Journal: BMC Cancer

Article Title: A combined blood based gene expression and plasma protein abundance signature for diagnosis of epithelial ovarian cancer - a study of the OVCAD consortium

doi: 10.1186/1471-2407-13-178

Figure Lengend Snippet: Gene list of the 27 genes from the three USC-models, corresponding Assay-on-Demand TaqMan ® probes, SAM-results from the second selection step, and coefficients of the final L1 penalized logistic regression model

Article Snippet: 115368 , AP2A1 , Hs00367123_m1 , yes , 0.15 , −0.199.

Techniques: Selection

Journal: BMC Cancer

Article Title: A combined blood based gene expression and plasma protein abundance signature for diagnosis of epithelial ovarian cancer - a study of the OVCAD consortium

doi: 10.1186/1471-2407-13-178

Figure Lengend Snippet: Gene names and functions of the 13 genes with mean log 2 expression fold changes (A) and six proteins with mean log 2 abundance values in controls, FIGO I/II patients, and FIGO III/IV patients (B)

Article Snippet: 115368 , AP2A1 , Hs00367123_m1 , yes , 0.15 , −0.199.

Techniques: Expressing, Activation Assay, Control

Journal: iScience

Article Title: FMRP-dependent translational control negatively regulates adapter protein complex 2-mediated endocytosis

doi: 10.1016/j.isci.2025.113062

Figure Lengend Snippet: FMRP negatively regulates the subcellular expression of AP-2 subunits (A) The subunits of three adapter protein complexes (AP1G1, AP2B1, and AP3D1), a postsynaptic marker (PSD95), a glial cell marker (GFAP), and GAPDH were examined in whole mouse brain lysates (INP) and synaptoneurosome (SNS) samples from mouse brain (postnatal day one). (B) Expression of PSD95, GFAP, and AP complexes in input (INP) and synaptoneurosomes (SNS). Signals were normalized to GAPDH. (C) AP-2 subunits, AP2A1 and AP2B1, in SNS samples prepared from eight pairs of WT and Fmr1 KO mouse brains are shown by western blot. (D) Expression levels of AP2A1 and AP2B1 in SNS samples from WT and Fmr1 KO mice. Data are represented as mean ± SEM. Unpaired t-test, N = 8, ∗ p < 0.05 and ∗∗ p < 0.01. (E) Representative images of cultured mouse cortical neurons (DIV12) from WT or Fmr1 KO mice. Immunofluorescence for AP2B1 overlaid with PSD95 and MAP2 to show the dendritic and synapse morphology. Enlarged boxes show dendritic segments of selected neurons. Scale bars, 40 μm. (F) Quantitative analysis of AP2B1 intensity and postsynaptic localization in soma and dendritic regions. Data are represented as mean ± SEM. Paired t-test, N = 3, ∗ p < 0.05 and ∗∗∗ p < 0.001.

Article Snippet: Ap2a1 TaqMan Gene Expression probe (Fam-MGB) , ThermoFisher , Assay ID: Mm00475919_m1.

Techniques: Expressing, Marker, Western Blot, Cell Culture, Immunofluorescence

Journal: iScience

Article Title: FMRP-dependent translational control negatively regulates adapter protein complex 2-mediated endocytosis

doi: 10.1016/j.isci.2025.113062

Figure Lengend Snippet: FMRP associates with Ap2a1 and Ap2b1 mRNAs and represses nascent protein translation (A) mRNA levels of Ap2a1 and Ap2b1 in WT and Fmr1 KO mouse brains. Gapdh mRNA was used as internal control. Data are represented as mean ± SEM. Unpaired t-test, N = 8. (B) FMRP eCLIP binding sites within the mRNA sequences of Ap2a1 and Ap2b1 in E13.5 mouse brains. The intact mRNA sequences of Ap2a1 and Ap2b1 , including their 3′UTR regions, are presented, with peaks indicating the read densities of predicted binding sites within these regions. Size-matched input (SMI) represents the background reading. (C) RNA-immunoprecipitation (RIP) of FMRP-mRNA complex from mouse brain lysates. Confirmation of FMRP immunoprecipitation by western blot. (D) qPCR analysis of FMRP-mRNA complexes. Both Ap2a1 and Ap2b1 mRNAs were detected by qPCR. Psd95 and Map1b mRNAs were used as positive controls and Gapdh mRNA as a negative control. Data are represented as mean ± SEM. Paired t-test, N = 3, ∗∗∗∗ p < 0.0001. (E) Newly synthesized AP2B1 was detected by puro-PLA. WT or Fmr1 KO cortical neurons were treated with puromycin for 5 min before fixation, and the puro-PLA signal show nascent synthesis of AP2B1 within the 5 min time frame. Scale bars, 20 μm. (F) Nascent synthesis of AP2B1 in the soma (left) and dendritic (right) regions of WT and Fmr1 KO neurons. Data are represented as mean ± SEM. Paired t - test, N = 4, ∗ p < 0.05.

Article Snippet: Ap2a1 TaqMan Gene Expression probe (Fam-MGB) , ThermoFisher , Assay ID: Mm00475919_m1.

Techniques: Control, Binding Assay, RNA Immunoprecipitation, Immunoprecipitation, Western Blot, Negative Control, Synthesized

Journal: Autophagy

Article Title: AP2M1 mediates autophagy-induced CLDN2 (claudin 2) degradation through endocytosis and interaction with LC3 and reduces intestinal epithelial tight junction permeability

doi: 10.1080/15548627.2021.2016233

Figure Lengend Snippet: Interaction of CLDN2 with clathrin and autophagy apparatus. (A) Co-immunoprecipitation studies showed an increased association of CLDN2 with AP2M1, AP2A1, clathrin, LC3 during early starvation and lysosomal marker protein LAMP2 at the later 12-h time point. The negative control includes immunoprecipitation with control IgG. (B) Quantification of CLDN2 fraction associated with various clathrin and autophagy proteins, as shown in panel A. (C) Confocal immunofluorescence examination showed that, CLDN2 (green) migrated away from the cell membrane and increased cytoplasmic colocalization with clathrin (red) after starvation (yellow). White bar: 5 µm. (D) AP2M1 immunoprecipitates showed increased presence of CLDN2, LC3 and clathrin after starvation. Representation of ≥ 3 independent experiments.

Article Snippet: The primary antibodies used included anti-CLDN2 (Abcam, ab53032), anti-LC3 (Sigma, L7543), anti-AP2A1 (Gene Tex, GTX22807), anti-phospho-AP2M1 (Cell signaling Technologies, 73,995), anti-clathrin, anti-AP2M1, anti-ATG7, anti-ATG16L1, anti-SQSTM1/p62, anti-ACTB/β.

Techniques: Immunoprecipitation, Marker, Negative Control, Immunofluorescence

Journal: Cellular and Molecular Life Sciences

Article Title: Mechano-regulation by clathrin pit-formation and passive cholesterol-dependent tubules during de-adhesion

doi: 10.1007/s00018-023-05072-4

Figure Lengend Snippet:

Article Snippet: AP2A1 Rabbit mAb , Abclonal , Cat#A4403.

Techniques: Purification, Recombinant, Cell Culture, Modification, Saline, Transfection, Plasmid Preparation, Software

Journal: Cancers

Article Title: MDK Activates the PI3K/AKT Axis to Induce AP2A1 Expression and Epithelial–Mesenchymal Transition in Colorectal Cancer

doi: 10.3390/cancers18081311

Figure Lengend Snippet: Correlation between MDK and AP2A1 and the expression of AP2A1 in CRC tissues and cells. ( A ) Volcano plot of RNA-seq data showing genes differentially expressed upon MDK knockdown (sh-MDK vs. sh-NC). Down- and up-regulated genes are highlighted in blue and red, respectively. ( B , C ) Correlation analyses between MDK and AP2A1 expression in the TCGA ( B ) and LinkedOmics ( C ) CRC cohorts. ( D , E ) Validation of MDK (( D ), GSE81558 ) and AP2A1 (( E ), TCGA) upregulation in CRC tumors compared to normal tissues. ( F – I ) MDK regulates AP2A1 expression. AP2A1 mRNA ( F , G ) and protein ( H , I ) levels were assessed by qRT-PCR and immunoblotting in cells with MDK overexpression or knockdown. Data are presented as mean ± SD; * p < 0.05, (Student’s t -test). The uncropped blots are shown in .

Article Snippet: Commercially synthesized human MDK and AP2A1 siRNAs were purchased from Shanghai Generay Biotech Co., Ltd. (Shanghai, China), with detailed information listed in .

Techniques: Expressing, RNA Sequencing, Knockdown, Biomarker Discovery, Quantitative RT-PCR, Western Blot, Over Expression

Journal: Cancers

Article Title: MDK Activates the PI3K/AKT Axis to Induce AP2A1 Expression and Epithelial–Mesenchymal Transition in Colorectal Cancer

doi: 10.3390/cancers18081311

Figure Lengend Snippet: AP2A1 functions as a downstream regulator of MDK-driven CRC invasion. ( A , B ) Immunoblotting verified that altering MDK levels correspondingly changes AP2A1 expression. Band intensities were quantified and normalized to Tubulin. ( C – F ) Functional rescue experiments showed that the increased invasion/migration caused by MDK overexpression (or the decrease caused by its knockdown) was reversed by co-manipulating AP2A1, as demonstrated by Transwell assays (with or without Matrigel). ×100 magnification; scale bar not shown. ( G , H ) Likewise, MDK-induced cell growth phenotypes were affected by changing AP2A1 levels. ×20 magnification; scale bar not shown. * p < 0.05 vs. control; # p < 0.05 vs. MDK-manipulated group (Student’s t -test). The uncropped blots are shown in .

Article Snippet: Commercially synthesized human MDK and AP2A1 siRNAs were purchased from Shanghai Generay Biotech Co., Ltd. (Shanghai, China), with detailed information listed in .

Techniques: Western Blot, Expressing, Functional Assay, Migration, Over Expression, Knockdown, Control

Journal: Cancers

Article Title: MDK Activates the PI3K/AKT Axis to Induce AP2A1 Expression and Epithelial–Mesenchymal Transition in Colorectal Cancer

doi: 10.3390/cancers18081311

Figure Lengend Snippet: MDK knockdown inhibits tumor growth in vivo. ( A ) IHC analysis of xenograft tumors for the expression of Ki-67, β-catenin, MMP2, MMP9, N-cadherin, and Vimentin in the control (NC) and MDK-KD groups. Scale bars = 200 μm. All data are presented as mean ± SD. ( B ) Western blot analysis of MDK and AP2A1 expression in the tumors. ( C ) qRT-PCR analysis of MDK expression in the tumors. Data are shown as means ± SD. ** p < 0.01. The uncropped blots are shown in .

Article Snippet: Commercially synthesized human MDK and AP2A1 siRNAs were purchased from Shanghai Generay Biotech Co., Ltd. (Shanghai, China), with detailed information listed in .

Techniques: Knockdown, In Vivo, Expressing, Control, Western Blot, Quantitative RT-PCR

Journal: Cancers

Article Title: MDK Activates the PI3K/AKT Axis to Induce AP2A1 Expression and Epithelial–Mesenchymal Transition in Colorectal Cancer

doi: 10.3390/cancers18081311

Figure Lengend Snippet: MDK-regulated AP2A1 expression and cell invasion depend on the activation of PI3K/AKT signaling. The expression of EMT markers ( A , B ) and key components of the PI3K/AKT pathway ( C ) was examined in CRC cells after co-transfection to manipulate MDK and AP2A1 levels. ( D ) The role of PI3K/AKT signaling was confirmed using the inhibitor LY294002. SW480 and RKO cells were pre-treated with LY294002 48 h post-transfection, then assessed for AP2A1 expression. Band intensities were quantified and normalized to GAPDH. ( E – G ) Functional effects of pathway inhibition: After LY294002 pre-treatment, the invasion, migration, and growth of SW480 cells were evaluated. ( E , F ): ×100 magnification; scale bar not shown. ( G ): ×20 magnification; scale bar not shown. * p < 0.05 vs. control; # p < 0.05 vs. MDK-overexpressing cells (Student’s t -test). The uncropped blots are shown in .

Article Snippet: Commercially synthesized human MDK and AP2A1 siRNAs were purchased from Shanghai Generay Biotech Co., Ltd. (Shanghai, China), with detailed information listed in .

Techniques: Expressing, Activation Assay, Cotransfection, Transfection, Functional Assay, Inhibition, Migration, Control

Journal: Cancers

Article Title: MDK Activates the PI3K/AKT Axis to Induce AP2A1 Expression and Epithelial–Mesenchymal Transition in Colorectal Cancer

doi: 10.3390/cancers18081311

Figure Lengend Snippet: Schematic illustration of the mechanism by which MDK promotes EMT progression and induces AP2A1 levels in CRC cells.

Article Snippet: Commercially synthesized human MDK and AP2A1 siRNAs were purchased from Shanghai Generay Biotech Co., Ltd. (Shanghai, China), with detailed information listed in .

Techniques: