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Bioss adam10 bioss bs 3574r wb
Adam10 Bioss Bs 3574r Wb, supplied by Bioss, used in various techniques. Bioz Stars score: 92/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 92 stars, based on 7 article reviews

adam10 bioss bs 3574r wb - by Bioz Stars, 2026-05

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Protein levels of ADAM10 species and mRNA in AD brain samples. Non-dementia controls (NDC, n = 13) and AD extracts ( n = 16) from prefrontal cortex were resolved by SDS-PAGE/electrophoresis prior to western blot assay. Each individual ADAM10 immunoreactive band was quantified, and levels normalized using GAPDH. A Representative western blot of ADAM10 using the rabbit anti- C-terminal region monoclonal antibody (ab124695, Abcam) and GAPDH with monoclonal antibody (60004-1-Ig, Proteintech) ( B ) Densitometric quantification of ADAM10 immunoreactive bands assigned to immature (iADAM10) and C mature (mADAM10) species normalized with respect to GAPDH. D Ratio mADAM10/iADAM10 that represents the amount of mature species vs. immature. E Relative mRNA levels of ADAM10 in NDC vs. AD patients’ samples were analyzed by qRT-PCR. Transcript levels were calculated by the comparative 2 − ΔCt method with respect to GAPDH. The graphs represent mean ± SEM. Significant P < 0.05 values assayed by t-test are indicated

Journal: Alzheimer's Research & Therapy

Article Title: Selective reduction of ADAM10 in brain and cerebrospinal fluid of Alzheimer’s disease patients

doi: 10.1186/s13195-026-02007-6

Figure Lengend Snippet: Protein levels of ADAM10 species and mRNA in AD brain samples. Non-dementia controls (NDC, n = 13) and AD extracts ( n = 16) from prefrontal cortex were resolved by SDS-PAGE/electrophoresis prior to western blot assay. Each individual ADAM10 immunoreactive band was quantified, and levels normalized using GAPDH. A Representative western blot of ADAM10 using the rabbit anti- C-terminal region monoclonal antibody (ab124695, Abcam) and GAPDH with monoclonal antibody (60004-1-Ig, Proteintech) ( B ) Densitometric quantification of ADAM10 immunoreactive bands assigned to immature (iADAM10) and C mature (mADAM10) species normalized with respect to GAPDH. D Ratio mADAM10/iADAM10 that represents the amount of mature species vs. immature. E Relative mRNA levels of ADAM10 in NDC vs. AD patients’ samples were analyzed by qRT-PCR. Transcript levels were calculated by the comparative 2 − ΔCt method with respect to GAPDH. The graphs represent mean ± SEM. Significant P < 0.05 values assayed by t-test are indicated

Article Snippet: Representative blots of CSF samples of non-AD control individuals with large age amplitude (the age of the subjects are shown on top) probed with ( A ) anti-ADAM10 polyclonal antibody to ectodomain region (OAGA02442, Aviva) and ( B ) ADAM17 antibody towards the ectodomain region (AF9301, R&D Systems).

Techniques: SDS Page, Electrophoresis, Western Blot, Quantitative RT-PCR

Aβ affects ADAM10 levels, but not ADAM17, in SH-SY5Y-differentiated neurons. SH-SY5Y cell cultures were differentiated to neurons with 10 µM retinoic acid treatment and then treated with 3 µM of Aβ42 for 48 h. A Representative western blot of control ( C ) and Aβ-treated (Aβ42) cell samples that was resolved with the anti C-terminal ADAM10 antibody (ab124695, Abcam). B Densitometric quantification of immunoreactive bands of iADAM10 and C mADAM10 with respect to GAPDH. Values represent the percentage with respect to control. D Values of the ratio between mature vs. immature species of ADAM10 (mADAM10/iADAM10). E Representative western blot of ADAM17 species resolved with anti-ectodomain region ADAM17 antibody (AF9301, R&D Systems) and the respective quantifications of F iADAM17 and G mADAM17 immunoreactive bands normalized to the ubiquitous protein GAPDH. H Result of the ratio of mADAM17/iADAM17. The graphs represent mean ± SEM of n = 12 samples of 3 independent experiments. Significant P < 0.05 values assayed by t-test are indicated

Journal: Alzheimer's Research & Therapy

Article Title: Selective reduction of ADAM10 in brain and cerebrospinal fluid of Alzheimer’s disease patients

doi: 10.1186/s13195-026-02007-6

Figure Lengend Snippet: Aβ affects ADAM10 levels, but not ADAM17, in SH-SY5Y-differentiated neurons. SH-SY5Y cell cultures were differentiated to neurons with 10 µM retinoic acid treatment and then treated with 3 µM of Aβ42 for 48 h. A Representative western blot of control ( C ) and Aβ-treated (Aβ42) cell samples that was resolved with the anti C-terminal ADAM10 antibody (ab124695, Abcam). B Densitometric quantification of immunoreactive bands of iADAM10 and C mADAM10 with respect to GAPDH. Values represent the percentage with respect to control. D Values of the ratio between mature vs. immature species of ADAM10 (mADAM10/iADAM10). E Representative western blot of ADAM17 species resolved with anti-ectodomain region ADAM17 antibody (AF9301, R&D Systems) and the respective quantifications of F iADAM17 and G mADAM17 immunoreactive bands normalized to the ubiquitous protein GAPDH. H Result of the ratio of mADAM17/iADAM17. The graphs represent mean ± SEM of n = 12 samples of 3 independent experiments. Significant P < 0.05 values assayed by t-test are indicated

Techniques: Western Blot, Control

ADAM10 and ADAM17 CSF levels are not altered with aging. Representative blots of CSF samples of non-AD control individuals with large age amplitude (the age of the subjects are shown on top) probed with ( A ) anti-ADAM10 polyclonal antibody to ectodomain region (OAGA02442, Aviva) and ( B ) ADAM17 antibody towards the ectodomain region (AF9301, R&D Systems). Correlations between the age and the levels of ADAM10 and ADAM17 species ( C ) iADAM10, ( D ) mADAM10, ( E ) sADAM10, ( F ) iADAM17, ( G ) mADAM17 and ( H ) sADAM17 were assayed. All graphs include their Spearman coefficient (r) and the P value. None of the ADAM10 species nor ADAM17 correlate with age. * Refers to unspecific bands

Journal: Alzheimer's Research & Therapy

Article Title: Selective reduction of ADAM10 in brain and cerebrospinal fluid of Alzheimer’s disease patients

doi: 10.1186/s13195-026-02007-6

Figure Lengend Snippet: ADAM10 and ADAM17 CSF levels are not altered with aging. Representative blots of CSF samples of non-AD control individuals with large age amplitude (the age of the subjects are shown on top) probed with ( A ) anti-ADAM10 polyclonal antibody to ectodomain region (OAGA02442, Aviva) and ( B ) ADAM17 antibody towards the ectodomain region (AF9301, R&D Systems). Correlations between the age and the levels of ADAM10 and ADAM17 species ( C ) iADAM10, ( D ) mADAM10, ( E ) sADAM10, ( F ) iADAM17, ( G ) mADAM17 and ( H ) sADAM17 were assayed. All graphs include their Spearman coefficient (r) and the P value. None of the ADAM10 species nor ADAM17 correlate with age. * Refers to unspecific bands

Techniques: Control

Levels of ADAM10 and ADAM17 species in AD CSF samples. Analysis of CSF ADAM10 and ADAM17 in non-AD controls (NADC) and in AD patients. A Representative blot of CSF probed against anti-ADAM10 ectodomain antibody. Quantification of immunoreactive band values obtained from B iADAM10, C mADAM10 and D sADAM10. E Values of the ratio between mature vs immature species of ADAM10 (mADAM10/iADAM10). F Representative blot of CSF probed against ADAM17 and the quantifications of the immunoreactivity of the bands for G iADAM17, H mADAM17 and I sADAM17. J Result of the ratio mADAM10/iADAM10. The graphs represent mean ± SEM. Significant P < 0.05 values assayed by t-test are indicated. * Refers to unspecific bands

Journal: Alzheimer's Research & Therapy

Article Title: Selective reduction of ADAM10 in brain and cerebrospinal fluid of Alzheimer’s disease patients

doi: 10.1186/s13195-026-02007-6

Figure Lengend Snippet: Levels of ADAM10 and ADAM17 species in AD CSF samples. Analysis of CSF ADAM10 and ADAM17 in non-AD controls (NADC) and in AD patients. A Representative blot of CSF probed against anti-ADAM10 ectodomain antibody. Quantification of immunoreactive band values obtained from B iADAM10, C mADAM10 and D sADAM10. E Values of the ratio between mature vs immature species of ADAM10 (mADAM10/iADAM10). F Representative blot of CSF probed against ADAM17 and the quantifications of the immunoreactivity of the bands for G iADAM17, H mADAM17 and I sADAM17. J Result of the ratio mADAM10/iADAM10. The graphs represent mean ± SEM. Significant P < 0.05 values assayed by t-test are indicated. * Refers to unspecific bands

Techniques:

Journal: Cell Communication and Signaling : CCS

Article Title: Regulation of ADAM10 activity through microdomain-dependent intracellular calcium changes

doi: 10.1186/s12964-024-01891-5

Figure Lengend Snippet: Antibodies and reagents

Article Snippet: Polyclonal ADAM10 C-terminal Antibody , Invitrogen by Thermo Fisher Scientific (Frankfurt, Germany) , 1 μg/ml.

Techniques: Concentration Assay, Affinity Purification, Control

Journal: Cell Communication and Signaling : CCS

Article Title: Regulation of ADAM10 activity through microdomain-dependent intracellular calcium changes

doi: 10.1186/s12964-024-01891-5

Figure Lengend Snippet: Buffer and solutions

Article Snippet: Polyclonal ADAM10 C-terminal Antibody , Invitrogen by Thermo Fisher Scientific (Frankfurt, Germany) , 1 μg/ml.

Techniques: Lysis, Protease Inhibitor, ALP Assay, Activity Assay, Saline

Calcium- and ADAM10-dependent cleavage of E-cadherin. A - C : Confluent A549 monolayers were starved overnight and stimulated with 10 µM ionomycin, 1 µM thapsigargin, or 100 µM trifluoperazine (TFP) in the absence or presence of 10 µM GI254023X (GI), an ADAM10 inhibitor for 1 h. DMSO (0.1%) served as a vehicle control. Lysates were collected and subjected to E-cadherin cleavage analyses in A and B ( n = 4). In C, cells were transfected with AP-BTC prior to seeding, and the cleavage of alkaline phosphatase (AP)-conjugated betacellulin (BTC) was analyzed via an alkaline phosphatase (AP) assay ( n = 3). The quantitative data are shown as the means + SDs. Asterisks without lines represent differences compared with the control, and those with lines represent differences between groups (* p < 0.05, ** p < 0.01, *** p < 0.001 and **** p < 0.0001)

Journal: Cell Communication and Signaling : CCS

Article Title: Regulation of ADAM10 activity through microdomain-dependent intracellular calcium changes

doi: 10.1186/s12964-024-01891-5

Figure Lengend Snippet: Calcium- and ADAM10-dependent cleavage of E-cadherin. A - C : Confluent A549 monolayers were starved overnight and stimulated with 10 µM ionomycin, 1 µM thapsigargin, or 100 µM trifluoperazine (TFP) in the absence or presence of 10 µM GI254023X (GI), an ADAM10 inhibitor for 1 h. DMSO (0.1%) served as a vehicle control. Lysates were collected and subjected to E-cadherin cleavage analyses in A and B ( n = 4). In C, cells were transfected with AP-BTC prior to seeding, and the cleavage of alkaline phosphatase (AP)-conjugated betacellulin (BTC) was analyzed via an alkaline phosphatase (AP) assay ( n = 3). The quantitative data are shown as the means + SDs. Asterisks without lines represent differences compared with the control, and those with lines represent differences between groups (* p < 0.05, ** p < 0.01, *** p < 0.001 and **** p < 0.0001)

Article Snippet: Polyclonal ADAM10 C-terminal Antibody , Invitrogen by Thermo Fisher Scientific (Frankfurt, Germany) , 1 μg/ml.

Techniques: Control, Transfection

Time-dependence of Ca 2+ -induced ADAM10 activation. A - D : Confluent A549 monolayers were starved overnight and stimulated with 10 µM ionomycin or 100 µM TFP in the presence or absence of 10 µM GI for different durations (1’=1 min). DMSO (0.1%) served as a vehicle control. Lysates were collected and subjected to E-cadherin cleavage analyses in A and C ( n = 3). In B and D, cells were transfected with AP-BTC prior to seeding, and AP-BTC cleavage was analyzed via the AP assay ( n = 3). E, F: A549 cells were grown to 70% confluence on poly-L-lysine coated cover slips, and subjected to calcium imaging. Ionomycin (10 µM), 1 µM thapsigargin and 100 µM trifluoperazine, were automatically injected after 1.5 min of baseline measurement in the presence or absence (Ca 2+ sequestration with EGTA) of Ca 2+ in Ringer’s solution, followed by further recording for 20 min. DMSO (0.1%) served as a baseline measurement and vehicle control. The number of experiments across the number of cells N/n is indicated in the figures. The quantitative data are shown as the means + SDs. Asterisks without lines represent differences compared with the control, and those with lines represent differences between groups (* p < 0.05, ** p < 0.01, *** p < 0.001 and **** p < 0.0001)

Journal: Cell Communication and Signaling : CCS

Article Title: Regulation of ADAM10 activity through microdomain-dependent intracellular calcium changes

doi: 10.1186/s12964-024-01891-5

Figure Lengend Snippet: Time-dependence of Ca 2+ -induced ADAM10 activation. A - D : Confluent A549 monolayers were starved overnight and stimulated with 10 µM ionomycin or 100 µM TFP in the presence or absence of 10 µM GI for different durations (1’=1 min). DMSO (0.1%) served as a vehicle control. Lysates were collected and subjected to E-cadherin cleavage analyses in A and C ( n = 3). In B and D, cells were transfected with AP-BTC prior to seeding, and AP-BTC cleavage was analyzed via the AP assay ( n = 3). E, F: A549 cells were grown to 70% confluence on poly-L-lysine coated cover slips, and subjected to calcium imaging. Ionomycin (10 µM), 1 µM thapsigargin and 100 µM trifluoperazine, were automatically injected after 1.5 min of baseline measurement in the presence or absence (Ca 2+ sequestration with EGTA) of Ca 2+ in Ringer’s solution, followed by further recording for 20 min. DMSO (0.1%) served as a baseline measurement and vehicle control. The number of experiments across the number of cells N/n is indicated in the figures. The quantitative data are shown as the means + SDs. Asterisks without lines represent differences compared with the control, and those with lines represent differences between groups (* p < 0.05, ** p < 0.01, *** p < 0.001 and **** p < 0.0001)

Article Snippet: Polyclonal ADAM10 C-terminal Antibody , Invitrogen by Thermo Fisher Scientific (Frankfurt, Germany) , 1 μg/ml.

Techniques: Activation Assay, Control, Transfection, Imaging, Injection

Threshold-dependence of Ca 2+ -induced ADAM10 activation. A - F : Confluent A549 monolayers were starved overnight and stimulated with different concentrations of ionomycin in the presence or absence of 10 µM GI for 30 min ( A , B ) or at different time points ( C - F ). DMSO (0.1%) served as a vehicle control. Lysates were collected and subjected to E-cadherin cleavage analysis in A, C, and E ( n = 3). In B, D, and F, the cells were transfected with AP-BTC prior to seeding, and AP-BTC cleavage was analyzed via the AP assay ( n = 3). Asterisks without lines represent differences compared with the control, and those with lines represent differences between groups (* p < 0.05, ** p < 0.01, *** p < 0.001 and **** p < 0.0001)

Journal: Cell Communication and Signaling : CCS

Article Title: Regulation of ADAM10 activity through microdomain-dependent intracellular calcium changes

doi: 10.1186/s12964-024-01891-5

Figure Lengend Snippet: Threshold-dependence of Ca 2+ -induced ADAM10 activation. A - F : Confluent A549 monolayers were starved overnight and stimulated with different concentrations of ionomycin in the presence or absence of 10 µM GI for 30 min ( A , B ) or at different time points ( C - F ). DMSO (0.1%) served as a vehicle control. Lysates were collected and subjected to E-cadherin cleavage analysis in A, C, and E ( n = 3). In B, D, and F, the cells were transfected with AP-BTC prior to seeding, and AP-BTC cleavage was analyzed via the AP assay ( n = 3). Asterisks without lines represent differences compared with the control, and those with lines represent differences between groups (* p < 0.05, ** p < 0.01, *** p < 0.001 and **** p < 0.0001)

Article Snippet: Polyclonal ADAM10 C-terminal Antibody , Invitrogen by Thermo Fisher Scientific (Frankfurt, Germany) , 1 μg/ml.

Techniques: Activation Assay, Control, Transfection

Dependence of ADAM10-mediated E-cadherin cleavage on the origin of the increase in calcium concentration. A - F : Confluent A549 monolayers were starved overnight and stimulated with 10 µM Ion or 100 µM TFP in the presence or absence of 10 µM GI for 1 h. DMSO (0.1%) served as a vehicle control. Experiments were performed in the presence (2 mM CaCl 2 ) or nominal absence of calcium ( A , C , F , G ), with extracellular Ca 2+ chelation by 3 mM EGTA (noncell permeable, added 30 min before stimulation) ( B , E , H ) or intracellular Ca 2+ depletion with 10 µM BAPTA-AM (cell loading 30 min prior to stimulation) ( C , F ). Lysates were collected and subjected to E-cadherin cleavage analyses in A to F ( n = 3). ( n = 4). In G and H, cells were transfected with AP-BTC prior to seeding, and AP-BTC cleavage was analyzed via the AP assay ( n = 3). The quantitative data are shown as the means + SDs. Asterisks without lines represent differences compared with the control, and those with lines represent differences between groups (* p < 0.05, ** p < 0.01, *** p < 0.001 and **** p < 0.0001)

Journal: Cell Communication and Signaling : CCS

Article Title: Regulation of ADAM10 activity through microdomain-dependent intracellular calcium changes

doi: 10.1186/s12964-024-01891-5

Figure Lengend Snippet: Dependence of ADAM10-mediated E-cadherin cleavage on the origin of the increase in calcium concentration. A - F : Confluent A549 monolayers were starved overnight and stimulated with 10 µM Ion or 100 µM TFP in the presence or absence of 10 µM GI for 1 h. DMSO (0.1%) served as a vehicle control. Experiments were performed in the presence (2 mM CaCl 2 ) or nominal absence of calcium ( A , C , F , G ), with extracellular Ca 2+ chelation by 3 mM EGTA (noncell permeable, added 30 min before stimulation) ( B , E , H ) or intracellular Ca 2+ depletion with 10 µM BAPTA-AM (cell loading 30 min prior to stimulation) ( C , F ). Lysates were collected and subjected to E-cadherin cleavage analyses in A to F ( n = 3). ( n = 4). In G and H, cells were transfected with AP-BTC prior to seeding, and AP-BTC cleavage was analyzed via the AP assay ( n = 3). The quantitative data are shown as the means + SDs. Asterisks without lines represent differences compared with the control, and those with lines represent differences between groups (* p < 0.05, ** p < 0.01, *** p < 0.001 and **** p < 0.0001)

Article Snippet: Polyclonal ADAM10 C-terminal Antibody , Invitrogen by Thermo Fisher Scientific (Frankfurt, Germany) , 1 μg/ml.

Techniques: Concentration Assay, Control, Transfection

Regulation of cell-associated and soluble ADAM10 activity by Ca 2+ transients. A , B : Confluent A549 monolayers were starved overnight and stimulated with 10 µM ionomycin or 100 µM TFP in the presence or absence of 10 µM GI for 1, 10, 30 and 60 min. Lysates were collected and subjected to E-cadherin cleavage analyses. The ratio of mature to pro-form was quantified as measure of maturation by densitometry ( n = 3). C , D : Confluent A549 cell monolayers were starved overnight and stimulated with 10 µM ionomycin, 1 µM thapsigargin or 100 µM TFP for 1 min–1 h. Subsequently, the cells were subjected to surface staining for ADAM10, and the fluorescence intensity was measured by flow cytometry ( n = 4). E - F . Confluent A549 monolayers were starved overnight and stimulated with 10 µM ionomycin or 100 µM TFP in the presence or absence of 10 µM GI for 1 min–1 h. Supernatants were subjected to FRET-based activity measurements ( n = 3). In A to F, 0.1% DMSO served as vehicle control. The data are shown as the means + SD. The statistical analyses was performed using a one-sample t-test followed by an FDR analysis. Asterisks without lines represent differences compared with the control, and those with lines represent differences between groups (* p < 0.05, ** p < 0.01, *** p < 0.001 and **** p < 0.0001)

Journal: Cell Communication and Signaling : CCS

Article Title: Regulation of ADAM10 activity through microdomain-dependent intracellular calcium changes

doi: 10.1186/s12964-024-01891-5

Figure Lengend Snippet: Regulation of cell-associated and soluble ADAM10 activity by Ca 2+ transients. A , B : Confluent A549 monolayers were starved overnight and stimulated with 10 µM ionomycin or 100 µM TFP in the presence or absence of 10 µM GI for 1, 10, 30 and 60 min. Lysates were collected and subjected to E-cadherin cleavage analyses. The ratio of mature to pro-form was quantified as measure of maturation by densitometry ( n = 3). C , D : Confluent A549 cell monolayers were starved overnight and stimulated with 10 µM ionomycin, 1 µM thapsigargin or 100 µM TFP for 1 min–1 h. Subsequently, the cells were subjected to surface staining for ADAM10, and the fluorescence intensity was measured by flow cytometry ( n = 4). E - F . Confluent A549 monolayers were starved overnight and stimulated with 10 µM ionomycin or 100 µM TFP in the presence or absence of 10 µM GI for 1 min–1 h. Supernatants were subjected to FRET-based activity measurements ( n = 3). In A to F, 0.1% DMSO served as vehicle control. The data are shown as the means + SD. The statistical analyses was performed using a one-sample t-test followed by an FDR analysis. Asterisks without lines represent differences compared with the control, and those with lines represent differences between groups (* p < 0.05, ** p < 0.01, *** p < 0.001 and **** p < 0.0001)

Article Snippet: Polyclonal ADAM10 C-terminal Antibody , Invitrogen by Thermo Fisher Scientific (Frankfurt, Germany) , 1 μg/ml.

Techniques: Activity Assay, Staining, Fluorescence, Flow Cytometry, Control

Ophiobolin A-induced ADAM10 activity. A , B : Confluent A549 monolayers were starved overnight and stimulated with 10 µM ophiobolin A in the absence or presence of 10 µM GI. DMSO (0.1%) served as a vehicle control. In A, cells were transfected with AP-BTC prior to seeding, and AP-BTC cleavage was analyzed via the AP assay ( n = 3). In B, lysates were collected and subjected to E-cadherin cleavage analyses ( n = 3). The quantitative data are shown as the means + SDs. Asterisks without lines represent differences compared with the control, and those with lines represent differences between groups (* p < 0.05, ** p < 0.01, *** p < 0.001 and **** p < 0.0001)

Journal: Cell Communication and Signaling : CCS

Article Title: Regulation of ADAM10 activity through microdomain-dependent intracellular calcium changes

doi: 10.1186/s12964-024-01891-5

Figure Lengend Snippet: Ophiobolin A-induced ADAM10 activity. A , B : Confluent A549 monolayers were starved overnight and stimulated with 10 µM ophiobolin A in the absence or presence of 10 µM GI. DMSO (0.1%) served as a vehicle control. In A, cells were transfected with AP-BTC prior to seeding, and AP-BTC cleavage was analyzed via the AP assay ( n = 3). In B, lysates were collected and subjected to E-cadherin cleavage analyses ( n = 3). The quantitative data are shown as the means + SDs. Asterisks without lines represent differences compared with the control, and those with lines represent differences between groups (* p < 0.05, ** p < 0.01, *** p < 0.001 and **** p < 0.0001)

Article Snippet: Polyclonal ADAM10 C-terminal Antibody , Invitrogen by Thermo Fisher Scientific (Frankfurt, Germany) , 1 μg/ml.

Techniques: Activity Assay, Control, Transfection

Spatial control of ADAM10 activation by Ca 2+ influx via TRP channels. A - C : HEK WT and stable HEK µOR-TRPC4, HEK-TRPM3α2 and HEK-TRPC5 cells were transfected with AP-BTC and stimulated with 10 µM ionomycin, 60 nM Englerin A (EngA) or 100 µM pregnenolone sulfate (PregS) for 30 min in the presence or absence of 10 µM GI. DMSO (0.1%) served as a vehicle control. AP-BTC cleavage was analyzed via the AP assay ( n = 3). D-H: HEK WT and stable HEK µOR-TRPC4, HEK-TRPM3α2 and HEK-TRPC5 cells were seeded on poly-L-lysine coated cover slips, grown to 70% confluence and subjected to calcium imaging. EngA (60 nM) ( A , C ) or 100 µM PregS ( B ) was automatically injected 1.5 min after the baseline measurement, followed by recording for 20 min. DMSO (0.1%) served as the baseline measurement and the vehicle control. The number of experiments across the number of cells N/n is indicated in the figures. The amplitude ( G ) and area under the curve ( H ) were quantified and plotted. The quantitative data are shown as the means + SDs. Statistical analyses were performed using ANOVA followed by Tukey´s post-hoc test for multiple comparisons between groups in G and H. Asterisks without lines represent differences compared with the control, and those with lines represent differences between groups (* p < 0.05, ** p < 0.01, *** p < 0.001 and **** p < 0.0001)

Journal: Cell Communication and Signaling : CCS

Article Title: Regulation of ADAM10 activity through microdomain-dependent intracellular calcium changes

doi: 10.1186/s12964-024-01891-5

Figure Lengend Snippet: Spatial control of ADAM10 activation by Ca 2+ influx via TRP channels. A - C : HEK WT and stable HEK µOR-TRPC4, HEK-TRPM3α2 and HEK-TRPC5 cells were transfected with AP-BTC and stimulated with 10 µM ionomycin, 60 nM Englerin A (EngA) or 100 µM pregnenolone sulfate (PregS) for 30 min in the presence or absence of 10 µM GI. DMSO (0.1%) served as a vehicle control. AP-BTC cleavage was analyzed via the AP assay ( n = 3). D-H: HEK WT and stable HEK µOR-TRPC4, HEK-TRPM3α2 and HEK-TRPC5 cells were seeded on poly-L-lysine coated cover slips, grown to 70% confluence and subjected to calcium imaging. EngA (60 nM) ( A , C ) or 100 µM PregS ( B ) was automatically injected 1.5 min after the baseline measurement, followed by recording for 20 min. DMSO (0.1%) served as the baseline measurement and the vehicle control. The number of experiments across the number of cells N/n is indicated in the figures. The amplitude ( G ) and area under the curve ( H ) were quantified and plotted. The quantitative data are shown as the means + SDs. Statistical analyses were performed using ANOVA followed by Tukey´s post-hoc test for multiple comparisons between groups in G and H. Asterisks without lines represent differences compared with the control, and those with lines represent differences between groups (* p < 0.05, ** p < 0.01, *** p < 0.001 and **** p < 0.0001)

Article Snippet: Polyclonal ADAM10 C-terminal Antibody , Invitrogen by Thermo Fisher Scientific (Frankfurt, Germany) , 1 μg/ml.

Techniques: Control, Activation Assay, Transfection, Imaging, Injection

AD inhibits ADAM10 expression in various cancer cells. (A) AD inhibited expression of ADAM10 in both protein showing in upper panel and mRNA showing in lower panel in the H1975 lung cancer cells. (B) AD inhibited expression of ADAM10 in both protein showing in upper panel and mRNA showing in lower panel in the A549 lung cancer cells. (C) AD inhibited expression of ADAM10 in both protein showing in upper panel and mRNA showing in lower panel in the BT549 breast cancer cells. (D) Quantitative results for ADAM10 protein levels. (E) Quantitative results for ADAM10 mRNA levels. AD, adenosine; ADAM10, a disintegrin and metalloproteinase domain 10. *P <0.05; **P < 0.005; ****P < 0.0001.

Journal: Frontiers in Immunology

Article Title: A disintegrin and metalloproteinase domain 10 expression inhibition by the small molecules adenosine, cordycepin and N6, N6-dimethyladenosine and immune regulation in malignant cancers

doi: 10.3389/fimmu.2024.1434027

Figure Lengend Snippet: AD inhibits ADAM10 expression in various cancer cells. (A) AD inhibited expression of ADAM10 in both protein showing in upper panel and mRNA showing in lower panel in the H1975 lung cancer cells. (B) AD inhibited expression of ADAM10 in both protein showing in upper panel and mRNA showing in lower panel in the A549 lung cancer cells. (C) AD inhibited expression of ADAM10 in both protein showing in upper panel and mRNA showing in lower panel in the BT549 breast cancer cells. (D) Quantitative results for ADAM10 protein levels. (E) Quantitative results for ADAM10 mRNA levels. AD, adenosine; ADAM10, a disintegrin and metalloproteinase domain 10. *P <0.05; **P < 0.005; ****P < 0.0001.