Journal: Blood

Article Title: CD4+ T cells from patients with acquired thrombotic thrombocytopenic purpura recognize CUB2 domain-derived peptides.

doi: 10.1182/blood-2015-10-668053

Figure Lengend Snippet: Figure 2. CD41 T-cell response in an HLA-DRB1*03–positive patient with acquired TTP. (A) Analysis of PBMCs from an HLA-DRB1*03–positive patient in the acute phase of the disease. Incubations of PBMCs with AIM-V (medium control), SEB (positive control), ADAMTS13 (10 mg/mL), ASYILIRD peptide (10 mg/mL), CP_ASYILIRD peptide (10 mg/mL) with modified anchor residues (negative control). CD40L is plotted on the y-axis whereas CD4 is plotted on the x-axis. The percentage of CD41 T cells expressing CD40L is depicted in the upper right quadrant. (B) Analysis of PBMCs obtained from an HLA-DRB1*03–positive healthy volunteer. PBMCs were incubated as described for the sample depicted in the panel A column. PBMCs of this HLA-DRB1*03–positive healthy volunteer only respond to SEB stimulation and not to stimulation with ADAMTS13, ASYILIRD, or CP_ASYILIRD peptides. We acquired at least 0.5 3 106 events for each sample analyzed.

Article Snippet: © 2016 by The American Society of Hematology 1606 BLOOD, 24 MARCH 2016 x VOLUME 127, NUMBER 12 to rest for 24hours andwere then stimulatedwith either 10mg/mLFINVAPHAR peptide, CP_FINVAPHAR peptide, ASYLIRD peptide, CP_ASYILIRD peptide, full-length ADAMTS13 (FL-ADAMTS13), Staphylococcus aureus enterotoxin B (SEB) (1 mg/mL; Sigma-Aldrich, St Louis, MO), or AIM-V medium only; all conditions were supplemented with 1 mg/mL blocking antibody aCD40 pure (clone HB14; Miltenyi Biotec, Auburn, CA).

Techniques: Control, Positive Control, Modification, Negative Control, Expressing, Incubation

Journal: OncoTargets and therapy

Article Title: SP1-Mediated Upregulation of lncRNA LINC01614 Functions a ceRNA for miR-383 to Facilitate Glioma Progression Through Regulation of ADAM12

doi: 10.2147/OTT.S242854

Figure Lengend Snippet: The Primers Used in This Study for RT-PCR

Article Snippet: The qPCR detection for SP1, LINC01614 and ADAM12 was conducted by using SYBR Green qPCR kits (MCE, Hangzhou, Zhejiang, China) according to the kits’ protocols.

Techniques:

Journal: OncoTargets and therapy

Article Title: SP1-Mediated Upregulation of lncRNA LINC01614 Functions a ceRNA for miR-383 to Facilitate Glioma Progression Through Regulation of ADAM12

doi: 10.2147/OTT.S242854

Figure Lengend Snippet: LINC01614 abrogated the miR-383-mediated suppression on ADAM12. ( A ) Venn diagram. ( B ) Overall survival curves were evaluated by GEPIA algorithm. ( C ) cBioPortal algorithm analyzed the genetic alternation of related genes. ( D ) GEPIA algorithm analyzed ADAM12 expression in glioma samples from TCGA data. ( E ) qPCR determined ADAM12 levels in glioma specimens. ( F ) UALCAN algorithm analyzed ADAM12 expression across diverse cancer types. ( G ) GO and KEGG pathway analysis of ADAM12 positively correlated genes in glioma. ( H ) The predicted binding sites for miR-383 in ADAM12 mRNA 3ʹ-UTR. ( I ) Luciferase reporter assays. ( J ) qPCR determined LINC01614 and ADAM12 levels. ( K ) qPCR measured ADAM12 levels. ( L ) Western blot examined LINC01614 levels. **P < 0.01. n.s (not significant) represents “P > 0.05”.

Article Snippet: The qPCR detection for SP1, LINC01614 and ADAM12 was conducted by using SYBR Green qPCR kits (MCE, Hangzhou, Zhejiang, China) according to the kits’ protocols.

Techniques: Expressing, Binding Assay, Luciferase, Western Blot

Journal: PLoS Genetics

Article Title: Microenvironmental Regulation by Fibrillin-1

doi: 10.1371/journal.pgen.1002425

Figure Lengend Snippet: This model of fibrillin-1 molecules arranged as parallel, staggered molecules within the beads-on-a-string microfibril was previously proposed . Two staggered fibrillin-1 molecules are shown with colored domains (see for domain structure), while other fibrillin molecules within the microfibril are depicted as dashed black lines. Beaded regions of the microfibril are represented as gray scalloped circles. The inset shows the N-terminus (black) of one molecule extending through cbEGF5 and crossing over the middle portion of a second molecule (shown from Hybrid2 through cbEGF27). In this model, binding sites for ADAMTSL proteins (within the first 8-cysteine domain, the proline-rich domain, and the adjacent generic EGF-like domain) and for LTBP-1 (within the first hybrid domain) on one molecule are very close to the integrin-binding RGD site (contained in the fourth 8-cysteine domain) on a second molecule. Mutations in the fourth 8-cysteine domain can cause SSKS, presumably by disrupting integrin binding. The fifth 8-cysteine domain or TB5 contains mutations in FBN1 that result in WMS , geleophysic (GD) or acromicric dysplasia (AD) . Mutations in ADAMTSL2 also lead to GD, and mutations in ADAMTS10 lead to WMS. We propose that this cluster of molecular interactions (magnified in the inset) constitutes a microenvironment controlling thick skin and musculoskeletal growth.

Article Snippet: A full length human ADAMTS10 clone (SC309981) was purchased from Origene, and mutations in this clone were corrected.

Techniques: Binding Assay

Journal: Cell Communication and Signaling : CCS

Article Title: Loss of ADAM15 prevents necroptosis induction by partial RIPK1 degradation due to enhanced TNF-R1 surface expression and basal caspase-8 activation

doi: 10.1186/s12964-025-02530-3

Figure Lengend Snippet: ADAM15 knockdown affects necroptosis but not apoptosis, NFκB, and MAPK signaling in U937 cells. a CRISPR Cas-9 mediated knockout of ADAM15 was monitored by WB using two different antibodies (R&D: MAB935 and HPA: HPA011633). Knockout (ko) cells are further referred to as ΔADAM15. Actin served as a loading control. n = 3 experiments performed. b ADAM15 knockout was validated by flow cytometry. The green curve represents staining using an anti-ADAM15 antibody (upper panel) or an isotype control (lower panel) in U937 wt cells. The red curve represents staining in U937 ΔADAM15 cells. The dashed non-coloured curves represent unstained cells. Right-shifted curves indicate higher fluorescence intensity. Representative data of n = 3 experiments are shown. c The degradation of IκB was monitored by WB. Band densities were quantified, and IkB:actin ratios are shown (green: U937 wt; red: U937 ΔADAM15). Representing n = 3 independent experiments. d The activation/phosphorylation of MAPK was monitored by WB. Band densities were quantified, and MAPK:actin ratios are shown (green: U937 wt; red: U937 ΔADAM15). Representative data of n = 3 experiments are shown. e Representative scatter plots of flow cytometry-based cell death analyses. The x-axis shows changes in fluorescence intensity due to increased Annexin V-FITC binding. The y-axis indicates increased fluorescence of 7AAD due to binding to DNA. Multiple ( n = 9) assays were quantified (right panel; green bars: WT; red bars: ΔADAM15). *: p = 0,05; ** p = 0,01; *** p = 0,001. f WB was used to monitor TC-mediated apoptosis (PARP-1 and caspases-3 and −8) and TCz-mediated necroptosis (MLKL oligomer). n = 3 experiments performed. Actin serves as a loading control

Article Snippet: For the quantification of DR and ADAM15 surface expression, the following biotinylated antibodies were used, diluted 1:200 in PBS: CD120a/TNF-R1 (130–106–358, Miltenyi Biotec), CD261/DR4 (103–109-084, Miltenyi Biotec), CD262/DR5 (103–097–303, Miltenyi Biotec), CD95 (103–113-067, Miltenyi Biotec), DR3 (130–105-075, Miltenyi Biotec), ADAM15 (BAF935, R&D Systems).

Techniques: Knockdown, CRISPR, Knock-Out, Control, Flow Cytometry, Staining, Fluorescence, Activation Assay, Phospho-proteomics, Binding Assay

Journal: Cell Communication and Signaling : CCS

Article Title: Loss of ADAM15 prevents necroptosis induction by partial RIPK1 degradation due to enhanced TNF-R1 surface expression and basal caspase-8 activation

doi: 10.1186/s12964-025-02530-3

Figure Lengend Snippet: ADAM15 knockdown affects necroptosis but not apoptosis induction in U937 cells mediated by TRAIL, FasL, TL1a, and Obatoclax. a-c Representative scatter plots of flow cytometry-based cell death analyses upon incubation with TRAIL (a), FasL (b), or TL1a ( c ) The x-axis shows changes in fluorescence intensity due to increased Annexin V-FITC binding. The y-axis indicates increased fluorescence of 7AAD due to binding to DNA. Multiple ( n = 3 per ligand) assays were quantified (right panels; green bars: WT; red bars: ΔADAM15) d Obatoclax mediated apoptosis (Oba) and necroptosis (Obaz) compared to TNF/BV-6 (TB: apoptosis) and TNF/BV-6/zVAD (TBz: necroptosis) were monitored by WB in U937 wt (left panel) and U937 ΔADAM15 cells (right panel). Represents n = 3 independent experiments. Tubulin serves as a loading control

Article Snippet: For the quantification of DR and ADAM15 surface expression, the following biotinylated antibodies were used, diluted 1:200 in PBS: CD120a/TNF-R1 (130–106–358, Miltenyi Biotec), CD261/DR4 (103–109-084, Miltenyi Biotec), CD262/DR5 (103–097–303, Miltenyi Biotec), CD95 (103–113-067, Miltenyi Biotec), DR3 (130–105-075, Miltenyi Biotec), ADAM15 (BAF935, R&D Systems).

Techniques: Knockdown, Flow Cytometry, Incubation, Fluorescence, Binding Assay, Control

Journal: Cell Communication and Signaling : CCS

Article Title: Loss of ADAM15 prevents necroptosis induction by partial RIPK1 degradation due to enhanced TNF-R1 surface expression and basal caspase-8 activation

doi: 10.1186/s12964-025-02530-3

Figure Lengend Snippet: Shotgun proteome analysis reveals regulated proteins upon ADAM15 knockout in U937 wt and U937 ΔADAM15 cells. a Volcano plot (p-value: 0.01; fdr: 0.01; fold-change cutoff 1: 0.3; fold-change cutoff 2: −0.3; min. samples for significance 0.75) shows proteins enriched in wt cells (red) versus U937 ΔADAM15 cells. The top 25 modulated proteins are indicated along with the selected proteins. The top annotated GSEA groups are shown: b ‘Regulation of endocytosis’, c ‘Regulation of autophagy’, d ‘Macroautophagy’, e ‘Organelle fusion’, f ‘Vacuole organization’, g ‘Regulation of mitochondrion organization’, h ‘Cell redox homeostasis’, i ‘Epigenetic regulation of gene expression’, and j ‘Mitotic cell cycle phase transition’. The upper panel shows the respective GO-termini, encircled by the involved proteins (Fold change is color-coded). The lower panels show the respective proteins as STRING-DB (V12.0) based networks. ADAM15 is highlighted for each network (dashed red circle)

Article Snippet: For the quantification of DR and ADAM15 surface expression, the following biotinylated antibodies were used, diluted 1:200 in PBS: CD120a/TNF-R1 (130–106–358, Miltenyi Biotec), CD261/DR4 (103–109-084, Miltenyi Biotec), CD262/DR5 (103–097–303, Miltenyi Biotec), CD95 (103–113-067, Miltenyi Biotec), DR3 (130–105-075, Miltenyi Biotec), ADAM15 (BAF935, R&D Systems).

Techniques: Knock-Out, Gene Expression, Sublimation

Journal: Cell Communication and Signaling : CCS

Article Title: Loss of ADAM15 prevents necroptosis induction by partial RIPK1 degradation due to enhanced TNF-R1 surface expression and basal caspase-8 activation

doi: 10.1186/s12964-025-02530-3

Figure Lengend Snippet: Analysis of differential protein expression by WB and caspase-8 activity. a Depicts the validation of up- and down-modulation of selected proteins from the proteome analysis. b Representative (of n = 3) WB for RIPK1 probed with two different antibodies (cell signaling: #3493S and BD: 610,459). c Representative (of n = 3) WB analysis of various cell death-associated and non-related proteins. d Caspase-8 appears partially active in U937 ΔADAM15 compared to wt cells, indicated by reduced p55/44 and increased p43/41 and p18 (blue box – enhanced contrast). e Validation of increased basal Caspase-8 activity by flow cytometry. Dashed colorless curves indicate no staining. The green curve indicates wt cells stained with IETD-FITC, and the red curve indicates U937 ADAM15 cells with IETD-FITC. X-axis shift to the right side indicates increased fluorescence due to binding of IETD to active caspase-8 (p-18). Representative of n = 3 experiments. f Flow cytometry-based analysis of death receptor and ADAM15 surface expression. The non-coloured curves represent unstained and Strep-AF488-stained cells, the green curve WT, and the red curve ADAM15 cells. Representative data of n = 3 experiments

Article Snippet: For the quantification of DR and ADAM15 surface expression, the following biotinylated antibodies were used, diluted 1:200 in PBS: CD120a/TNF-R1 (130–106–358, Miltenyi Biotec), CD261/DR4 (103–109-084, Miltenyi Biotec), CD262/DR5 (103–097–303, Miltenyi Biotec), CD95 (103–113-067, Miltenyi Biotec), DR3 (130–105-075, Miltenyi Biotec), ADAM15 (BAF935, R&D Systems).

Techniques: Expressing, Activity Assay, Biomarker Discovery, Flow Cytometry, Staining, Fluorescence, Binding Assay

Journal: Cell Communication and Signaling : CCS

Article Title: Loss of ADAM15 prevents necroptosis induction by partial RIPK1 degradation due to enhanced TNF-R1 surface expression and basal caspase-8 activation

doi: 10.1186/s12964-025-02530-3

Figure Lengend Snippet: ADAM15 knockout in Jurkat cells results in abrogation of necroptosis induction and enhanced basal caspase-8 activity. a ADAM15 knockout was monitored by WB and b flow cytometry. The green curve represents staining using an anti-ADAM15 antibody (upper panel) or an isotype control (lower panel) in U937 wt cells. The red curve represents staining in Jurkat ΔADAM15 cells. The dashed non-coloured curves represent unstained cells. Right-shifted curves indicate higher fluorescence intensity. c degradation of IκB and d phosphorylation of MAPK are not affected by ADAM15 knockout. Band densities were quantified, and IκB:actin or MAPK:actin ratios are shown (green: Jurkat wt; red: Jurkat ΔADAM15). e WB analysis of cell death in Jurkat cells. f Representation of multiple ( N = 4) flow cytometry-based cell death analyses (green bars: WT; red bars: ΔADAM15). g WB analysis of Obatoclax (Oba) mediated cell death in Jurkat cells. TNF/BV-6 or TNF/BV-6/zVAD treatment served as control. h WB was probed for cell death-related and unrelated proteins, revealing reduced amounts of full-length RIPK1 (third panel, left) and pre-activated caspase-8 (first panel, right). i The enhanced basal activation of caspase-8 was validated using flow cytometry. The dashed colorless curves indicate no staining. The green curve indicates wt cells stained with IETD-FITC, and the red curve indicates U937 ADAM15 cells with IETD-FITC. X-axis shift to the right side indicates increased fluorescence due to binding of IETD to active caspase-8 (p-18). In a, c, d, e, and f, actin or tubulin served as loading controls. Where not stated otherwise, representative data of n = 3 experiments are shown

Article Snippet: For the quantification of DR and ADAM15 surface expression, the following biotinylated antibodies were used, diluted 1:200 in PBS: CD120a/TNF-R1 (130–106–358, Miltenyi Biotec), CD261/DR4 (103–109-084, Miltenyi Biotec), CD262/DR5 (103–097–303, Miltenyi Biotec), CD95 (103–113-067, Miltenyi Biotec), DR3 (130–105-075, Miltenyi Biotec), ADAM15 (BAF935, R&D Systems).

Techniques: Knock-Out, Activity Assay, Flow Cytometry, Staining, Control, Fluorescence, Phospho-proteomics, Activation Assay, Binding Assay

Journal: Cell Communication and Signaling : CCS

Article Title: Loss of ADAM15 prevents necroptosis induction by partial RIPK1 degradation due to enhanced TNF-R1 surface expression and basal caspase-8 activation

doi: 10.1186/s12964-025-02530-3

Figure Lengend Snippet: Exogenously expressed RIPK1 is degraded in U937 ΔADAM15 cells, and ADAM15 is partially located in lysosome-like organelles. a WB analysis of exogenously expressed RIPK1: accumulation of full-length RIPK1 in U937 wt cells, and moderately in U937 ΔADAM15 cells (black arrowhead). In U937 ΔADAM15 cells, RIPK1 is directly cleaved (grey arrowhead). Actin serves as a loading control. b Lamp-2, Cathepsin D, and also ADAM15 are enriched in the lysosome-containing fraction (LysIP), compared to total lysate or soluble proteins (SNT). nM represents the lysosome-depleted non-magnetic fraction remaining after the isolation procedure. p8 and p10 represent two different homogenization procedures. Nucleoporin p62 and actin serve as loading/purity controls. c Fluorescence microscopy monitoring ADAM15 (red) and Lamp-1 (green) reveals partial co-localization (arrowheads) of both proteins in U937 cells. Manders’ tM1/tM2 values are: 0.495/0.619 (upper left); 0.403/: 0.362 (upper right), (lower left) 0.434/0.377; (lower right) 0.302/0.371 (lower right). Values of tM1/tM2 > 0.5 are considered moderate, > 0.7 strong colocalized. DNA (blue) is stained with DAPI. Scale bar indicates 10 µm. Where not stated otherwise, representative data of n = 3 experiments are shown. d Working model of ADAM15-mediated control of necroptosis induction (Model created in BioRender)

Article Snippet: For the quantification of DR and ADAM15 surface expression, the following biotinylated antibodies were used, diluted 1:200 in PBS: CD120a/TNF-R1 (130–106–358, Miltenyi Biotec), CD261/DR4 (103–109-084, Miltenyi Biotec), CD262/DR5 (103–097–303, Miltenyi Biotec), CD95 (103–113-067, Miltenyi Biotec), DR3 (130–105-075, Miltenyi Biotec), ADAM15 (BAF935, R&D Systems).

Techniques: Control, Isolation, Homogenization, Fluorescence, Microscopy, Staining

Journal: bioRxiv

Article Title: The novel coronary artery disease risk factor ADAMTS-7 modulates atherosclerotic plaque formation by degradation of TIMP-1

doi: 10.1101/2023.03.06.531428

Figure Lengend Snippet: Matrisome profiling of atherosclerotic aortas in Apoe-/- (n=3) and Apoe-/-Adamts7-/- (n=4) mice. A . Volcano plot displaying matrisome proteins that were more abundant in Apoe-/-Adamts7-/- mice (right) as compared to Apoe-/- mice. B . The known ADAMTS-7 targets Comp and thrombospondin 1 (Thbs1) were detected at lower levels in aortic tissue of Apoe-/- as compared to Apoe-/-Adamts7-/- mice. C . As putative novel targets of ADAMTS-7, we observed higher levels for the endogenous tissue inhibitors of MMPs (Timp) Timp-2 and, in particular, Timp-1 (Timp2 was detected in only one of three aortas of Apoe-/- mice). Student’s t-test with imputation of missing values (i.e., not detected proteins). Each symbol represents one animal. Data are mean and s.e.m .

Article Snippet: A clone containing the consensus ADAMTS7 coding sequence (NM_014272 Human Untagged Clone) was purchased from Origene (Rockville, USA).

Techniques:

Journal: bioRxiv

Article Title: The novel coronary artery disease risk factor ADAMTS-7 modulates atherosclerotic plaque formation by degradation of TIMP-1

doi: 10.1101/2023.03.06.531428

Figure Lengend Snippet: Binding of TIMP-1 to ADAMTS-7. A . ADAMTS-7 constructs. We cloned full-length ADAMTS-7 containing a C-terminal V5-tag (ADAMTS7-V5) and two constructs lacking the C-terminal disintegrin domain and thrombospondin repeats ( ΔTSPr ADAMTS7-V5) or the N-terminal catalytic domain ( Δcat ADAMTS7-V5), respectively. The constructs were ectopically expressed in HEK 293 cells. B . Co-IP of ADAMTS-7 and TIMP-1-HA. After precipitation of TIMP-1-HA, ADAMTS7-V5 was detectable. C, D . Binding of TIMP-1-HA to different parts of ADAMTS-7. After precipitation of TIMP-1-HA, ΔTSPr ADAMTS7-V5 was detectable ( C ) while in contrast Δcat ADAMTS7-V5 was not detectable ( D ) indicating binding of TIMP-1 to the N-terminal part containing the catalytic domain.

Article Snippet: A clone containing the consensus ADAMTS7 coding sequence (NM_014272 Human Untagged Clone) was purchased from Origene (Rockville, USA).

Techniques: Binding Assay, Construct, Clone Assay, Co-Immunoprecipitation Assay

Journal: bioRxiv

Article Title: The novel coronary artery disease risk factor ADAMTS-7 modulates atherosclerotic plaque formation by degradation of TIMP-1

doi: 10.1101/2023.03.06.531428

Figure Lengend Snippet: Degradation of TIMP-1 by ADAMTS-7. A, B . In vitro degradation assay. TIMP-1-HA was either overexpressed with full-length ADAMTS7-V5 (TS7-V5), the C-terminal part lacking the N-terminal catalytic domain ( Δcat TS7-V5) or an empty vector (mock). ADAMTS-7 constructs and TIMP-1 were detected by immunoblotting in cell lysates (CL) and the supernatant (SN). Vinculin served as housekeeping control. After co-expression with full-length ADAMTS7-V5, less TIMP-1-HA was detectable compared to mock or Δcat TS7-V5 co-expression. C, D . Fluorescence intensity of TIMP-1-GFP after co-expression with an empty vector (mock), TS7-V5 or Δcat TS7-V5 indicates reduced TIMP-1 levels in the presence of full-length ADAMTS-7. E, F . GFP-positive cells after overexpression of TIMP-1-GFP with either empty vector (mock), TS7-V5 or Δcat TS7-V5. Presence of full-length ADAMTS-7 leads to reduced TIMP-1-GFP fluorescence. One-way ANOVA with Sidak’s multiple comparisons test. Symbols indicate independent experiments. Data are mean and s.e.m .

Article Snippet: A clone containing the consensus ADAMTS7 coding sequence (NM_014272 Human Untagged Clone) was purchased from Origene (Rockville, USA).

Techniques: In Vitro, Degradation Assay, Plasmid Preparation, Construct, Western Blot, Control, Expressing, Fluorescence, Over Expression

Journal: bioRxiv

Article Title: The novel coronary artery disease risk factor ADAMTS-7 modulates atherosclerotic plaque formation by degradation of TIMP-1

doi: 10.1101/2023.03.06.531428

Figure Lengend Snippet: Influence of ADAMTS-7 on inhibition of MMP-9 by TIMP-1. A . Endogenous MMP-2-/MMP-9-activity of hCASMC in the presence (TS7-V5) or absence (mock transfection) of full-length ADAMTS-7. Presence of full-length ADAMTS-7 reduced the inhibitory potential of TIMP-1. Student’s t-test. B - D . Gel zymography with endogenous (pro-) MMP-2 and MMP-9 in the presence of either mock or TS7-V5 ( B ). Quantification of MMP-9 and MMP-2 bands reveals higher MMP-9 ( C ) and MMP-2 activity ( D ) in the presence of full-length ADAMTS-7, respectively. Mann-Whitney (C) and Student’s t-test (D). E . Reduced inhibition of recombinant MMP-9 (rMMP-9) by TIMP-1 in the presence (TS7-V5) as compared to the absence (mock) of full-length ADAMTS-7. Student’s t-test. F, G . Secondary to precipitating FLAG-tagged MMP-9 (MMP-9-FLAG) more TIMP-1-HA could be recovered in the presence of full-length ADAMTS-7 (TS7-V5) as compared to Δcat TS7-V5. Representative Western Blot. Student’s t-test. H, I . Picosirius red staining of collagen fibers in aortic root sections of Apoe-/- and Apoe-/-Adamts7-/- mice which were fed a Western diet. Mice lacking Adamts-7 displayed increased collagen content as compared to Apoe-/- mice. Student’s t-test. Symbols indicate independent experiments/animals.

Article Snippet: A clone containing the consensus ADAMTS7 coding sequence (NM_014272 Human Untagged Clone) was purchased from Origene (Rockville, USA).

Techniques: Inhibition, Activity Assay, Transfection, Zymography, MANN-WHITNEY, Recombinant, Western Blot, Staining

Journal: bioRxiv

Article Title: The novel coronary artery disease risk factor ADAMTS-7 modulates atherosclerotic plaque formation by degradation of TIMP-1

doi: 10.1101/2023.03.06.531428

Figure Lengend Snippet: ADAMTS7 expression in human atherosclerotic carotid plaques. ADAMTS7 mRNA was detected at higher levels in caps of unstable as compared to caps of stable plaques. Mann-Whitney test. Symbols indicate independent human individuals.

Article Snippet: A clone containing the consensus ADAMTS7 coding sequence (NM_014272 Human Untagged Clone) was purchased from Origene (Rockville, USA).

Techniques: Expressing, MANN-WHITNEY

Journal: bioRxiv

Article Title: The novel coronary artery disease risk factor ADAMTS-7 modulates atherosclerotic plaque formation by degradation of TIMP-1

doi: 10.1101/2023.03.06.531428

Figure Lengend Snippet: Schematic illustration of the ADAMTS-7/TIMP-1 interaction in atherosclerosis. Genetic variation and inflammation can lead to an upregulation of ADAMTS7 expression in vascular tissues. As one downstream target, TIMP-1 binds to ADAMTS-7 and is subsequently degraded. Reduced availability of TIMP-1 can lead to MMP-independent and -dependent downstream effects. Among the latter, MMP-9 activity is increased and thereby plaque collagen content reduced. Reduced plaque collagen content can reduce plaque stability and increase plaque vulnerability. Both MMP-independent and -dependent downstream mechanisms may result in altered coronary plaque remodeling and render ADAMTS-7 a promising target in CAD and MI.

Article Snippet: A clone containing the consensus ADAMTS7 coding sequence (NM_014272 Human Untagged Clone) was purchased from Origene (Rockville, USA).

Techniques: Expressing, Activity Assay

Journal: Oncotarget

Article Title: Interaction between the ADAMTS-12 metalloprotease and fibulin-2 induces tumor-suppressive effects in breast cancer cells

doi:

Figure Lengend Snippet: (A) representative tissue images for detection of ADAMTS-12 and fibulin-2 in healthy breast tissue and breast carcinoma samples. Arrows indicate detection of ADAMTS-12 and fibulin-2 in grade 1 breast carcinoma. Scale bar, 200 μm. (B) Kaplan-Meier survival plots showing a better outcome of breast patients with high expression level of both ADAMTS12 and FBLN2 (Hts+Hfb). Plots for high ADAMTS12 and low FBLN2 (Hts+Lfb); low ADAMTS12 and high FBLN2 (Lts+Hfb); and low ADAMTS12 and low FBLN2 (Lts+Lfb) are also included.

Article Snippet: A breast cancer tissue array containing 16 tumors samples from different tumor stages (Acris Antibodies) was employed to evaluate ADAMTS12 and FBLN2 expression in human breast samples.

Techniques: Expressing