Journal:

Article Title: Entry of Human Parechovirus 1

doi: 10.1128/JVI.75.4.1958-1967.2001

Figure Lengend Snippet: Localization of HPEV-1 capsid proteins and integrin subunits (α2, αV, β1, and β3) during the early steps of infection. Red, virus; green, integrin subunits; yellow, colocalization. Bars, 10 μm.

Article Snippet: In addition, MAbs against the following cell surface molecules were used: integrin α V subunit (1.2 mg/ml) (L230; ATCC) ( 16 ), integrin α 2 subunit (1 mg/ml) (Chemicon), and integrin β 1 subunit (1 mg/ml) (Chemicon).

Techniques: Infection

Journal: Journal of Lipid Research

Article Title: Hepatoprotective drug screening identifies daclatasvir, a promising therapeutic candidate for MASLD by targeting PLIN2

doi: 10.1016/j.jlr.2025.100835

Figure Lengend Snippet: Daclatasvir treatment ameliorates liver damage and fibrosis in MCD diet-induced MASH mouse model. A: Schematic illustration of the experimental workflow for the daclatasvir treatment strategy in a methionine-choline deficient (MCD) diet-induced MASH mouse model. B: Liver weight, LW/BW, and LW/BMI were recorded for MCD diet-fed mice after 3 weeks of treatment with either vehicle or daclatasvir. C: Representative images of H&E, PSR, and CD11b staining of liver samples from vehicle or daclatasvir treated mice at 4 weeks of MCD diet administration. Scale bar, 200 μm for H&E and PSR; 100 μm for CD11b. D: Quantitative results for PSR and CD11b staining shown in (C). E: Enzyme activities of serum hepatic transaminases in MCD diet-fed mice after 3 weeks of treatment with either vehicle or daclatasvir. F–H: The mRNA expression of genes associated with lipid catabolism (F), inflammation (G), and fibrosis (H) in liver tissues from MCD diet-induced MASH mice following 3 weeks of daclatasvir or vehicle treatment. For (B–H), n = 6 mice per group. Data are presented as mean ± SD; ∗ P < 0.05, ∗∗ P < 0.01; Student’s t test for statistics.

Article Snippet: The sections were incubated with a rabbit anti-CD11b primary antibody (BM3925, Boster) overnight at 4°C, followed by incubation with a goat anti-rabbit fluorophore-conjugated secondary antibody (A-11036, Invitrogen).

Techniques: Staining, Expressing

Journal: Oncotarget

Article Title: The metastasis suppressor CD82/KAI1 inhibits fibronectin adhesion-induced epithelial-to-mesenchymal transition in prostate cancer cells by repressing the associated integrin signaling

doi: 10.18632/oncotarget.13767

Figure Lengend Snippet: A. Stably CD82-transfected DU145 and antisense CD82 fragment-transfected LNCaP cell clones suspended in culture medium were pretreated with a mouse normal IgG 1 or integrin β 1 -blocking IgG 1 for 2 hours and cultured on plates precoated with fibronectin (FN) for 8 hours. Cells in suspension (Susp), and cells grown onto the plates were examined for expression of E-cadherin and Snail using immunoblotting analysis. Bar graphs under the immunoblots indicate the relative band intensity of E-cadherin and Snail normalized to the loading control (actin). Values are the mean ± s.d. from three separate experiments performed in triplicate (*, **, †, and ‡, p < 0.03). ND, not detectable. B-D. Cells grown on FN were transfected with either scrambled (scrmb) siRNAs or integrin α 3 (B), α 5 (C), or α 6 (D) subunit-specific siRNAs and then examined for E-cadherin and Snail expression.

Article Snippet: Monoclonal Antibodies to integrin β 1 subunit (P5D2) and α-SMA (E184) and an inhibitor to ILK (Cpd22) were purchased from Millipore (Billerica, MA).

Techniques: Stable Transfection, Transfection, Clone Assay, Blocking Assay, Cell Culture, Suspension, Expressing, Western Blot, Control

Journal: Oncotarget

Article Title: The metastasis suppressor CD82/KAI1 inhibits fibronectin adhesion-induced epithelial-to-mesenchymal transition in prostate cancer cells by repressing the associated integrin signaling

doi: 10.18632/oncotarget.13767

Figure Lengend Snippet: A. PZ-HPV-7 prostate epithelial cells were lysed with Brij 97 detergent, and immunoprecipitation (IP) was performed with normal mouse IgG or anti-CD82 antibody. The immunoprecipitates were analyzed by immnublotting using anti-integrin β 1 , α 3 , α 5 , or α 6 antibody. B. CD82 mutant cDNA, which encodes CD82 with a large extracellular loop (LEL) substituted with that of TM4SF2 as illustrated, was generated by PCR and subcloned into the pAdEasy-1 adenoviral vector to produce recombinant adenovirus. C. CD82-deficient PC3 prostate cancer cells grown on fibronectin (FN) were infected with adenovirus containing a wild-type (wt) or mutant (mt) CD82 expression construct, and Brij 97 detergent lysates were subjected to immunoprecipitation with an anti-β 1 integrin antibody followed by immunoblotting analysis using antibodies that recognize the C-terminus or LEL of CD82 and the LEL of TM4SF2. D. PC3 cells grown on poly-L(+)-lysine (p-Lys) or FN were infected with adenovirus containing a wt- or mt-CD82 expression construct and then assessed for the protein levels of E-cadherin and Snail. E. PC3 cells grown on FN were infected with wt-CD82 construct-containing adenovirus either alone or together with mt-CD82 construct-containing adenovirus and examined for E-cadherin and Snail expression. Numbers in parentheses represent the MOI values of adenovirus.

Article Snippet: Monoclonal Antibodies to integrin β 1 subunit (P5D2) and α-SMA (E184) and an inhibitor to ILK (Cpd22) were purchased from Millipore (Billerica, MA).

Techniques: Immunoprecipitation, Mutagenesis, Generated, Plasmid Preparation, Recombinant, Infection, Expressing, Construct, Western Blot