Journal: Frontiers in Oncology

Article Title: ADAMTS2 drives prostate cancer progression by activating FAK/PI3K/AKT signaling and suppressing ferroptosis via COL1A1

doi: 10.3389/fonc.2026.1784882

Figure Lengend Snippet: ADAMTS2 is coexpressed and physically interacts with COL1A1 in PCa. (A) Heatmap of the top 10 genes most strongly related to ADAMTS2 expression in the TCGA-PRAD cohort. (B) Scatter plot showing the correlation between ADAMTS2 and COL1A1 mRNA levels. (C) PPI network prediction from the STRING database indicating a potential interaction between ADAMTS2 and COL1A1. (D, E) Validation of COL1A1 mRNA ( n =6 pairs) and protein ( n =3 pairs) levels in paired human PCa and adjacent non-tumoral tissues using qRT-PCR and WB (paired two-tailed Student’s t-test). (F, G) Reciprocal Co-IP assessments illustrating physical interaction between endogenous and exogenously expressed ADAMTS2 and COL1A1 in DU145 cells. (H) WB of COL1A1 protein levels upon ADAMTS2 overexpression or knockdown in DU145 cells. (I) Evaluation of COL1A1 upregulation and downregulation effectiveness by WB in DU145 cells. Representative images from three independent experiments are shown. All quantitative data are presented as the mean ± SD from three independent biological replicates (n=3; unpaired two-tailed Student’s t-test). *P < 0.05, ***P < 0.001.

Article Snippet: The lentiviral particles carrying ADAMTS2 or COL1A1 overexpression constructs, as well as short hairpin RNAs (shRNAs) targeting ADAMTS2 or COL1A1, were acquired from GeneChem (China).

Techniques: Expressing, Biomarker Discovery, Quantitative RT-PCR, Two Tailed Test, Co-Immunoprecipitation Assay, Over Expression, Knockdown

Journal: Frontiers in Oncology

Article Title: ADAMTS2 drives prostate cancer progression by activating FAK/PI3K/AKT signaling and suppressing ferroptosis via COL1A1

doi: 10.3389/fonc.2026.1784882

Figure Lengend Snippet: ADAMTS2 confers resistance to ferroptosis in PCa cells through COL1A1. (A) GSEA showing negative enrichment of ferroptosis-related gene signatures in TCGA-PRAD tumors with high ADAMTS2 expression. (B, C) Dose–response curves and IC 50 values for ferroptosis inducers erastin and RSL3 in control, ADAMTS2-overexpressing, and ADAMTS2-knockdown DU145 cells. IC 50 values were determined using non-linear regression analysis (n=3). (D) WB of SLC7A11 and GPX4 protein levels in ADAMTS2-knockdown cells in the presence or absence of COL1A1 overexpression. (E) WB of SLC7A11 and GPX4 in ADAMTS2-overexpressing cells in the presence or absence of COL1A1 knockdown. (F, G) MDA levels reflecting lipid peroxidation in the indicated cell groups. (H–K) Quantification of reduced GSH and oxidized GSSG under the specified genetic manipulations. All quantitative data are presented as the mean ± SD from three independent biological replicates (n=3). Statistical significance for multiple group comparisons was determined using one-way ANOVA followed by Tukey’s post hoc test. *P < 0.05.

Article Snippet: The lentiviral particles carrying ADAMTS2 or COL1A1 overexpression constructs, as well as short hairpin RNAs (shRNAs) targeting ADAMTS2 or COL1A1, were acquired from GeneChem (China).

Techniques: Expressing, Control, Knockdown, Over Expression

Journal: Frontiers in Oncology

Article Title: ADAMTS2 drives prostate cancer progression by activating FAK/PI3K/AKT signaling and suppressing ferroptosis via COL1A1

doi: 10.3389/fonc.2026.1784882

Figure Lengend Snippet: Suppression of ADAMTS2 suppresses tumor growth in vivo and downregulates FAK/PI3K/AKT signaling and ferroptosis resistance markers. (A) Tumor growth curves of xenografts derived from control or ADAMTS2-knockdown DU145 cells in nude mice, evaluated every 7 days over 28 days. (n=5 mice per group). Statistical significance was determined using two-way ANOVA followed by Sidak’s multiple comparisons test. (B) Representative photographs and quantification of tumor weight at the experimental endpoint. Data are presented as the mean ± SD (n=5 mice per group; two-tailed Student’s t-test). (C) WB of ADAMTS2, p-FAK, FAK, p-PI3K, PI3K, COL1A1, p-AKT, AKT, SLC7A11, and GPX4 in excised xenograft tumor tissues. Representative blots from three independent tumor samples per group are shown. All quantitative data are presented as the mean ± SD. *P < 0.05.

Article Snippet: The lentiviral particles carrying ADAMTS2 or COL1A1 overexpression constructs, as well as short hairpin RNAs (shRNAs) targeting ADAMTS2 or COL1A1, were acquired from GeneChem (China).

Techniques: In Vivo, Derivative Assay, Control, Knockdown, Two Tailed Test

Journal: bioRxiv

Article Title: WDR44 drives de novo α-synuclein aggregation at the lysosomal membrane and promotes neuronal dysfunction in Parkinson’s Disease

doi: 10.64898/2026.04.03.716340

Figure Lengend Snippet: Validation of WDR44 knockdown and confirmation of WDR44 colocalization with α -SYN in vivo and neuronal culture. a , b , c , Knockdown validation for WDR44 KD induced by shRNA at the mRNA level ( a ) and at the protein level with a representative Western blot (b) and its relative quantification (c, scatter dot plot represented as mean ± SEM, n=3). d , e , f Knockdown validation for IGF2R KD induced by shRNA at the mRNA level (d) and at the protein level with a representative Western blot (e) and its relative quantification (f, scatter dot plot represented as mean ± SEM, N=3). g , h , i Knockdown validation for BLTP3A KD induced by shRNA at the mRNA level (g) and at the protein level with a representative Western blot (h) and its relative quantification (i, scatter dot plot represented as mean ± SEM, N=3, 2-way ANOVA with Dunnett’s multiple comparisons test comparing all conditions to the WT (WB)). j , Representative Western blot membrane showing the specificity of the antibodies targeting WDR44 used in this study (Bethyl for biochemistry, Invitrogen for IF). Samples loaded were HEK293T lysates (WT or shRNA KD) or RPE-E1 knockout for WDR44 (through CRISPR-KO ). k , Quantification of total mCherry protein levels for the filter retardation assay related to and showing equal loaded protein levels (scatter dot plot represented as mean ± SEM, n=3, 2-way ANOVA with Dunnett’s multiple comparisons test). l , Representative confocal images showing HEK293T transfected with LIPA-TDP-43 (top panel) or LIPA-EMPTY (bottom panel), exposed to 90 min blue light and stained for endogenous LAMP2 (yellow) and WDR44 (cyan). The small panels on the right show magnified views of the region highlighted by the red box. Intensity profiles (right) are displayed over the red-dotted line in the small panels. Scale bar, 5 µm. m , Representative confocal images showing HEK293T transfected with 3K-α-SYN exposed to 24 hrs of doxycycline and stained for endogenous LAMP2 (yellow) and WDR44 (cyan). The small panels on the right show magnified views of the region highlighted by the red box. Intensity profiles (right) are displayed over the red-dotted line in the small panels. Scale bar, 5 µm. n , Representative confocal images showing iDA neurons transfected with either LIPA-α-SYN exposed to 90 min blue light and stained for endogenous TH (white), LAMP2 (yellow) and WDR44 (cyan). The small panels on the right show magnified views of the region highlighted by the red box. Intensity profiles (right) are displayed over the red-dotted line in the small panels. Scale bar, 5 µm. o , Representative confocal images showing mouse dopaminergic neurons infected with an AAV-LIPA-α-SYN, exposed to the blue light for 1h/day for 7 days and stained for endogenous TH (white) and WDR44 (green). The small panels on the right show magnified views of the region highlighted by the red box. Intensity profiles (right) are displayed over the red-dotted line in the small panels. Scale bar, 5 µm. Each experiment was independently replicated at least three times, and results were reproducible across replicates. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001.

Article Snippet: Total RNA was extracted from HEK293T cells stably expressing either scramble or shRNA constructs using the RNeasy Mini Kit (Qiagen, cat. 74104).

Techniques: Biomarker Discovery, Knockdown, In Vivo, shRNA, Western Blot, Quantitative Proteomics, Membrane, Knock-Out, CRISPR, Transfection, Staining, Infection