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Sino Biological human rage protein
Human Rage Protein, supplied by Sino Biological, used in various techniques. Bioz Stars score: 93/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/human+rage+protein/Human+AGER+%2F+RAGE+Protein/pm41226481-415-2-8
Average 93 stars, based on 4 article reviews

human rage protein - by Bioz Stars, 2026-09

93/100 stars

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Article Title: A branched arabinoglucan from Angelica sinensis ameliorates diabetic renal damage in rats.
Article Snippet: Shaanxi Key Laboratory of Natural Products and Chemical Biology, School of Chemistry and Pharmacy, Northwest A&F University, Yangling 712100, China Department of Natural Medicine and Institute of Materia Medica, School of Pharmacy, Fourth Military Medical University, Xi'an 710032, China Department of Pharmacology, School of Pharmacy, Fourth Military Medical University, Xi'an 710032, China Key Laboratory of Gastrointestinal Pharmacology of Chinese Materia Medica of the State Administration of Traditional Chinese Medicine, Fourth Military Medical University, Xi'an 710032, China Correspondence Wei Cao, Shaanxi Key Laboratory of Natural Products and Chemical Biology, School of Chemistry and Pharmacy, Northwest A&F University, Yangling 712100, China.. Email: caowei@nwafu.edu.cn; caowei@fmmu. edu.cn Funding information National Natural Science Foundation of China, Grant/Award Number: 81473329; Science and Technology Innovation Project of Shaanxi Province, Grant/Award Number: 2016SF‐284; Special Foundation for Talents in Science and Technology of Northwest A&F University, Grant/Award Number: Z111021601

Article Title: A Novel, Multi-Target Natural Drug Candidate, Matrine, Improves Cognitive Deficits in Alzheimer's Disease Transgenic Mice by Inhibiting Aβ Aggregation and Blocking the RAGE/Aβ Axis.
Article Snippet: The treatment of AD is a topic that has puzzled researchers for many years.. Current mainstream theories still consider Aβ to be themost important target for the cure of AD.. In this study, we attempted to explore multiple targets for AD treatments with the aim of identifying a qualified compound that could both inhibit the aggregation of Aβ and block the RAGE/Aβ axis.We believed that a compound that targets both Aβ and RAGEmay be a feasible strategy for AD treatment.

Labeling:

Article Title: Geniposide ameliorates diabetic nephropathy in type 2 diabetic mice by targeting AGEs-RAGE-dependent inflammatory pathway.
Article Snippet: Background: Diabetic nephropathy (DN) is a prevalent complication of diabetes mellitus and the primary cause of morbidity and mortality in end-stage renal disease.. The receptor for advanced glycation end products (RAGE) plays a crucial role in mediating AGE-triggered inflammation, which has been implicated in DN pathogenesis.. While geniposide, a natural compound, has demonstrated anti-inflammatory and hypoglycemic properties, its potential to mitigate AGE-induced renal inflammation and consequently impede DN progression remains

Recombinant:

Article Title: Dendritic Polyglycerol Sulfate Reduces Inflammation Through Inhibition of the HMGB1/RAGE Axis in RAW 264.7 Macrophages.
Article Snippet: .. The recombinant Human RAGE Protein (His-Tag, cat.# 11629-H08H, Sino Biological, Eschborn, Germany) was reconstituted by adding 500 μL Milli-Q water to the vial. .. Subsequently, it was concentrated to 50 μL using Amicon® Ultra centrifugal filter units (3 kDa molecular weight cutoff, total volume 500 μL, Merck Millipore, Darmstadt, Germany).

Article Title: Dendritic Polyglycerol Sulfate Reduces Inflammation Through Inhibition of the HMGB1/RAGE Axis in RAW 264.7 Macrophages
Article Snippet: .. The recombinant Human RAGE Protein (His-Tag, cat.# 11629-H08H, Sino Biological, Eschborn, Germany) was reconstituted by adding 500 μL Milli-Q water to the vial. .. Subsequently, it was concentrated to 50 μL using Amicon ® Ultra centrifugal filter units (3 kDa molecular weight cutoff, total volume 500 μL, Merck Millipore, Darmstadt, Germany).

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HMGB1 induces SARS-CoV-2 infection in an ACE2-independent RAGE-dependent manner (A) Western blot analysis of receptors responsible for SARS-CoV-2 infection and HMGB1 binding. S.E., short exposure; L.E., long exposure. (B) Flow cytometry analysis of ectodomain ACE2 in A549 and NCI-H1975 cells used in this study. Vero E6 cells were used as control. (C) A549 cells were transfected with shRNA-ACE2 for 48 h prior to infection with 1 MOI SARS-CoV-2, which was preincubated with HMGB1 for 1 h at 37°C, cultured further for 3 h, and subjected to western blotting. (D and E) A549 cells were infected for 1 h with 1 MOI SARS-CoV-2, which was preincubated with HMGB1 for 1 h, in the presence of 40 μg/mL sRAGE at 37°C as indicated. Cells were harvested at 3 hpi and subjected to western blotting (D) n = 3, and qRT-PCR for viral RNA measurement (E) n = 3. (F) NCI-H1975 cells were infected with SARS-CoV-2 preincubated with 20 μg/mL HMGB1 in the presence of azeliragon. Cells were harvested at 3 hpi and subjected to western blotting. (G) A549 cells were infected with 5 MOI SARS-CoV-2, which was treated as above to observe NP. Representative confocal images are shown. The percentage of infected cells and NP intensity were measured by counting at least 700 visible cells. n = 4. (H) Cycloheximide pretreated NCI-H1975 cells were infected with 5 MOI SARS-CoV-2 (preincubated with HMGB1). Cells were stained for NP before permeabilization (green; external) and post-permeabilization (red; external and internal). Representative images and their magnifications are shown. The percentage of intracellular spots was measured by counting at least 200 visible cells. n = 4. (I and J) SARS2pp was preincubated with or without HMGB1 in the presence of sRAGE before transduction in NCI-H1975 cells. NanoLuc luciferase activity was measured 72 h post-transduction. n = 3 Scale bars represent 5 μm. Data are presented as mean ± SEM, ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001, ∗∗∗∗ p < 0.0001; ns, not significant, using one-way ANOVA with Tukey’s multiple comparison test and Student’s unpaired t-test. HMGB1, high-mobility group box 1; SARS-CoV-2, severe acute respiratory syndrome coronavirus 2; MOI, multiplicity of infection; qRT-PCR, quantitative reverse transcription polymerase chain reaction; NP, nucleocapsid protein; SEM, standard error of the mean; ANOVA, analysis of variance; hpi, hours post-infection; RAGE, receptor for advanced glycation end-products; ACE2, angiotensin-converting enzyme 2; SARS2pp, SARS-CoV-2 spike protein (S)-pseudotyped retrovirus.

Journal: iScience

Article Title: Direct interaction of HMGB1 with SARS-CoV-2 facilitates its infection via RAGE-dependent endocytosis

doi: 10.1016/j.isci.2025.113063

Figure Lengend Snippet: HMGB1 induces SARS-CoV-2 infection in an ACE2-independent RAGE-dependent manner (A) Western blot analysis of receptors responsible for SARS-CoV-2 infection and HMGB1 binding. S.E., short exposure; L.E., long exposure. (B) Flow cytometry analysis of ectodomain ACE2 in A549 and NCI-H1975 cells used in this study. Vero E6 cells were used as control. (C) A549 cells were transfected with shRNA-ACE2 for 48 h prior to infection with 1 MOI SARS-CoV-2, which was preincubated with HMGB1 for 1 h at 37°C, cultured further for 3 h, and subjected to western blotting. (D and E) A549 cells were infected for 1 h with 1 MOI SARS-CoV-2, which was preincubated with HMGB1 for 1 h, in the presence of 40 μg/mL sRAGE at 37°C as indicated. Cells were harvested at 3 hpi and subjected to western blotting (D) n = 3, and qRT-PCR for viral RNA measurement (E) n = 3. (F) NCI-H1975 cells were infected with SARS-CoV-2 preincubated with 20 μg/mL HMGB1 in the presence of azeliragon. Cells were harvested at 3 hpi and subjected to western blotting. (G) A549 cells were infected with 5 MOI SARS-CoV-2, which was treated as above to observe NP. Representative confocal images are shown. The percentage of infected cells and NP intensity were measured by counting at least 700 visible cells. n = 4. (H) Cycloheximide pretreated NCI-H1975 cells were infected with 5 MOI SARS-CoV-2 (preincubated with HMGB1). Cells were stained for NP before permeabilization (green; external) and post-permeabilization (red; external and internal). Representative images and their magnifications are shown. The percentage of intracellular spots was measured by counting at least 200 visible cells. n = 4. (I and J) SARS2pp was preincubated with or without HMGB1 in the presence of sRAGE before transduction in NCI-H1975 cells. NanoLuc luciferase activity was measured 72 h post-transduction. n = 3 Scale bars represent 5 μm. Data are presented as mean ± SEM, ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001, ∗∗∗∗ p < 0.0001; ns, not significant, using one-way ANOVA with Tukey’s multiple comparison test and Student’s unpaired t-test. HMGB1, high-mobility group box 1; SARS-CoV-2, severe acute respiratory syndrome coronavirus 2; MOI, multiplicity of infection; qRT-PCR, quantitative reverse transcription polymerase chain reaction; NP, nucleocapsid protein; SEM, standard error of the mean; ANOVA, analysis of variance; hpi, hours post-infection; RAGE, receptor for advanced glycation end-products; ACE2, angiotensin-converting enzyme 2; SARS2pp, SARS-CoV-2 spike protein (S)-pseudotyped retrovirus.

Article Snippet: 40 μg/mL sRAGE (11629-HCCH, Sino Biological, Oklahoma City, OK, USA), azeliragon (S6415, Selleckchem, Houston, TX, USA), dynasore (D7693, Sigma-Aldrich, St. Louis, MO, USA) and chloroquine (C6628, Sigma-Aldrich) were pretreated for 2 h at 37°C, prior to the infection procedure.

Techniques: Infection, Western Blot, Binding Assay, Flow Cytometry, Control, Transfection, shRNA, Cell Culture, Quantitative RT-PCR, Staining, Transduction, Luciferase, Activity Assay, Comparison, Reverse Transcription, Polymerase Chain Reaction

Fig. 2. SC79 induces the shedding of the RAGE ectodomain. HAECs were incubated with 10 µM SC79 for various times (5, 10, 30, and 60 min) (n = 4) (A) or different concentrations of SC79 (0.1, 1, 5, and 10 µM) for 30 min (n = 3) (B). The cell lysate and culture supernatant were immunoblotted with a monoclonal antibody to the extracellular domain of human RAGE and an anti-actin antibody. To compare the size of RAGE in cell lysate and culture supernatant, untreated cell lysate (a) and conditioned media from cells treated with 10 µM SC79 for 30 min (b) were run on the same gel and immunoblotted with the RAGE antibody (C). The cell lysates of HAECs treated with different concentrations of SC79 (0.1, 1, 5, and 10 µM) for 30 min were immunoblotted with an antibody to the C-terminal domain of human RAGE and an anti-actin antibody (n = 4) (D). (*p < 0.05 vs. control)

Journal: Scientific reports

Article Title: AKT activation triggers Rab14-mediated ADAM10 translocation to the cell surface in human aortic endothelial cells.

doi: 10.1038/s41598-025-90624-w

Figure Lengend Snippet: Fig. 2. SC79 induces the shedding of the RAGE ectodomain. HAECs were incubated with 10 µM SC79 for various times (5, 10, 30, and 60 min) (n = 4) (A) or different concentrations of SC79 (0.1, 1, 5, and 10 µM) for 30 min (n = 3) (B). The cell lysate and culture supernatant were immunoblotted with a monoclonal antibody to the extracellular domain of human RAGE and an anti-actin antibody. To compare the size of RAGE in cell lysate and culture supernatant, untreated cell lysate (a) and conditioned media from cells treated with 10 µM SC79 for 30 min (b) were run on the same gel and immunoblotted with the RAGE antibody (C). The cell lysates of HAECs treated with different concentrations of SC79 (0.1, 1, 5, and 10 µM) for 30 min were immunoblotted with an antibody to the C-terminal domain of human RAGE and an anti-actin antibody (n = 4) (D). (*p < 0.05 vs. control)

Article Snippet: Anti-RAGE (JF0975) rabbit monoclonal antibody against amino acids 350–390 corresponding to the C-terminal region of human RAGE was from R&D Systems, Inc. (Minneapolis, MN, USA).

Techniques: Incubation, Control

Fig. 3. Inhibitors of AKT and ADAM10 diminish SC79-induced RAGE ectodomain shedding. HAECs were preincubated with or without MK-2206 (1 µM), GI 254023X (2 µM), or DMSO (vehicle) for 60 min. Following this, they were further incubated for 30 min with or without SC79 (10 µM). The cell lysate and culture supernatant were immunoblotted with a monoclonal antibody to the extracellular domain of human RAGE and an anti-actin antibody. (n = 3, *p < 0.05 vs. control, #p < 0.05 vs. SC79 treatment alone)

Journal: Scientific reports

Article Title: AKT activation triggers Rab14-mediated ADAM10 translocation to the cell surface in human aortic endothelial cells.

doi: 10.1038/s41598-025-90624-w

Figure Lengend Snippet: Fig. 3. Inhibitors of AKT and ADAM10 diminish SC79-induced RAGE ectodomain shedding. HAECs were preincubated with or without MK-2206 (1 µM), GI 254023X (2 µM), or DMSO (vehicle) for 60 min. Following this, they were further incubated for 30 min with or without SC79 (10 µM). The cell lysate and culture supernatant were immunoblotted with a monoclonal antibody to the extracellular domain of human RAGE and an anti-actin antibody. (n = 3, *p < 0.05 vs. control, #p < 0.05 vs. SC79 treatment alone)

Techniques: Incubation, Control

Fig. 4. AKT1 activation is required for SC79-induced RAGE ectodomain shedding. (A) HAECs express all three AKT isoforms, and AKT1-, AKT2-, and AKT3-siRNAs selectively deplete each AKT isoform. HAECs were transfected with AKT1-, AKT2-, AKT3-siRNAs, or control siRNAs, and the cell lysates were immunoblotted with antibodies to AKT1, AKT2, AKT3, or actin. (n = 3, *p < 0.05 vs. control). (B) SC79 activates AKT1. HAECs were incubated with 10 µM SC79 for various times (1, 5, 10, and 30 min) (upper panel) or different concentrations of SC79 (0.1, 1, 5, and 10 µM) for 30 min (lower panel). The cell lysates were immunoblotted with antibodies to p-AKT1 (Ser473) and AKT1. (n = 3, *p < 0.05 vs. control). (C) AKT1 knockdown inhibits SC79-induced RAGE ectodomain shedding. HAECs were transfected with AKT1-siRNA or control siRNA and then incubated for 30 min with or without SC79 (10 µM). The cell lysate and culture supernatant were immunoblotted with a monoclonal antibody to the extracellular domain of human RAGE and antibodies to AKT1 and actin. (n = 3, *p < 0.05 vs. control cells transfected with control siRNA). (D) AKT1 knockdown abolishes SC79’s inhibitory effect against AGE-BSA. HAECs transfected with AKT1-siRNA or control siRNA were treated for 30 min with or without SC79 (10 µM). The cells were then treated with AGE- BSA (100 µg/ml) for 24 h. The cell lysates were immunoblotted with antibodies to ICAM-1, AKT1, and actin. (n = 3, *p < 0.05 vs. control; #p < 0.05 vs. AGE-BSA; †p < 0.05 vs. control cells transfected with AKT1-siRNA)

Journal: Scientific reports

Article Title: AKT activation triggers Rab14-mediated ADAM10 translocation to the cell surface in human aortic endothelial cells.

doi: 10.1038/s41598-025-90624-w

Figure Lengend Snippet: Fig. 4. AKT1 activation is required for SC79-induced RAGE ectodomain shedding. (A) HAECs express all three AKT isoforms, and AKT1-, AKT2-, and AKT3-siRNAs selectively deplete each AKT isoform. HAECs were transfected with AKT1-, AKT2-, AKT3-siRNAs, or control siRNAs, and the cell lysates were immunoblotted with antibodies to AKT1, AKT2, AKT3, or actin. (n = 3, *p < 0.05 vs. control). (B) SC79 activates AKT1. HAECs were incubated with 10 µM SC79 for various times (1, 5, 10, and 30 min) (upper panel) or different concentrations of SC79 (0.1, 1, 5, and 10 µM) for 30 min (lower panel). The cell lysates were immunoblotted with antibodies to p-AKT1 (Ser473) and AKT1. (n = 3, *p < 0.05 vs. control). (C) AKT1 knockdown inhibits SC79-induced RAGE ectodomain shedding. HAECs were transfected with AKT1-siRNA or control siRNA and then incubated for 30 min with or without SC79 (10 µM). The cell lysate and culture supernatant were immunoblotted with a monoclonal antibody to the extracellular domain of human RAGE and antibodies to AKT1 and actin. (n = 3, *p < 0.05 vs. control cells transfected with control siRNA). (D) AKT1 knockdown abolishes SC79’s inhibitory effect against AGE-BSA. HAECs transfected with AKT1-siRNA or control siRNA were treated for 30 min with or without SC79 (10 µM). The cells were then treated with AGE- BSA (100 µg/ml) for 24 h. The cell lysates were immunoblotted with antibodies to ICAM-1, AKT1, and actin. (n = 3, *p < 0.05 vs. control; #p < 0.05 vs. AGE-BSA; †p < 0.05 vs. control cells transfected with AKT1-siRNA)

Techniques: Activation Assay, Transfection, Control, Incubation, Knockdown

Fig. 5. AKT2 activation is required for SC79-induced RAGE ectodomain shedding. (A) SC79 activates AKT2. HAECs were incubated with 10 µM SC79 for various times (1, 5, 10, and 30 min) (upper panel) or different concentrations of SC79 (0.1, 1, 5, and 10 µM) for 30 min (lower panel). The cell lysates were immunoblotted with antibodies to p-AKT2 (Ser474) and AKT2. (n = 4, *p < 0.05 vs. control). (B) AKT2 knockdown inhibits SC79-induced RAGE ectodomain shedding. HAECs were transfected with AKT2-siRNA or control siRNA and then incubated for 30 min with or without SC79 (10 µM). The cell lysate and culture supernatant were immunoblotted with a monoclonal antibody to the extracellular domain of human RAGE and antibodies to AKT2 and actin. (n = 4, *p < 0.05 vs. control cells transfected with control siRNA). (C) AKT2 knockdown abolishes SC79’s inhibitory effect against AGE-BSA. HAECs transfected with AKT2-siRNA or control siRNA were treated for 30 min with or without SC79 (10 µM). The cells were then treated with AGE-BSA (100 µg/ml) for 24 h. The cell lysates were immunoblotted with antibodies to ICAM-1, AKT2, and actin. (n = 3, *p < 0.05 vs. control; #p < 0.05 vs. AGE-BSA; †p < 0.05 vs. control cells transfected with AKT2-siRNA)

Journal: Scientific reports

Article Title: AKT activation triggers Rab14-mediated ADAM10 translocation to the cell surface in human aortic endothelial cells.

doi: 10.1038/s41598-025-90624-w

Figure Lengend Snippet: Fig. 5. AKT2 activation is required for SC79-induced RAGE ectodomain shedding. (A) SC79 activates AKT2. HAECs were incubated with 10 µM SC79 for various times (1, 5, 10, and 30 min) (upper panel) or different concentrations of SC79 (0.1, 1, 5, and 10 µM) for 30 min (lower panel). The cell lysates were immunoblotted with antibodies to p-AKT2 (Ser474) and AKT2. (n = 4, *p < 0.05 vs. control). (B) AKT2 knockdown inhibits SC79-induced RAGE ectodomain shedding. HAECs were transfected with AKT2-siRNA or control siRNA and then incubated for 30 min with or without SC79 (10 µM). The cell lysate and culture supernatant were immunoblotted with a monoclonal antibody to the extracellular domain of human RAGE and antibodies to AKT2 and actin. (n = 4, *p < 0.05 vs. control cells transfected with control siRNA). (C) AKT2 knockdown abolishes SC79’s inhibitory effect against AGE-BSA. HAECs transfected with AKT2-siRNA or control siRNA were treated for 30 min with or without SC79 (10 µM). The cells were then treated with AGE-BSA (100 µg/ml) for 24 h. The cell lysates were immunoblotted with antibodies to ICAM-1, AKT2, and actin. (n = 3, *p < 0.05 vs. control; #p < 0.05 vs. AGE-BSA; †p < 0.05 vs. control cells transfected with AKT2-siRNA)

Techniques: Activation Assay, Incubation, Control, Knockdown, Transfection

Fig. 6. AKT3 activation is required for SC79-induced RAGE ectodomain shedding. (A) SC79 activates AKT3. HAECs were incubated with 10 µM SC79 for various times (1, 5, 10, and 30 min) (upper panel) or different concentrations of SC79 (0.1, 1, 5, and 10 µM) for 30 min (lower panel). The cell lysates were immunoblotted with antibodies to p-AKT3 (Ser472) and AKT3. (n = 3, *p < 0.05 vs. control). (B) AKT3 knockdown inhibits SC79-induced RAGE ectodomain shedding. HAECs were transfected with AKT3-siRNA or control siRNA and then incubated for 30 min with or without SC79 (10 µM). The cell lysate and culture supernatant were immunoblotted with a monoclonal antibody to the extracellular domain of human RAGE and antibodies to AKT3 and actin. (n = 3, *p < 0.05 vs. control cells transfected with control siRNA). (C) AKT3 knockdown abolishes SC79’s inhibitory effect against AGE-BSA. HAECs transfected with AKT3-siRNA or control siRNA were treated for 30 min with or without SC79 (10 µM). The cells were then treated with AGE-BSA (100 µg/ml) for 24 h. The cell lysates were immunoblotted with antibodies to ICAM-1, AKT3, and actin. (n = 3, *p < 0.05 vs. control; #p < 0.05 vs. AGE-BSA; †p < 0.05 vs. control cells transfected with AKT3-siRNA)

Journal: Scientific reports

Article Title: AKT activation triggers Rab14-mediated ADAM10 translocation to the cell surface in human aortic endothelial cells.

doi: 10.1038/s41598-025-90624-w

Figure Lengend Snippet: Fig. 6. AKT3 activation is required for SC79-induced RAGE ectodomain shedding. (A) SC79 activates AKT3. HAECs were incubated with 10 µM SC79 for various times (1, 5, 10, and 30 min) (upper panel) or different concentrations of SC79 (0.1, 1, 5, and 10 µM) for 30 min (lower panel). The cell lysates were immunoblotted with antibodies to p-AKT3 (Ser472) and AKT3. (n = 3, *p < 0.05 vs. control). (B) AKT3 knockdown inhibits SC79-induced RAGE ectodomain shedding. HAECs were transfected with AKT3-siRNA or control siRNA and then incubated for 30 min with or without SC79 (10 µM). The cell lysate and culture supernatant were immunoblotted with a monoclonal antibody to the extracellular domain of human RAGE and antibodies to AKT3 and actin. (n = 3, *p < 0.05 vs. control cells transfected with control siRNA). (C) AKT3 knockdown abolishes SC79’s inhibitory effect against AGE-BSA. HAECs transfected with AKT3-siRNA or control siRNA were treated for 30 min with or without SC79 (10 µM). The cells were then treated with AGE-BSA (100 µg/ml) for 24 h. The cell lysates were immunoblotted with antibodies to ICAM-1, AKT3, and actin. (n = 3, *p < 0.05 vs. control; #p < 0.05 vs. AGE-BSA; †p < 0.05 vs. control cells transfected with AKT3-siRNA)

Techniques: Activation Assay, Incubation, Control, Knockdown, Transfection

Fig. 7. SC79 induces RAGE ectodomain shedding by promoting ADAM10 cell surface translocation. (A) Immunofluorescence staining to evaluate the effect of SC79 on ADAM10 localization. HAECs grown in culture dishes with a coverslip were treated with SC79 (10 µM) for 10–120 min. (a) The cells on the coverslip were fixed for 10 min with 4% paraformaldehyde without permeabilization, then immunostained with an antibody to an extracellular portion of ADAM10 and examined using confocal microscopy. DAPI was used to label the nuclei of the cells. Representative photos and the relative fluorescence intensities are shown (scale bar: 100 μm). (b) Cell lysates from cells that were not on the coverslip in the same culture plate were immunoblotted with antibodies to ADAM10 and actin. (n = 3, *p < 0.05 vs. control). (B) ADAM10 knockdown inhibits SC79-induced RAGE ectodomain shedding. HAECs were transfected with ADAM10-siRNA or control siRNA and then incubated for 30 min with or without SC79 (10 µM). The cell lysate and culture supernatant were immunoblotted with a monoclonal antibody to the extracellular domain of human RAGE and antibodies to ADAM10 and actin. (n = 3, *p < 0.05 vs. control cells transfected with control siRNA). (C) ADAM10 knockdown abolishes SC79’s inhibitory effect against AGE-BSA. HAECs transfected with ADAM10-siRNA or control siRNA were treated for 30 min with or without SC79 (10 µM). The cells were then treated with AGE- BSA (100 µg/ml) for 24 h. The cell lysates were immunoblotted with antibodies to ICAM-1, ADAM10, and actin. (n = 3, *p < 0.05 vs. control; #p < 0.05 vs. AGE-BSA; †p < 0.05 vs. control cells transfected with ADAM10- siRNA)

Journal: Scientific reports

Article Title: AKT activation triggers Rab14-mediated ADAM10 translocation to the cell surface in human aortic endothelial cells.

doi: 10.1038/s41598-025-90624-w

Figure Lengend Snippet: Fig. 7. SC79 induces RAGE ectodomain shedding by promoting ADAM10 cell surface translocation. (A) Immunofluorescence staining to evaluate the effect of SC79 on ADAM10 localization. HAECs grown in culture dishes with a coverslip were treated with SC79 (10 µM) for 10–120 min. (a) The cells on the coverslip were fixed for 10 min with 4% paraformaldehyde without permeabilization, then immunostained with an antibody to an extracellular portion of ADAM10 and examined using confocal microscopy. DAPI was used to label the nuclei of the cells. Representative photos and the relative fluorescence intensities are shown (scale bar: 100 μm). (b) Cell lysates from cells that were not on the coverslip in the same culture plate were immunoblotted with antibodies to ADAM10 and actin. (n = 3, *p < 0.05 vs. control). (B) ADAM10 knockdown inhibits SC79-induced RAGE ectodomain shedding. HAECs were transfected with ADAM10-siRNA or control siRNA and then incubated for 30 min with or without SC79 (10 µM). The cell lysate and culture supernatant were immunoblotted with a monoclonal antibody to the extracellular domain of human RAGE and antibodies to ADAM10 and actin. (n = 3, *p < 0.05 vs. control cells transfected with control siRNA). (C) ADAM10 knockdown abolishes SC79’s inhibitory effect against AGE-BSA. HAECs transfected with ADAM10-siRNA or control siRNA were treated for 30 min with or without SC79 (10 µM). The cells were then treated with AGE- BSA (100 µg/ml) for 24 h. The cell lysates were immunoblotted with antibodies to ICAM-1, ADAM10, and actin. (n = 3, *p < 0.05 vs. control; #p < 0.05 vs. AGE-BSA; †p < 0.05 vs. control cells transfected with ADAM10- siRNA)

Techniques: Translocation Assay, Immunofluorescence, Staining, Confocal Microscopy, Fluorescence, Control, Knockdown, Transfection, Incubation

Fig. 10. Rab14 is required for SC79-induced ADAM10 cell surface translocation. (A) Rab14 knockdown prevents SC79-induced ADAM10 cell surface translocation. HAECs grown in culture dishes with a coverslip were transfected with Rab14-siRNA or control siRNA and then incubated for 20 min with DMSO or SC79 (10 µM). (a) Cells grown on the coverslip were immunostained with an antibody to an extracellular portion of ADAM10. Representative photos and the relative fluorescence intensities are shown (scale bar: 100 μm). (b) Cell lysates from cells that were not on the coverslip in the same culture plate were immunoblotted with antibodies to Rab14 and actin. (n = 3, *p < 0.05 vs. control cells transfected with control siRNA). (B) Rab14 knockdown inhibits SC79-induced RAGE ectodomain shedding. HAECs were transfected with Rab14-siRNA or control siRNA and then incubated for 30 min with or without SC79 (10 µM). The cell lysate and culture supernatant were immunoblotted with a monoclonal antibody to the extracellular domain of human RAGE and antibodies to Rab14 and actin. (n = 3, *p < 0.05 vs. control cells transfected with control siRNA). (C) Rab14 knockdown abolishes SC79’s inhibitory effect against AGE-BSA. HAECs transfected with Rab14-siRNA or control siRNA were treated for 30 min with or without SC79 (10 µM). The cells were then treated with AGE- BSA (100 µg/ml) for 24 h. The cell lysates were immunoblotted with antibodies to ICAM-1, Rab14, and actin. (n = 4, *p < 0.05 vs. control; #p < 0.05 vs. AGE-BSA; †p < 0.05 vs. control cells transfected with Rab14-siRNA)

Journal: Scientific reports

Article Title: AKT activation triggers Rab14-mediated ADAM10 translocation to the cell surface in human aortic endothelial cells.

doi: 10.1038/s41598-025-90624-w

Figure Lengend Snippet: Fig. 10. Rab14 is required for SC79-induced ADAM10 cell surface translocation. (A) Rab14 knockdown prevents SC79-induced ADAM10 cell surface translocation. HAECs grown in culture dishes with a coverslip were transfected with Rab14-siRNA or control siRNA and then incubated for 20 min with DMSO or SC79 (10 µM). (a) Cells grown on the coverslip were immunostained with an antibody to an extracellular portion of ADAM10. Representative photos and the relative fluorescence intensities are shown (scale bar: 100 μm). (b) Cell lysates from cells that were not on the coverslip in the same culture plate were immunoblotted with antibodies to Rab14 and actin. (n = 3, *p < 0.05 vs. control cells transfected with control siRNA). (B) Rab14 knockdown inhibits SC79-induced RAGE ectodomain shedding. HAECs were transfected with Rab14-siRNA or control siRNA and then incubated for 30 min with or without SC79 (10 µM). The cell lysate and culture supernatant were immunoblotted with a monoclonal antibody to the extracellular domain of human RAGE and antibodies to Rab14 and actin. (n = 3, *p < 0.05 vs. control cells transfected with control siRNA). (C) Rab14 knockdown abolishes SC79’s inhibitory effect against AGE-BSA. HAECs transfected with Rab14-siRNA or control siRNA were treated for 30 min with or without SC79 (10 µM). The cells were then treated with AGE- BSA (100 µg/ml) for 24 h. The cell lysates were immunoblotted with antibodies to ICAM-1, Rab14, and actin. (n = 4, *p < 0.05 vs. control; #p < 0.05 vs. AGE-BSA; †p < 0.05 vs. control cells transfected with Rab14-siRNA)

Techniques: Translocation Assay, Knockdown, Transfection, Control, Incubation, Fluorescence

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