α ν β 3  (R&D Systems)

Journal: Molecular Imaging and Biology

Article Title: Quantifying Molecular Changes in the Preeclamptic Rat Placenta with Targeted Contrast-Enhanced Ultrasound Imaging

doi: 10.1007/s11307-025-01988-4

Figure Lengend Snippet: Quantification methods for binding contrast agent.​ a LE method: Acoustic intensity at t = t Burst – 40 s represents attached contrast agent value. b dTE method: Schematic showing changes before (t ≈ 2 min) and after Burst (t = t Burst + 30 s). The schematic illustrates the dTE method to quantify the attached contrast agent within the placenta. After tail vein injection, MBs adhere to the α ν β 3 integrin on the endothelial cells. Ten minutes later, a destructive ultrasound pulse is applied to destroy the adherent MBs, and 1 min later, the free-circulating MBs are replenished. c BCM method: data from t = 0 ~ 2 min are fitted into the complete equation for each pixel to calculate the binding constant of the attached MBs

Article Snippet: Placental sections were incubated with mouse polyclonal α ν β 3 integrin (1:200 dilution, Bioss antibodies, bs‐1310R) and secondary HRP-polymer (Rabbit-On-Rodent HRP-polymer, Biocare Medical, Pacheco, CA).

Techniques: Binding Assay, Injection

Journal: Molecular Imaging and Biology

Article Title: Quantifying Molecular Changes in the Preeclamptic Rat Placenta with Targeted Contrast-Enhanced Ultrasound Imaging

doi: 10.1007/s11307-025-01988-4

Figure Lengend Snippet: α ν β 3 integrin expression in NP vs RUPP placentas. a IHC staining in NP placenta. b IHC staining in RUPP placenta, showing decreased intensity. c Quantification of α ν β 3 integrin protein expression. Each data point represents the mean of 3–4 slices from a single placenta from each rat subject. ( n = 4 rats; mean ± SEM; * p < 0.05). d Relative α ν β 3 mRNA levels ( n = 6 each; normalized to β-Actin; mean ± SEM; ** p < 0.01)

Article Snippet: Placental sections were incubated with mouse polyclonal α ν β 3 integrin (1:200 dilution, Bioss antibodies, bs‐1310R) and secondary HRP-polymer (Rabbit-On-Rodent HRP-polymer, Biocare Medical, Pacheco, CA).

Techniques: Expressing, Immunohistochemistry

Journal: Radiation Oncology (London, England)

Article Title: Targeting α ν β 3 and α ν β 5 inhibits photon-induced hypermigration of malignant glioma cells

doi: 10.1186/1748-717X-6-132

Figure Lengend Snippet: Photon-induced stimulation of integrin expression . A: FACS analysis of α ν β 3 (upper row) and α ν β 5 (lower row) expression with (red) and without (black) photon irradiation with single doses of 2 Gy (left) and 10 Gy (right). B: Graphical analysis of integrin α ν β 3 (gray bars) and α ν β 5 (black bars) expression with (bars) and without (red line) irradiation with single photon doses of 2, 5, and 10 Gy in U87 (upper chart) and Ln229 (lower chart) glioma cells. Display of mean value ± standard deviation (SD); statistical analysis using Student's t -test (*, indicating significance p < 0.05)

Article Snippet: Integrin blockade was performed using monoclonal antibodies directed against α ν β 3 - (MAB3050, R&D) and α ν β 5 -integrins (MAB 2528, R&D).

Techniques: Expressing, Irradiation, Standard Deviation

Journal: Radiation Oncology (London, England)

Article Title: Targeting α ν β 3 and α ν β 5 inhibits photon-induced hypermigration of malignant glioma cells

doi: 10.1186/1748-717X-6-132

Figure Lengend Snippet: Inhibiton of Ln229 glioma cell migration by integrin inhibition . Quantitative analysis of Vn-based transmigration of Ln229 glioma cells following single photon doses of 0, 2, and 10 Gy without and with the addition of 50 ng/ml anti-α ν β 3 - and -α ν β 5 -antibodies and corresponding isotype controls. Display of mean value ± standard deviation (SD); statistical analysis using Student's t -test (*, indicating significance p < 0.05)

Article Snippet: Integrin blockade was performed using monoclonal antibodies directed against α ν β 3 - (MAB3050, R&D) and α ν β 5 -integrins (MAB 2528, R&D).

Techniques: Migration, Inhibition, Transmigration Assay, Standard Deviation

Journal: Radiation Oncology (London, England)

Article Title: Targeting α ν β 3 and α ν β 5 inhibits photon-induced hypermigration of malignant glioma cells

doi: 10.1186/1748-717X-6-132

Figure Lengend Snippet: Inhibiton of U87 glioma cell migration by integrin inhibition . Quantitative analysis of Vn-based transmigration of U87 glioma cells following single photon doses of 0, 2, and 10 Gy without and with the addition of 50 ng/ml anti-α ν β 3 - and -α ν β 5 -antibodies and corresponding isotype controls.

Article Snippet: Integrin blockade was performed using monoclonal antibodies directed against α ν β 3 - (MAB3050, R&D) and α ν β 5 -integrins (MAB 2528, R&D).

Techniques: Migration, Inhibition, Transmigration Assay

Journal: International Journal of Molecular Sciences

Article Title: Pleiotrophin Activates cMet- and mTORC1-Dependent Protein Synthesis through PTPRZ1—The Role of α ν β 3 Integrin

doi: 10.3390/ijms251910839

Figure Lengend Snippet: Ligand binding to α ν β 3 integrin activates cMet and mTORC1 in endothelial cells. Serum-starved HUVEC were stimulated with PTN (100 ng/mL), LM609 (10 ng/mL), crizotinib (1 μM) or combinations, for 10 min in A, C, and D and 2 h in B. ( A , C ) Representative Western blot images of phosphorylated and total S6K1 and 4EBP1 in HUVEC. The bands were quantified, and the results are presented as the mean ± standard deviation of the % ratio of phosphorylated to total protein compared to the corresponding control (cells incubated with 10 ng/mL IgG, considered 100%). The bullets on the graphs indicate independent assays. ( B ) Representative Western blot images of the newly synthesized peptides labeled with puromycin from total cell lysates from serum-starved HUVEC treated with the tested agents as shown. Puromycin was added for the last 10 min of incubation. Beta (β)-actin was used as a loading control. Results are expressed as the mean ± standard deviation (n = 3) of the % ratio of puromycin incorporation (puromycilation) compared to the control (cells incubated with 10 ng/mL IgG, considered 100%). ( D ) Representative confocal microscopy images and quantification from PLA assay of the tyrosine phosphorylation sites of cMet (red dots) in serum-starved HUVEC treated with IgG or LM609. Nuclei stained with Draq5 are shown in blue. Scale bars correspond to 10 μm. Box plots indicate the median, mean, and range of detected signals (8–10 image fields with 4–8 cells per image, per sample, n = 3).

Article Snippet: Function-blocking monoclonal antibody against α ν β 3 (LM609) was from Merck (#MAB1976, Merck KGaA, Darmstadt, Germany).

Techniques: Ligand Binding Assay, Western Blot, Standard Deviation, Control, Incubation, Synthesized, Labeling, Confocal Microscopy, Staining

Journal: International Journal of Molecular Sciences

Article Title: Pleiotrophin Activates cMet- and mTORC1-Dependent Protein Synthesis through PTPRZ1—The Role of α ν β 3 Integrin

doi: 10.3390/ijms251910839

Figure Lengend Snippet: A schematic representation of the PTN/PTPRZ1 signaling pathway that includes α ν β integrin and leads to cMet and mTORC1 activation and enhanced protein synthesis. ( A ) PTN binds to PTPRZ1 and leads to cMet activation, as previously shown . PTPRZ1 deletion is also known to lead to cMet activation . cMet activates mTORC1, which results in enhanced protein synthesis and cell migration. ( B ) LM609 and PTN 112–136 bind to α ν β integrin and activate cMet, mTORC1, and protein synthesis. The arrows signify up-regulation.

Article Snippet: Function-blocking monoclonal antibody against α ν β 3 (LM609) was from Merck (#MAB1976, Merck KGaA, Darmstadt, Germany).

Techniques: Activation Assay, Migration

Journal: Molecular Therapy Oncology

Article Title: Conditionally replicative adenovirus as a therapy for malignant peripheral nerve sheath tumors

doi: 10.1016/j.omton.2024.200783

Figure Lengend Snippet: Adenovirus binding affinity to MPNST cell lines and viral receptor expression (A) Schematic of viral genome for Ad vectors used in binding assay. (B) Each cell line was infected with Ad vectors equipped with either WT (Ad5), RGD fiber-modified (RGD), or chimeric Ad5/Ad3 fiber (Ad5/3) at 100 VP/cell. Binding was allowed to proceed for 2 h at 4°C, then was assessed by qPCR. (C) Flow cytometry analysis of CAR and integrin expression. MPNST cell lines were incubated with fluorescent antibodies against α V β 3 and α V β 5 integrins and coxsackie adenovirus receptor (CAR). The data are shown as a relative percentage of positive cells scored among at least 10,000 cells assessed. (D) Flow cytometry plots by cell line with respective isotype control for viral entry receptors in MPNST cell lines and iHSC1 λ controls. Error bars represents ± standard deviation. ∗p < 0.05; ∗∗ p < 0.01; ∗∗∗p < 0.001; ∗∗∗∗p < 0.0001, Student's t test.

Article Snippet: Cells were plated and cultured for 24 h, non-enzymatically lifted off the plate (Sigma C5789), washed with PBS, and stained with antibodies for integrins α ν β 3 (BS-1310R-Cy3, Bioss) or immunoglobulin (Ig)G isotype control (BS-025P); α ν β 5 (565836-AF647, BD) or κ isotype control (565378-AF647, BD); and CAR (BS-2389R-A488, Bioss) or IgG Isotype control (BS-0295P-A488).

Techniques: Binding Assay, Expressing, Infection, Modification, Flow Cytometry, Incubation, Control, Standard Deviation

Journal: Theranostics

Article Title: Anti-Angiogenesis Therapy in the Vx2 Rabbit Cancer Model with a Lipase-cleavable Sn 2 Taxane Phospholipid Prodrug using α v β 3 -Targeted Theranostic Nanoparticles

doi: 10.7150/thno.7581

Figure Lengend Snippet: Characterization of docetaxel prodrug (Dxtl-PD) loaded PFC nanoparticles (NP). (A) Number-averaged hydrodynamic diameter distribution of α v β 3 -Dxtl-PD in hydrated state; (B) transmission electron microscopy (TEM) image of the integrin targeted nanoparticles (scale bar: 200 nm); (C) dissolution of Dxtl-PD over 3 days when incubated in PBS with albumin (red) or human plasma (green); HPLC traces of Dxtl-PD (D), Dxtl-PD-NP treated with PLA2 (E) and Dxtl-PD-NP “cracked” with isopropanol and exposed to PLA2. PLA2=phospholipase A2.

Article Snippet: The α ν β 3 -integrin antagonist was a quinalone nonpeptide developed by Bristol-Myers Squibb Medical Imaging (US patent 6,511,648 and related patents) and initially reported and characterized as the 111 In-DOTA conjugate RP478 and cyan 5.5 homologue TA145 .

Techniques: Transmission Assay, Electron Microscopy, Incubation

Journal: Theranostics

Article Title: Anti-Angiogenesis Therapy in the Vx2 Rabbit Cancer Model with a Lipase-cleavable Sn 2 Taxane Phospholipid Prodrug using α v β 3 -Targeted Theranostic Nanoparticles

doi: 10.7150/thno.7581

Figure Lengend Snippet: A) Cell proliferation via MTT assay comparing docetaxel prodrug targeted to angiotensin II activated integrin receptor in 2F2B endothelial cells versus Taxol ® and no drug targeted particles. At 96 hours, the prodrug was significantly (p < 0.05) more effective than the control and at least equivalent to Taxol ® . B) Cell proliferation via Vybrant Cell Metabolic Assay comparing docetaxel prodrug in HUVEC endothelial cells versus docetaxel in methanol and no drug targeted particles. Marked and equivalent reductions in cell proliferation were appreciated at 48, 72, and 96 hours with free drug and the integrin targeted Dxtl-PD NPs. * p<0.05.

Article Snippet: The α ν β 3 -integrin antagonist was a quinalone nonpeptide developed by Bristol-Myers Squibb Medical Imaging (US patent 6,511,648 and related patents) and initially reported and characterized as the 111 In-DOTA conjugate RP478 and cyan 5.5 homologue TA145 .

Techniques: MTT Assay, Metabolic Assay