus.

Article Title: LAMP3 transfer via extracellular particles induces apoptosis in Sjögren’s disease
Article Snippet: Galectin-3 puncta formation indicates a loss of lysosomal membrane integrity as a marker of LMP, which may imply release of lysosomal digestive enzymes into the cell cytoplasm .

Article Title: FASN Inactivation-Induced Progranulin (GRN) Expression Promotes Lysosome-Dependent Cell Death to Suppress Leukemogenesis
Article Snippet: In our study, we observed that the marker of LMP, Galectin-3 puncta formation, was significantly increased in FASN-depleted cells ( ).

Article Title: FASN Inactivation-Induced Progranulin (GRN) Expression Promotes Lysosome-Dependent Cell Death to Suppress Leukemogenesis
Article Snippet: In support of this hypothesis, Galectin-3 puncta formation, a marker of LMP , was accumulated in FASN-depleted MOLM-13 cells ( and fig. S12C).

Article Title: Lysosome-Associated Membrane Protein 3 Induces Lysosome-Dependent Cell Death by Impairing Autophagic Caspase 8 Degradation in the Salivary Glands of Individuals With Sjögren's Disease.
Article Snippet: Objective.. Lysosome-associated membrane protein 3 (LAMP3) overexpression is implicated in the development and progression of Sjögren’s disease (SjD) by inducing lysosomal membrane permeabilization (LMP) and apoptotic cell death in salivary gland epithelium.. The aim of this study was to clarify the molecular details of LAMP3-induced lysosome-dependent cell death and to test lysosomal biogenesis as a therapeutic intervention.

Microscopy:

Article Title: VirPorters: Insights into the action of cationic and histidine-rich cell-penetrating peptides.
Article Snippet: The utilization of nanoparticles for the intracellular delivery of theranostic agents faces one substantial limitation.. Sequestration in intracellular vesicles prevents them from reaching the desired location in the cytoplasm or nucleus to deliver their cargo.. We investigated whether three different cell-penetrating peptides (CPPs), namely, octa-arginine R8, polyhistidine KH27K and histidine-rich LAH4, could promote cytosolic and/or nuclear transfer of unique model nanoparticles—pseudovirions derived from murine polyomavirus.

Article Title: LAMP3 transfer via extracellular particles induces apoptosis in Sjögren’s disease
Article Snippet: Galectin-3 puncta formation indicates a loss of lysosomal membrane integrity as a marker of LMP, which may imply release of lysosomal digestive enzymes into the cell cytoplasm .

Article Title: FASN Inactivation-Induced Progranulin (GRN) Expression Promotes Lysosome-Dependent Cell Death to Suppress Leukemogenesis
Article Snippet: In our study, we observed that the marker of LMP, Galectin-3 puncta formation, was significantly increased in FASN-depleted cells ( ).

Article Title: FASN Inactivation-Induced Progranulin (GRN) Expression Promotes Lysosome-Dependent Cell Death to Suppress Leukemogenesis
Article Snippet: In support of this hypothesis, Galectin-3 puncta formation, a marker of LMP , was accumulated in FASN-depleted MOLM-13 cells ( and fig. S12C).

Article Title: Lysosome-Associated Membrane Protein 3 Induces Lysosome-Dependent Cell Death by Impairing Autophagic Caspase 8 Degradation in the Salivary Glands of Individuals With Sjögren's Disease.
Article Snippet: Objective.. Lysosome-associated membrane protein 3 (LAMP3) overexpression is implicated in the development and progression of Sjögren’s disease (SjD) by inducing lysosomal membrane permeabilization (LMP) and apoptotic cell death in salivary gland epithelium.. The aim of this study was to clarify the molecular details of LAMP3-induced lysosome-dependent cell death and to test lysosomal biogenesis as a therapeutic intervention.

Control:

Article Title: VirPorters: Insights into the action of cationic and histidine-rich cell-penetrating peptides.
Article Snippet: The utilization of nanoparticles for the intracellular delivery of theranostic agents faces one substantial limitation.. Sequestration in intracellular vesicles prevents them from reaching the desired location in the cytoplasm or nucleus to deliver their cargo.. We investigated whether three different cell-penetrating peptides (CPPs), namely, octa-arginine R8, polyhistidine KH27K and histidine-rich LAH4, could promote cytosolic and/or nuclear transfer of unique model nanoparticles—pseudovirions derived from murine polyomavirus.

Article Title: LAMP3 transfer via extracellular particles induces apoptosis in Sjögren’s disease
Article Snippet: Galectin-3 puncta formation indicates a loss of lysosomal membrane integrity as a marker of LMP, which may imply release of lysosomal digestive enzymes into the cell cytoplasm .

Article Title: FASN Inactivation-Induced Progranulin (GRN) Expression Promotes Lysosome-Dependent Cell Death to Suppress Leukemogenesis
Article Snippet: In our study, we observed that the marker of LMP, Galectin-3 puncta formation, was significantly increased in FASN-depleted cells ( ).

Article Title: FASN Inactivation-Induced Progranulin (GRN) Expression Promotes Lysosome-Dependent Cell Death to Suppress Leukemogenesis
Article Snippet: In support of this hypothesis, Galectin-3 puncta formation, a marker of LMP , was accumulated in FASN-depleted MOLM-13 cells ( and fig. S12C).

Article Title: Lysosome-Associated Membrane Protein 3 Induces Lysosome-Dependent Cell Death by Impairing Autophagic Caspase 8 Degradation in the Salivary Glands of Individuals With Sjögren's Disease.
Article Snippet: Objective.. Lysosome-associated membrane protein 3 (LAMP3) overexpression is implicated in the development and progression of Sjögren’s disease (SjD) by inducing lysosomal membrane permeabilization (LMP) and apoptotic cell death in salivary gland epithelium.. The aim of this study was to clarify the molecular details of LAMP3-induced lysosome-dependent cell death and to test lysosomal biogenesis as a therapeutic intervention.

Luciferase:

Article Title: VirPorters: Insights into the action of cationic and histidine-rich cell-penetrating peptides.
Article Snippet: The utilization of nanoparticles for the intracellular delivery of theranostic agents faces one substantial limitation.. Sequestration in intracellular vesicles prevents them from reaching the desired location in the cytoplasm or nucleus to deliver their cargo.. We investigated whether three different cell-penetrating peptides (CPPs), namely, octa-arginine R8, polyhistidine KH27K and histidine-rich LAH4, could promote cytosolic and/or nuclear transfer of unique model nanoparticles—pseudovirions derived from murine polyomavirus.

Article Title: LAMP3 transfer via extracellular particles induces apoptosis in Sjögren’s disease
Article Snippet: Galectin-3 puncta formation indicates a loss of lysosomal membrane integrity as a marker of LMP, which may imply release of lysosomal digestive enzymes into the cell cytoplasm .

Article Title: FASN Inactivation-Induced Progranulin (GRN) Expression Promotes Lysosome-Dependent Cell Death to Suppress Leukemogenesis
Article Snippet: In our study, we observed that the marker of LMP, Galectin-3 puncta formation, was significantly increased in FASN-depleted cells ( ).

Article Title: FASN Inactivation-Induced Progranulin (GRN) Expression Promotes Lysosome-Dependent Cell Death to Suppress Leukemogenesis
Article Snippet: In support of this hypothesis, Galectin-3 puncta formation, a marker of LMP , was accumulated in FASN-depleted MOLM-13 cells ( and fig. S12C).

Article Title: Lysosome-Associated Membrane Protein 3 Induces Lysosome-Dependent Cell Death by Impairing Autophagic Caspase 8 Degradation in the Salivary Glands of Individuals With Sjögren's Disease.
Article Snippet: Objective.. Lysosome-associated membrane protein 3 (LAMP3) overexpression is implicated in the development and progression of Sjögren’s disease (SjD) by inducing lysosomal membrane permeabilization (LMP) and apoptotic cell death in salivary gland epithelium.. The aim of this study was to clarify the molecular details of LAMP3-induced lysosome-dependent cell death and to test lysosomal biogenesis as a therapeutic intervention.

Activity Assay:

Article Title: VirPorters: Insights into the action of cationic and histidine-rich cell-penetrating peptides.
Article Snippet: The utilization of nanoparticles for the intracellular delivery of theranostic agents faces one substantial limitation.. Sequestration in intracellular vesicles prevents them from reaching the desired location in the cytoplasm or nucleus to deliver their cargo.. We investigated whether three different cell-penetrating peptides (CPPs), namely, octa-arginine R8, polyhistidine KH27K and histidine-rich LAH4, could promote cytosolic and/or nuclear transfer of unique model nanoparticles—pseudovirions derived from murine polyomavirus.

Article Title: LAMP3 transfer via extracellular particles induces apoptosis in Sjögren’s disease
Article Snippet: Galectin-3 puncta formation indicates a loss of lysosomal membrane integrity as a marker of LMP, which may imply release of lysosomal digestive enzymes into the cell cytoplasm .

Article Title: FASN Inactivation-Induced Progranulin (GRN) Expression Promotes Lysosome-Dependent Cell Death to Suppress Leukemogenesis
Article Snippet: In our study, we observed that the marker of LMP, Galectin-3 puncta formation, was significantly increased in FASN-depleted cells ( ).

Article Title: FASN Inactivation-Induced Progranulin (GRN) Expression Promotes Lysosome-Dependent Cell Death to Suppress Leukemogenesis
Article Snippet: In support of this hypothesis, Galectin-3 puncta formation, a marker of LMP , was accumulated in FASN-depleted MOLM-13 cells ( and fig. S12C).

Article Title: Lysosome-Associated Membrane Protein 3 Induces Lysosome-Dependent Cell Death by Impairing Autophagic Caspase 8 Degradation in the Salivary Glands of Individuals With Sjögren's Disease.
Article Snippet: Objective.. Lysosome-associated membrane protein 3 (LAMP3) overexpression is implicated in the development and progression of Sjögren’s disease (SjD) by inducing lysosomal membrane permeabilization (LMP) and apoptotic cell death in salivary gland epithelium.. The aim of this study was to clarify the molecular details of LAMP3-induced lysosome-dependent cell death and to test lysosomal biogenesis as a therapeutic intervention.

Construct:

Article Title: VirPorters: Insights into the action of cationic and histidine-rich cell-penetrating peptides.
Article Snippet: The utilization of nanoparticles for the intracellular delivery of theranostic agents faces one substantial limitation.. Sequestration in intracellular vesicles prevents them from reaching the desired location in the cytoplasm or nucleus to deliver their cargo.. We investigated whether three different cell-penetrating peptides (CPPs), namely, octa-arginine R8, polyhistidine KH27K and histidine-rich LAH4, could promote cytosolic and/or nuclear transfer of unique model nanoparticles—pseudovirions derived from murine polyomavirus.

Article Title: LAMP3 transfer via extracellular particles induces apoptosis in Sjögren’s disease
Article Snippet: Galectin-3 puncta formation indicates a loss of lysosomal membrane integrity as a marker of LMP, which may imply release of lysosomal digestive enzymes into the cell cytoplasm .

Article Title: FASN Inactivation-Induced Progranulin (GRN) Expression Promotes Lysosome-Dependent Cell Death to Suppress Leukemogenesis
Article Snippet: In our study, we observed that the marker of LMP, Galectin-3 puncta formation, was significantly increased in FASN-depleted cells ( ).

Article Title: FASN Inactivation-Induced Progranulin (GRN) Expression Promotes Lysosome-Dependent Cell Death to Suppress Leukemogenesis
Article Snippet: In support of this hypothesis, Galectin-3 puncta formation, a marker of LMP , was accumulated in FASN-depleted MOLM-13 cells ( and fig. S12C).

Article Title: Lysosome-Associated Membrane Protein 3 Induces Lysosome-Dependent Cell Death by Impairing Autophagic Caspase 8 Degradation in the Salivary Glands of Individuals With Sjögren's Disease.
Article Snippet: Objective.. Lysosome-associated membrane protein 3 (LAMP3) overexpression is implicated in the development and progression of Sjögren’s disease (SjD) by inducing lysosomal membrane permeabilization (LMP) and apoptotic cell death in salivary gland epithelium.. The aim of this study was to clarify the molecular details of LAMP3-induced lysosome-dependent cell death and to test lysosomal biogenesis as a therapeutic intervention.

Expressing:

Article Title: VirPorters: Insights into the action of cationic and histidine-rich cell-penetrating peptides.
Article Snippet: The utilization of nanoparticles for the intracellular delivery of theranostic agents faces one substantial limitation.. Sequestration in intracellular vesicles prevents them from reaching the desired location in the cytoplasm or nucleus to deliver their cargo.. We investigated whether three different cell-penetrating peptides (CPPs), namely, octa-arginine R8, polyhistidine KH27K and histidine-rich LAH4, could promote cytosolic and/or nuclear transfer of unique model nanoparticles—pseudovirions derived from murine polyomavirus.

Article Title: LAMP3 transfer via extracellular particles induces apoptosis in Sjögren’s disease
Article Snippet: Galectin-3 puncta formation indicates a loss of lysosomal membrane integrity as a marker of LMP, which may imply release of lysosomal digestive enzymes into the cell cytoplasm .

Article Title: FASN Inactivation-Induced Progranulin (GRN) Expression Promotes Lysosome-Dependent Cell Death to Suppress Leukemogenesis
Article Snippet: In our study, we observed that the marker of LMP, Galectin-3 puncta formation, was significantly increased in FASN-depleted cells ( ).

Article Title: FASN Inactivation-Induced Progranulin (GRN) Expression Promotes Lysosome-Dependent Cell Death to Suppress Leukemogenesis
Article Snippet: In support of this hypothesis, Galectin-3 puncta formation, a marker of LMP , was accumulated in FASN-depleted MOLM-13 cells ( and fig. S12C).

Article Title: Lysosome-Associated Membrane Protein 3 Induces Lysosome-Dependent Cell Death by Impairing Autophagic Caspase 8 Degradation in the Salivary Glands of Individuals With Sjögren's Disease.
Article Snippet: Objective.. Lysosome-associated membrane protein 3 (LAMP3) overexpression is implicated in the development and progression of Sjögren’s disease (SjD) by inducing lysosomal membrane permeabilization (LMP) and apoptotic cell death in salivary gland epithelium.. The aim of this study was to clarify the molecular details of LAMP3-induced lysosome-dependent cell death and to test lysosomal biogenesis as a therapeutic intervention.

Sequencing:

Article Title: VirPorters: Insights into the action of cationic and histidine-rich cell-penetrating peptides.
Article Snippet: The utilization of nanoparticles for the intracellular delivery of theranostic agents faces one substantial limitation.. Sequestration in intracellular vesicles prevents them from reaching the desired location in the cytoplasm or nucleus to deliver their cargo.. We investigated whether three different cell-penetrating peptides (CPPs), namely, octa-arginine R8, polyhistidine KH27K and histidine-rich LAH4, could promote cytosolic and/or nuclear transfer of unique model nanoparticles—pseudovirions derived from murine polyomavirus.

Article Title: LAMP3 transfer via extracellular particles induces apoptosis in Sjögren’s disease
Article Snippet: Galectin-3 puncta formation indicates a loss of lysosomal membrane integrity as a marker of LMP, which may imply release of lysosomal digestive enzymes into the cell cytoplasm .

Article Title: FASN Inactivation-Induced Progranulin (GRN) Expression Promotes Lysosome-Dependent Cell Death to Suppress Leukemogenesis
Article Snippet: In our study, we observed that the marker of LMP, Galectin-3 puncta formation, was significantly increased in FASN-depleted cells ( ).

Article Title: FASN Inactivation-Induced Progranulin (GRN) Expression Promotes Lysosome-Dependent Cell Death to Suppress Leukemogenesis
Article Snippet: In support of this hypothesis, Galectin-3 puncta formation, a marker of LMP , was accumulated in FASN-depleted MOLM-13 cells ( and fig. S12C).

Article Title: Lysosome-Associated Membrane Protein 3 Induces Lysosome-Dependent Cell Death by Impairing Autophagic Caspase 8 Degradation in the Salivary Glands of Individuals With Sjögren's Disease.
Article Snippet: Objective.. Lysosome-associated membrane protein 3 (LAMP3) overexpression is implicated in the development and progression of Sjögren’s disease (SjD) by inducing lysosomal membrane permeabilization (LMP) and apoptotic cell death in salivary gland epithelium.. The aim of this study was to clarify the molecular details of LAMP3-induced lysosome-dependent cell death and to test lysosomal biogenesis as a therapeutic intervention.

Mutagenesis:

Article Title: VirPorters: Insights into the action of cationic and histidine-rich cell-penetrating peptides.
Article Snippet: The utilization of nanoparticles for the intracellular delivery of theranostic agents faces one substantial limitation.. Sequestration in intracellular vesicles prevents them from reaching the desired location in the cytoplasm or nucleus to deliver their cargo.. We investigated whether three different cell-penetrating peptides (CPPs), namely, octa-arginine R8, polyhistidine KH27K and histidine-rich LAH4, could promote cytosolic and/or nuclear transfer of unique model nanoparticles—pseudovirions derived from murine polyomavirus.

Article Title: LAMP3 transfer via extracellular particles induces apoptosis in Sjögren’s disease
Article Snippet: Galectin-3 puncta formation indicates a loss of lysosomal membrane integrity as a marker of LMP, which may imply release of lysosomal digestive enzymes into the cell cytoplasm .

Article Title: FASN Inactivation-Induced Progranulin (GRN) Expression Promotes Lysosome-Dependent Cell Death to Suppress Leukemogenesis
Article Snippet: In our study, we observed that the marker of LMP, Galectin-3 puncta formation, was significantly increased in FASN-depleted cells ( ).

Article Title: FASN Inactivation-Induced Progranulin (GRN) Expression Promotes Lysosome-Dependent Cell Death to Suppress Leukemogenesis
Article Snippet: In support of this hypothesis, Galectin-3 puncta formation, a marker of LMP , was accumulated in FASN-depleted MOLM-13 cells ( and fig. S12C).

Article Title: Lysosome-Associated Membrane Protein 3 Induces Lysosome-Dependent Cell Death by Impairing Autophagic Caspase 8 Degradation in the Salivary Glands of Individuals With Sjögren's Disease.
Article Snippet: Objective.. Lysosome-associated membrane protein 3 (LAMP3) overexpression is implicated in the development and progression of Sjögren’s disease (SjD) by inducing lysosomal membrane permeabilization (LMP) and apoptotic cell death in salivary gland epithelium.. The aim of this study was to clarify the molecular details of LAMP3-induced lysosome-dependent cell death and to test lysosomal biogenesis as a therapeutic intervention.

Transfection:

Article Title: VirPorters: Insights into the action of cationic and histidine-rich cell-penetrating peptides.
Article Snippet: The utilization of nanoparticles for the intracellular delivery of theranostic agents faces one substantial limitation.. Sequestration in intracellular vesicles prevents them from reaching the desired location in the cytoplasm or nucleus to deliver their cargo.. We investigated whether three different cell-penetrating peptides (CPPs), namely, octa-arginine R8, polyhistidine KH27K and histidine-rich LAH4, could promote cytosolic and/or nuclear transfer of unique model nanoparticles—pseudovirions derived from murine polyomavirus.

Article Title: LAMP3 transfer via extracellular particles induces apoptosis in Sjögren’s disease
Article Snippet: Galectin-3 puncta formation indicates a loss of lysosomal membrane integrity as a marker of LMP, which may imply release of lysosomal digestive enzymes into the cell cytoplasm .

Article Title: FASN Inactivation-Induced Progranulin (GRN) Expression Promotes Lysosome-Dependent Cell Death to Suppress Leukemogenesis
Article Snippet: In our study, we observed that the marker of LMP, Galectin-3 puncta formation, was significantly increased in FASN-depleted cells ( ).

Article Title: FASN Inactivation-Induced Progranulin (GRN) Expression Promotes Lysosome-Dependent Cell Death to Suppress Leukemogenesis
Article Snippet: In support of this hypothesis, Galectin-3 puncta formation, a marker of LMP , was accumulated in FASN-depleted MOLM-13 cells ( and fig. S12C).

Article Title: Lysosome-Associated Membrane Protein 3 Induces Lysosome-Dependent Cell Death by Impairing Autophagic Caspase 8 Degradation in the Salivary Glands of Individuals With Sjögren's Disease.
Article Snippet: Objective.. Lysosome-associated membrane protein 3 (LAMP3) overexpression is implicated in the development and progression of Sjögren’s disease (SjD) by inducing lysosomal membrane permeabilization (LMP) and apoptotic cell death in salivary gland epithelium.. The aim of this study was to clarify the molecular details of LAMP3-induced lysosome-dependent cell death and to test lysosomal biogenesis as a therapeutic intervention.

Plasmid Preparation:

Article Title: VirPorters: Insights into the action of cationic and histidine-rich cell-penetrating peptides.
Article Snippet: The utilization of nanoparticles for the intracellular delivery of theranostic agents faces one substantial limitation.. Sequestration in intracellular vesicles prevents them from reaching the desired location in the cytoplasm or nucleus to deliver their cargo.. We investigated whether three different cell-penetrating peptides (CPPs), namely, octa-arginine R8, polyhistidine KH27K and histidine-rich LAH4, could promote cytosolic and/or nuclear transfer of unique model nanoparticles—pseudovirions derived from murine polyomavirus.

Article Title: LAMP3 transfer via extracellular particles induces apoptosis in Sjögren’s disease
Article Snippet: Galectin-3 puncta formation indicates a loss of lysosomal membrane integrity as a marker of LMP, which may imply release of lysosomal digestive enzymes into the cell cytoplasm .

Article Title: FASN Inactivation-Induced Progranulin (GRN) Expression Promotes Lysosome-Dependent Cell Death to Suppress Leukemogenesis
Article Snippet: In our study, we observed that the marker of LMP, Galectin-3 puncta formation, was significantly increased in FASN-depleted cells ( ).

Article Title: FASN Inactivation-Induced Progranulin (GRN) Expression Promotes Lysosome-Dependent Cell Death to Suppress Leukemogenesis
Article Snippet: In support of this hypothesis, Galectin-3 puncta formation, a marker of LMP , was accumulated in FASN-depleted MOLM-13 cells ( and fig. S12C).

Article Title: Lysosome-Associated Membrane Protein 3 Induces Lysosome-Dependent Cell Death by Impairing Autophagic Caspase 8 Degradation in the Salivary Glands of Individuals With Sjögren's Disease.
Article Snippet: Objective.. Lysosome-associated membrane protein 3 (LAMP3) overexpression is implicated in the development and progression of Sjögren’s disease (SjD) by inducing lysosomal membrane permeabilization (LMP) and apoptotic cell death in salivary gland epithelium.. The aim of this study was to clarify the molecular details of LAMP3-induced lysosome-dependent cell death and to test lysosomal biogenesis as a therapeutic intervention.

Infection:

Article Title: VirPorters: Insights into the action of cationic and histidine-rich cell-penetrating peptides.
Article Snippet: The utilization of nanoparticles for the intracellular delivery of theranostic agents faces one substantial limitation.. Sequestration in intracellular vesicles prevents them from reaching the desired location in the cytoplasm or nucleus to deliver their cargo.. We investigated whether three different cell-penetrating peptides (CPPs), namely, octa-arginine R8, polyhistidine KH27K and histidine-rich LAH4, could promote cytosolic and/or nuclear transfer of unique model nanoparticles—pseudovirions derived from murine polyomavirus.

Article Title: LAMP3 transfer via extracellular particles induces apoptosis in Sjögren’s disease
Article Snippet: Galectin-3 puncta formation indicates a loss of lysosomal membrane integrity as a marker of LMP, which may imply release of lysosomal digestive enzymes into the cell cytoplasm .

Article Title: FASN Inactivation-Induced Progranulin (GRN) Expression Promotes Lysosome-Dependent Cell Death to Suppress Leukemogenesis
Article Snippet: In our study, we observed that the marker of LMP, Galectin-3 puncta formation, was significantly increased in FASN-depleted cells ( ).

Article Title: FASN Inactivation-Induced Progranulin (GRN) Expression Promotes Lysosome-Dependent Cell Death to Suppress Leukemogenesis
Article Snippet: In support of this hypothesis, Galectin-3 puncta formation, a marker of LMP , was accumulated in FASN-depleted MOLM-13 cells ( and fig. S12C).

Article Title: Lysosome-Associated Membrane Protein 3 Induces Lysosome-Dependent Cell Death by Impairing Autophagic Caspase 8 Degradation in the Salivary Glands of Individuals With Sjögren's Disease.
Article Snippet: Objective.. Lysosome-associated membrane protein 3 (LAMP3) overexpression is implicated in the development and progression of Sjögren’s disease (SjD) by inducing lysosomal membrane permeabilization (LMP) and apoptotic cell death in salivary gland epithelium.. The aim of this study was to clarify the molecular details of LAMP3-induced lysosome-dependent cell death and to test lysosomal biogenesis as a therapeutic intervention.

Real-time Polymerase Chain Reaction:

Article Title: VirPorters: Insights into the action of cationic and histidine-rich cell-penetrating peptides.
Article Snippet: The utilization of nanoparticles for the intracellular delivery of theranostic agents faces one substantial limitation.. Sequestration in intracellular vesicles prevents them from reaching the desired location in the cytoplasm or nucleus to deliver their cargo.. We investigated whether three different cell-penetrating peptides (CPPs), namely, octa-arginine R8, polyhistidine KH27K and histidine-rich LAH4, could promote cytosolic and/or nuclear transfer of unique model nanoparticles—pseudovirions derived from murine polyomavirus.

Article Title: LAMP3 transfer via extracellular particles induces apoptosis in Sjögren’s disease
Article Snippet: Galectin-3 puncta formation indicates a loss of lysosomal membrane integrity as a marker of LMP, which may imply release of lysosomal digestive enzymes into the cell cytoplasm .

Article Title: FASN Inactivation-Induced Progranulin (GRN) Expression Promotes Lysosome-Dependent Cell Death to Suppress Leukemogenesis
Article Snippet: In our study, we observed that the marker of LMP, Galectin-3 puncta formation, was significantly increased in FASN-depleted cells ( ).

Article Title: FASN Inactivation-Induced Progranulin (GRN) Expression Promotes Lysosome-Dependent Cell Death to Suppress Leukemogenesis
Article Snippet: In support of this hypothesis, Galectin-3 puncta formation, a marker of LMP , was accumulated in FASN-depleted MOLM-13 cells ( and fig. S12C).

Article Title: Lysosome-Associated Membrane Protein 3 Induces Lysosome-Dependent Cell Death by Impairing Autophagic Caspase 8 Degradation in the Salivary Glands of Individuals With Sjögren's Disease.
Article Snippet: Objective.. Lysosome-associated membrane protein 3 (LAMP3) overexpression is implicated in the development and progression of Sjögren’s disease (SjD) by inducing lysosomal membrane permeabilization (LMP) and apoptotic cell death in salivary gland epithelium.. The aim of this study was to clarify the molecular details of LAMP3-induced lysosome-dependent cell death and to test lysosomal biogenesis as a therapeutic intervention.

Activation Assay:

Article Title: VirPorters: Insights into the action of cationic and histidine-rich cell-penetrating peptides.
Article Snippet: The utilization of nanoparticles for the intracellular delivery of theranostic agents faces one substantial limitation.. Sequestration in intracellular vesicles prevents them from reaching the desired location in the cytoplasm or nucleus to deliver their cargo.. We investigated whether three different cell-penetrating peptides (CPPs), namely, octa-arginine R8, polyhistidine KH27K and histidine-rich LAH4, could promote cytosolic and/or nuclear transfer of unique model nanoparticles—pseudovirions derived from murine polyomavirus.

Article Title: LAMP3 transfer via extracellular particles induces apoptosis in Sjögren’s disease
Article Snippet: Galectin-3 puncta formation indicates a loss of lysosomal membrane integrity as a marker of LMP, which may imply release of lysosomal digestive enzymes into the cell cytoplasm .

Article Title: FASN Inactivation-Induced Progranulin (GRN) Expression Promotes Lysosome-Dependent Cell Death to Suppress Leukemogenesis
Article Snippet: In our study, we observed that the marker of LMP, Galectin-3 puncta formation, was significantly increased in FASN-depleted cells ( ).

Article Title: FASN Inactivation-Induced Progranulin (GRN) Expression Promotes Lysosome-Dependent Cell Death to Suppress Leukemogenesis
Article Snippet: In support of this hypothesis, Galectin-3 puncta formation, a marker of LMP , was accumulated in FASN-depleted MOLM-13 cells ( and fig. S12C).

Article Title: Lysosome-Associated Membrane Protein 3 Induces Lysosome-Dependent Cell Death by Impairing Autophagic Caspase 8 Degradation in the Salivary Glands of Individuals With Sjögren's Disease.
Article Snippet: Objective.. Lysosome-associated membrane protein 3 (LAMP3) overexpression is implicated in the development and progression of Sjögren’s disease (SjD) by inducing lysosomal membrane permeabilization (LMP) and apoptotic cell death in salivary gland epithelium.. The aim of this study was to clarify the molecular details of LAMP3-induced lysosome-dependent cell death and to test lysosomal biogenesis as a therapeutic intervention.

Membrane:

Article Title: VirPorters: Insights into the action of cationic and histidine-rich cell-penetrating peptides.
Article Snippet: The utilization of nanoparticles for the intracellular delivery of theranostic agents faces one substantial limitation.. Sequestration in intracellular vesicles prevents them from reaching the desired location in the cytoplasm or nucleus to deliver their cargo.. We investigated whether three different cell-penetrating peptides (CPPs), namely, octa-arginine R8, polyhistidine KH27K and histidine-rich LAH4, could promote cytosolic and/or nuclear transfer of unique model nanoparticles—pseudovirions derived from murine polyomavirus.

Article Title: LAMP3 transfer via extracellular particles induces apoptosis in Sjögren’s disease
Article Snippet: Galectin-3 puncta formation indicates a loss of lysosomal membrane integrity as a marker of LMP, which may imply release of lysosomal digestive enzymes into the cell cytoplasm .

Article Title: FASN Inactivation-Induced Progranulin (GRN) Expression Promotes Lysosome-Dependent Cell Death to Suppress Leukemogenesis
Article Snippet: In our study, we observed that the marker of LMP, Galectin-3 puncta formation, was significantly increased in FASN-depleted cells ( ).

Article Title: FASN Inactivation-Induced Progranulin (GRN) Expression Promotes Lysosome-Dependent Cell Death to Suppress Leukemogenesis
Article Snippet: In support of this hypothesis, Galectin-3 puncta formation, a marker of LMP , was accumulated in FASN-depleted MOLM-13 cells ( and fig. S12C).

Article Title: Lysosome-Associated Membrane Protein 3 Induces Lysosome-Dependent Cell Death by Impairing Autophagic Caspase 8 Degradation in the Salivary Glands of Individuals With Sjögren's Disease.
Article Snippet: Objective.. Lysosome-associated membrane protein 3 (LAMP3) overexpression is implicated in the development and progression of Sjögren’s disease (SjD) by inducing lysosomal membrane permeabilization (LMP) and apoptotic cell death in salivary gland epithelium.. The aim of this study was to clarify the molecular details of LAMP3-induced lysosome-dependent cell death and to test lysosomal biogenesis as a therapeutic intervention.

Cell Culture:

Article Title: VirPorters: Insights into the action of cationic and histidine-rich cell-penetrating peptides.
Article Snippet: The utilization of nanoparticles for the intracellular delivery of theranostic agents faces one substantial limitation.. Sequestration in intracellular vesicles prevents them from reaching the desired location in the cytoplasm or nucleus to deliver their cargo.. We investigated whether three different cell-penetrating peptides (CPPs), namely, octa-arginine R8, polyhistidine KH27K and histidine-rich LAH4, could promote cytosolic and/or nuclear transfer of unique model nanoparticles—pseudovirions derived from murine polyomavirus.

Article Title: LAMP3 transfer via extracellular particles induces apoptosis in Sjögren’s disease
Article Snippet: Galectin-3 puncta formation indicates a loss of lysosomal membrane integrity as a marker of LMP, which may imply release of lysosomal digestive enzymes into the cell cytoplasm .

Article Title: FASN Inactivation-Induced Progranulin (GRN) Expression Promotes Lysosome-Dependent Cell Death to Suppress Leukemogenesis
Article Snippet: In our study, we observed that the marker of LMP, Galectin-3 puncta formation, was significantly increased in FASN-depleted cells ( ).

Article Title: FASN Inactivation-Induced Progranulin (GRN) Expression Promotes Lysosome-Dependent Cell Death to Suppress Leukemogenesis
Article Snippet: In support of this hypothesis, Galectin-3 puncta formation, a marker of LMP , was accumulated in FASN-depleted MOLM-13 cells ( and fig. S12C).

Article Title: Lysosome-Associated Membrane Protein 3 Induces Lysosome-Dependent Cell Death by Impairing Autophagic Caspase 8 Degradation in the Salivary Glands of Individuals With Sjögren's Disease.
Article Snippet: Objective.. Lysosome-associated membrane protein 3 (LAMP3) overexpression is implicated in the development and progression of Sjögren’s disease (SjD) by inducing lysosomal membrane permeabilization (LMP) and apoptotic cell death in salivary gland epithelium.. The aim of this study was to clarify the molecular details of LAMP3-induced lysosome-dependent cell death and to test lysosomal biogenesis as a therapeutic intervention.

Immunofluorescence:

Article Title: VirPorters: Insights into the action of cationic and histidine-rich cell-penetrating peptides.
Article Snippet: The utilization of nanoparticles for the intracellular delivery of theranostic agents faces one substantial limitation.. Sequestration in intracellular vesicles prevents them from reaching the desired location in the cytoplasm or nucleus to deliver their cargo.. We investigated whether three different cell-penetrating peptides (CPPs), namely, octa-arginine R8, polyhistidine KH27K and histidine-rich LAH4, could promote cytosolic and/or nuclear transfer of unique model nanoparticles—pseudovirions derived from murine polyomavirus.

Article Title: LAMP3 transfer via extracellular particles induces apoptosis in Sjögren’s disease
Article Snippet: Galectin-3 puncta formation indicates a loss of lysosomal membrane integrity as a marker of LMP, which may imply release of lysosomal digestive enzymes into the cell cytoplasm .

Article Title: FASN Inactivation-Induced Progranulin (GRN) Expression Promotes Lysosome-Dependent Cell Death to Suppress Leukemogenesis
Article Snippet: In our study, we observed that the marker of LMP, Galectin-3 puncta formation, was significantly increased in FASN-depleted cells ( ).

Article Title: FASN Inactivation-Induced Progranulin (GRN) Expression Promotes Lysosome-Dependent Cell Death to Suppress Leukemogenesis
Article Snippet: In support of this hypothesis, Galectin-3 puncta formation, a marker of LMP , was accumulated in FASN-depleted MOLM-13 cells ( and fig. S12C).

Article Title: Lysosome-Associated Membrane Protein 3 Induces Lysosome-Dependent Cell Death by Impairing Autophagic Caspase 8 Degradation in the Salivary Glands of Individuals With Sjögren's Disease.
Article Snippet: Objective.. Lysosome-associated membrane protein 3 (LAMP3) overexpression is implicated in the development and progression of Sjögren’s disease (SjD) by inducing lysosomal membrane permeabilization (LMP) and apoptotic cell death in salivary gland epithelium.. The aim of this study was to clarify the molecular details of LAMP3-induced lysosome-dependent cell death and to test lysosomal biogenesis as a therapeutic intervention.

Disruption:

Article Title: VirPorters: Insights into the action of cationic and histidine-rich cell-penetrating peptides.
Article Snippet: The utilization of nanoparticles for the intracellular delivery of theranostic agents faces one substantial limitation.. Sequestration in intracellular vesicles prevents them from reaching the desired location in the cytoplasm or nucleus to deliver their cargo.. We investigated whether three different cell-penetrating peptides (CPPs), namely, octa-arginine R8, polyhistidine KH27K and histidine-rich LAH4, could promote cytosolic and/or nuclear transfer of unique model nanoparticles—pseudovirions derived from murine polyomavirus.

Article Title: LAMP3 transfer via extracellular particles induces apoptosis in Sjögren’s disease
Article Snippet: Galectin-3 puncta formation indicates a loss of lysosomal membrane integrity as a marker of LMP, which may imply release of lysosomal digestive enzymes into the cell cytoplasm .

Article Title: FASN Inactivation-Induced Progranulin (GRN) Expression Promotes Lysosome-Dependent Cell Death to Suppress Leukemogenesis
Article Snippet: In our study, we observed that the marker of LMP, Galectin-3 puncta formation, was significantly increased in FASN-depleted cells ( ).

Article Title: FASN Inactivation-Induced Progranulin (GRN) Expression Promotes Lysosome-Dependent Cell Death to Suppress Leukemogenesis
Article Snippet: In support of this hypothesis, Galectin-3 puncta formation, a marker of LMP , was accumulated in FASN-depleted MOLM-13 cells ( and fig. S12C).

Article Title: Lysosome-Associated Membrane Protein 3 Induces Lysosome-Dependent Cell Death by Impairing Autophagic Caspase 8 Degradation in the Salivary Glands of Individuals With Sjögren's Disease.
Article Snippet: Objective.. Lysosome-associated membrane protein 3 (LAMP3) overexpression is implicated in the development and progression of Sjögren’s disease (SjD) by inducing lysosomal membrane permeabilization (LMP) and apoptotic cell death in salivary gland epithelium.. The aim of this study was to clarify the molecular details of LAMP3-induced lysosome-dependent cell death and to test lysosomal biogenesis as a therapeutic intervention.



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( A ) Representative immunofluorescent images for V-ATPase (green) <t>and</t> <t>galectin-3</t> (red) staining on labial minor salivary gland sections from SjD patients ( n = 10) or control non-SjD sicca subjects ( n = 5). Original magnification: 40x (inset: 100x). ( B ) Bar chart showing mean (± SD) percentage of galctin-3 puncta-positive cells. ** P < 0.01, t -test.
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Image Search Results


( A ) Representative immunofluorescent images for V-ATPase (green) and galectin-3 (red) staining on labial minor salivary gland sections from SjD patients ( n = 10) or control non-SjD sicca subjects ( n = 5). Original magnification: 40x (inset: 100x). ( B ) Bar chart showing mean (± SD) percentage of galctin-3 puncta-positive cells. ** P < 0.01, t -test.

Journal: Arthritis & rheumatology (Hoboken, N.J.)

Article Title: LAMP3 induces lysosome-dependent cell death by impairing autophagic caspase-8 degradation in Sjögren’s salivary glands

doi: 10.1002/art.42540

Figure Lengend Snippet: ( A ) Representative immunofluorescent images for V-ATPase (green) and galectin-3 (red) staining on labial minor salivary gland sections from SjD patients ( n = 10) or control non-SjD sicca subjects ( n = 5). Original magnification: 40x (inset: 100x). ( B ) Bar chart showing mean (± SD) percentage of galctin-3 puncta-positive cells. ** P < 0.01, t -test.

Article Snippet: Results: Galectin-3 puncta formation was more frequent in SjD patients’ salivary glands compared to control glands.

Techniques: Staining, Control

( A , B ) Labial minor salivary gland sections from SjD patients ( n = 80) were stained for ( A ) V-ATPase (green) and galectin-3 (red) (original magnification: 40x) or for ( B ) LAMP3 (green) (original magnification: 20x). Representative immunofluorescent image in each LMP and LAMP3 expression grade are shown. ( C ) Matrix shows the number of patients having indicated combination of LMP and LAMP3 expression grades. ( D ) Bar charts show the number of patients having indicated LMP grade based on positivity of serum anti-SSA/Ro antibodies or salivary gland histology. FLS, focal lymphocytic sialadenitis; NSCS, non-specific chronic sialadenitis; SCS, sclerosing chronic sialadenitis; F/S, combination of FLS and SCS features.

Journal: Arthritis & rheumatology (Hoboken, N.J.)

Article Title: LAMP3 induces lysosome-dependent cell death by impairing autophagic caspase-8 degradation in Sjögren’s salivary glands

doi: 10.1002/art.42540

Figure Lengend Snippet: ( A , B ) Labial minor salivary gland sections from SjD patients ( n = 80) were stained for ( A ) V-ATPase (green) and galectin-3 (red) (original magnification: 40x) or for ( B ) LAMP3 (green) (original magnification: 20x). Representative immunofluorescent image in each LMP and LAMP3 expression grade are shown. ( C ) Matrix shows the number of patients having indicated combination of LMP and LAMP3 expression grades. ( D ) Bar charts show the number of patients having indicated LMP grade based on positivity of serum anti-SSA/Ro antibodies or salivary gland histology. FLS, focal lymphocytic sialadenitis; NSCS, non-specific chronic sialadenitis; SCS, sclerosing chronic sialadenitis; F/S, combination of FLS and SCS features.

Article Snippet: Results: Galectin-3 puncta formation was more frequent in SjD patients’ salivary glands compared to control glands.

Techniques: Expressing, Staining

( A ) Western blots showing caspase-8 and α-tubulin (internal control) expressions in control and LAMP3-overexpressing A253 cells. ( B , C ) A253 cells were transfected with CASP8 -GFP and/or empty-GFP expression plasmids. ( B ) Flow cytometry using APC-annexin V and 7-AAD 48 hours after transfection, and bar chart showing the difference in the rate of annexin V-positive cells from that in control ( n = 5). ( C ) Immunofluorescent images for GFP (green) or galectin-3 (magenta) staining, and bar chart showing percentage of galectin-3 puncta-positive cells ( n = 5). ( D-F ) LAMP3-overexpressing A253 cells were treated with negative control or two types of CASP8 siRNA for 72 hours. ( D ) Western blots showing caspase-8 and α-tubulin expressions. ( E ) Flow cytometry using APC-annexin V and 7-AAD, and bar chart showing the difference in the rate of annexin V-positive cells from that in control A253 cells ( n = 3). ( F ) Immunofluorescent images for galectin-3 (magenta) staining, and bar chart showing percentage of galectin-3 puncta-positive cells ( n = 3). Original magnification: 40x. Values shown are mean ± SD. * p < 0.05, ** p < 0.01, t -test with Dunnett’s correction.

Journal: Arthritis & rheumatology (Hoboken, N.J.)

Article Title: LAMP3 induces lysosome-dependent cell death by impairing autophagic caspase-8 degradation in Sjögren’s salivary glands

doi: 10.1002/art.42540

Figure Lengend Snippet: ( A ) Western blots showing caspase-8 and α-tubulin (internal control) expressions in control and LAMP3-overexpressing A253 cells. ( B , C ) A253 cells were transfected with CASP8 -GFP and/or empty-GFP expression plasmids. ( B ) Flow cytometry using APC-annexin V and 7-AAD 48 hours after transfection, and bar chart showing the difference in the rate of annexin V-positive cells from that in control ( n = 5). ( C ) Immunofluorescent images for GFP (green) or galectin-3 (magenta) staining, and bar chart showing percentage of galectin-3 puncta-positive cells ( n = 5). ( D-F ) LAMP3-overexpressing A253 cells were treated with negative control or two types of CASP8 siRNA for 72 hours. ( D ) Western blots showing caspase-8 and α-tubulin expressions. ( E ) Flow cytometry using APC-annexin V and 7-AAD, and bar chart showing the difference in the rate of annexin V-positive cells from that in control A253 cells ( n = 3). ( F ) Immunofluorescent images for galectin-3 (magenta) staining, and bar chart showing percentage of galectin-3 puncta-positive cells ( n = 3). Original magnification: 40x. Values shown are mean ± SD. * p < 0.05, ** p < 0.01, t -test with Dunnett’s correction.

Article Snippet: Results: Galectin-3 puncta formation was more frequent in SjD patients’ salivary glands compared to control glands.

Techniques: Expressing, Western Blot, Control, Transfection, Flow Cytometry, Staining, Negative Control

Control or LAMP3-overexpressing A253 cells were treated with liraglutide, an inducer of lysosomal biogenesis, at indicated concentration or vehicle control for 18 hours. ( A ) Flow cytometry using Lysotracker Deep Red (Black line: without Lysotracker; Red line: with Lysotracker) and bar chart showing mean fluorescent intensity. ( B ) Western blots showing caspase-8 and α-tubulin (internal control) expressions and bar chart showing relative change of caspase-8 expression normalized by α-tubulin expression. ( C , D ) Control or LAMP3-overexpressing A253 cells were treated with liraglutide at 60 nM or vehicle control for 18 hours. ( C ) Immunofluorescent images for galectin-3 (magenta) staining and bar chart showing percentage of galectin-3 puncta-positive cells. Original magnification: 40x. ( D ) Flow cytometry using APC-annexin V and 7-AAD and bar chart showing the difference in the rate of annexin V-positive cells from that in control cells. Values shown are mean ± SD ( n = 4 for all experiments). * p < 0.05, ** p < 0.01, t -test with Dunnett’s correction.

Journal: Arthritis & rheumatology (Hoboken, N.J.)

Article Title: LAMP3 induces lysosome-dependent cell death by impairing autophagic caspase-8 degradation in Sjögren’s salivary glands

doi: 10.1002/art.42540

Figure Lengend Snippet: Control or LAMP3-overexpressing A253 cells were treated with liraglutide, an inducer of lysosomal biogenesis, at indicated concentration or vehicle control for 18 hours. ( A ) Flow cytometry using Lysotracker Deep Red (Black line: without Lysotracker; Red line: with Lysotracker) and bar chart showing mean fluorescent intensity. ( B ) Western blots showing caspase-8 and α-tubulin (internal control) expressions and bar chart showing relative change of caspase-8 expression normalized by α-tubulin expression. ( C , D ) Control or LAMP3-overexpressing A253 cells were treated with liraglutide at 60 nM or vehicle control for 18 hours. ( C ) Immunofluorescent images for galectin-3 (magenta) staining and bar chart showing percentage of galectin-3 puncta-positive cells. Original magnification: 40x. ( D ) Flow cytometry using APC-annexin V and 7-AAD and bar chart showing the difference in the rate of annexin V-positive cells from that in control cells. Values shown are mean ± SD ( n = 4 for all experiments). * p < 0.05, ** p < 0.01, t -test with Dunnett’s correction.

Article Snippet: Results: Galectin-3 puncta formation was more frequent in SjD patients’ salivary glands compared to control glands.

Techniques: Expressing, In Vitro, Control, Concentration Assay, Flow Cytometry, Western Blot, Staining

LAMP3-overexpressing mice received weekly subcutaneous injections of dulaglutide, an inducer of lysosomal biogenesis, at 0.6 mg/kg or placebo for 3 months after developing an SjD-like phenotype. ( A ) Immunofluorescent images of murine submandibular glands for galectin-3 (magenta) staining and bar chart showing the percentage of galectin-3 puncta-positive cells. ( B ) Immunofluorescent images of submandibular glands with terminal deoxynucleotidyl transferase dUTP nick end labelling (TUNEL, red) and bar chart showing the percentage of TUNEL-positive apoptotic cells. ( C ) Hematoxylin and eosin staining of glands and the percentage of lymphocytic infiltration area in whole glands. ( D ) Pilocarpine-stimulated salivary flow per body weight in 20 minutes before and after treatment. ( E ) Serum anti-Ro/SS-A antibody levels. Original magnification: 40x (inset: 100x) for ( A ) and ( B ), and 4x for ( C ). Values shown are median and quartile ( n = 9, each group). * p < 0.05, ** p < 0.01, Wilcoxon test.

Journal: Arthritis & rheumatology (Hoboken, N.J.)

Article Title: LAMP3 induces lysosome-dependent cell death by impairing autophagic caspase-8 degradation in Sjögren’s salivary glands

doi: 10.1002/art.42540

Figure Lengend Snippet: LAMP3-overexpressing mice received weekly subcutaneous injections of dulaglutide, an inducer of lysosomal biogenesis, at 0.6 mg/kg or placebo for 3 months after developing an SjD-like phenotype. ( A ) Immunofluorescent images of murine submandibular glands for galectin-3 (magenta) staining and bar chart showing the percentage of galectin-3 puncta-positive cells. ( B ) Immunofluorescent images of submandibular glands with terminal deoxynucleotidyl transferase dUTP nick end labelling (TUNEL, red) and bar chart showing the percentage of TUNEL-positive apoptotic cells. ( C ) Hematoxylin and eosin staining of glands and the percentage of lymphocytic infiltration area in whole glands. ( D ) Pilocarpine-stimulated salivary flow per body weight in 20 minutes before and after treatment. ( E ) Serum anti-Ro/SS-A antibody levels. Original magnification: 40x (inset: 100x) for ( A ) and ( B ), and 4x for ( C ). Values shown are median and quartile ( n = 9, each group). * p < 0.05, ** p < 0.01, Wilcoxon test.

Article Snippet: Results: Galectin-3 puncta formation was more frequent in SjD patients’ salivary glands compared to control glands.

Techniques: Staining, TUNEL Assay