Journal: Cancers

Article Title: Are Integrins Still Practicable Targets for Anti-Cancer Therapy?

doi: 10.3390/cancers11070978

Figure Lengend Snippet: Selected clinical trials of agents targeting integrins. Non-exhaustive listing of the recent most important clinical studies with integrin inhibitors and their salient features and results).

Article Snippet: Cilengitide (EMD 121974, anti-αVβ3/αVβ5 integrin cyclic peptide) (Merck-Serono): total no. of trials: 21 (+ 8 terminated) , , , , , , .

Techniques: Activity Assay

Journal: PLoS ONE

Article Title: Phosphorylated fibronectin enhances cell attachment and upregulates mechanical cell functions

doi: 10.1371/journal.pone.0218893

Figure Lengend Snippet: A : Cell spreading assay on fibronectin (Fn) fragments as defined in . B : Inhibition of αvβ3 and α5β1 integrins on CKII-treated fibronectin. Fibroblasts were preincubated for 10 min with 2.5μg/ml integrin isoform-specific anti-αvβ3 antibodies, anti-α5 antibodies, or 10μg/ml cyclic RGD. Cell spreading area of single cells was measured 30 min after seeding. Statistical comparison done with Student’s t -test between pair of samples connected with lines on the column plots: ***, p-value<0.005; **, p-value<0.01; *, p-value<0.05; not significant (ns).

Article Snippet: The anti-αvβ3 antibody (clone LM6 Fisher-Scientific MAB1976BMI) was diluted to 2.5μg/ml in the 200μl cell samples.

Techniques: Inhibition, Comparison

Journal: PLoS ONE

Article Title: Phosphorylated fibronectin enhances cell attachment and upregulates mechanical cell functions

doi: 10.1371/journal.pone.0218893

Figure Lengend Snippet: A: Sequence alignment of the FnIII 9-10 for various species, namely human, mouse, rat, bovine, chicken, pleurodeles waltl (PW), xenopus tropicalis (XT), xenopus laevis (XL) and danio rerio (DR). Experimentally determined phosphorylation sites for human fibronectin are depicted in red, predicted phosphorylation sites are shown in green. B: Structure of αvβ3 integrin headpiece docked to FnIII 9-10 . RGD (yellow) and synergy site (blue) are shown in sticks representation. C: Sequences of 20 RGD (yellow) containing human integrin ligands were analyzed -/+ 50 residues around their RGD. Shown are experimentally verified phosphor-sites. Black boxes indicate the sequences of the analyzed structures in D. D: The structures of fibronectin, vitronectin, bone sialoprotein, fibrinogen A and osteopontin were analyzed in proximity of their RGD (yellow) sites and experimentally verified phosphorylated sites (red) are highlighted.

Article Snippet: The anti-αvβ3 antibody (clone LM6 Fisher-Scientific MAB1976BMI) was diluted to 2.5μg/ml in the 200μl cell samples.

Techniques: Sequencing, Phospho-proteomics

Journal: Viruses

Article Title: An Improved αvβ6-Receptor-Expressing Suspension Cell Line for Foot-and-Mouth Disease Vaccine Production

doi: 10.3390/v14030621

Figure Lengend Snippet: Flow cytometry analyses of integrin and heparan sulphate expression on the cell surface of BHK-21 cell lines. Four adherent cell lines (BHK-21 Strain 31, 35 and 38, and BHK 21 Clone 13), and the respective suspension cell lines generated from them (SP Strain 31, 35, and 38, and SP Clone 13) were analyzed by flow cytometry using a panel of antibodies recognizing α5β1, β1, αvβ3, αvβ5, αvβ6, αvβ8 and heparan sulphate. BHK21C13-2P was analyzed alongside and served as a comparative suspension cell line. Matched isotype antibodies served as negative controls and the expression of each receptor is presented as the percentage of positive cells.

Article Snippet: Primary mAbs used: anti-integrin β1 (clone 9EG7, 553715, IgG2a; BD Pharmingen, San Diego, CA, USA), anti αvβ3 (clone LM609, MAB1976, IgG1; Merck), anti-αvβ5 (clone P1F6, MAB1961, IgG1; Merck), anti-α5β1 (clone SAM-1, ab6131, IgG2b; Abcam, Cambridge, UK), anti-αvβ6 (clone 10D5, ab77906, IgG2a; Abcam), anti-integrin β8 (clone ADWA 16, IgG1; gift from Amha Atakilit at the University of California, San Francisco) and anti-heparan sulphate (clone JM403, 370730-1, IgM; AMSBIO, Abingdon, UK).

Techniques: Flow Cytometry, Expressing, Generated

Journal: Cancers

Article Title: Are Integrins Still Practicable Targets for Anti-Cancer Therapy?

doi: 10.3390/cancers11070978

Figure Lengend Snippet: Selected clinical trials of agents targeting integrins. Non-exhaustive listing of the recent most important clinical studies with integrin inhibitors and their salient features and results).

Article Snippet: Etaracizumab (MEDI-522, anti-αVβ3 integrin antibody) (MedImmune, Astra Zeneca): total trial 9 (+1 discontinued early) , , , , , , .

Techniques: Clinical Proteomics, Control, Activity Assay, Comparison