Direct technetium-99m labeling of anti-hepatoma monoclonal antibody fragment: a radioimmunoconjugate for hepatocellular carcinoma imaging

Bian, Hui Jie; Chen, Zhi‐Nan; Deng, Jing Lan

doi:10.3748/wjg.v6.i3.348

Cited by 13 publications

(5 citation statements)

References 12 publications

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“…To analyze the interaction between HAb18G/CD147 and CyPA, 100 mg of HAb18G/CD147 (a recombinant extracellular fragment of HAb18G/CD147, prepared in our lab) was incubated with an equivalent amount of CyPA (Alexis Biochemical) overnight at room temperature (RT). The mixture was then added to the gel, which was coupled with 200 mg of mouse anti-human HAb18G/CD147 monoclonal antibody (MAb) HAb18 (prepared in our lab) [25][26][27][28][29][30][31][32][33], for incubation with gentle end-over-end mixing for 4 h. After the bound proteins were eluted, aliquots of the eluent were analyzed by a Western blot developed with rabbit anti-human CyPA antibody (diluted 1:2000; Calbiochem-Novabiochem) and horseradish peroxidase (HRP)conjugated goat anti-rabbit IgG (diluted 1:5000; Amersham Pharmacia). Purchased CyPA (2.5 mg) was used as the positive control.…”

Section: Methodsmentioning

confidence: 99%

Function of HAb18G/CD147 in Invasion of Host Cells by Severe Acute Respiratory Syndrome Coronavirus

et al. 2005

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To identify the function of HAb18G/CD147 in invasion of host cells by severe acute respiratory syndrome (SARS) coronavirus (CoV), we analyzed the protein-protein interaction among HAb18G/CD147, cyclophilin A (CyPA), and SARS-CoV structural proteins by coimmunoprecipitation and surface plasmon resonance analysis. Although none of the SARS-CoV proteins was found to be directly bound to HAb18G/CD147, the nucleocapsid (N) protein of SARS-CoV was bound to CyPA, which interacted with HAb18G/CD147. Further research showed that HAb18G/CD147, a transmembrane molecule, was highly expressed on 293 cells and that CyPA was integrated with SARS-CoV. HAb18G/CD147-antagonistic peptide (AP)-9, an AP of HAb18G/CD147, had a high rate of binding to 293 cells and an inhibitory effect on SARS-CoV. These results show that HAb18G/CD147, mediated by CyPA bound to SARS-CoV N protein, plays a functional role in facilitating invasion of host cells by SARS-CoV. Our findings provide some evidence for the cytologic mechanism of invasion by SARS-CoV and provide a molecular basis for screening anti-SARS drugs.

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Section: Methodsmentioning

confidence: 99%

Function of HAb18G/CD147 in Invasion of Host Cells by Severe Acute Respiratory Syndrome Coronavirus

et al. 2005

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“…[8][9][10]13,14 In the future, we need to generate F(ab)2 or scFv fragments of the monoclonal antibody to avoid or reduce its antigenicity for use in human subjects, which has already been carried out for monoclonal anti-carcinoembryonic antigen antibody. 32…”

Section: Discussionmentioning

confidence: 99%

“…Labeling of monoclonal antibodies with 99m Tc has been found to be effective for radioimmunoscintigraphy. [8][9][10][11]14 The antibody was labeled with 99m Tc as described by Karube et al 8 with minor modifi cations. Anti-KL-6/ MUC1 antibody (2.5 mg) was reduced by reaction with 2-mercaptoethanol at room temperature for 60 min.…”

Section: Methodsmentioning

confidence: 99%

“…[3][4][5] Specifi c monoclonal antibodies are extremely powerful tools for the diagnosis or treatment of some diseases; for example, daclizumab (a monoclonal antibody against the α chain of the interleukin 2 receptor) has been used to prevent acute rejection after renal transplantation 6 and rituximab (a monoclonal antibody against CD20) has been used to treat lymphomas. 7 Radiolabeling of tumorspecifi c antibodies for use as in vivo tracers has been attempted to detect the distribution of neoplasms by scintigraphy, [8][9][10][11] and one of these approaches is now in clinical use. 12 Mucins comprise a group of high-molecular-weight glycoproteins.…”

Section: Introductionmentioning

confidence: 99%

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Radioimmunoscintigraphy of pancreatic cancer in tumor-bearing athymic nude mice using 99mtechnetium-labeled anti-KL-6/MUC1 antibody

et al. 2008

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“…a relation of radioactivity of the labeled molecules capable of specific binding to the antigen to the total radioactivity of the labeled radioimmunoconjugate molecules. Traditionally, radioimmunoconjugates are incubated with the tumor cells expressing the target molecules on their surface [1][2][3][4][5][6]. This approach is connected with a number of limitations and drawbacks.…”

Section: Introductionmentioning

confidence: 99%

Application of Magnetic Particles for Fast Determination of Immunoreactive Fraction of 68Ga-Labelled VHH Antibodies to PD-L1

Avrov,

Shatik,

Zaitsev

et al. 2023

Sovrem Tehnol Med

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Quantification of the immunoreactive fraction (IRF) of radioactive isotope-labeled antibodies or their fragments is necessary to assess the specific activity of radiopharmaceuticals. Traditionally, cells expressing the target molecules on their surface are used to determine IRF, but such analysis is time-consuming and has difficulties with standardization.The aim of the study was to develop a fast and reliable method for quantitative determination of IRF by 68 Ga-labeled VHH antibodies to PD-L1 based on the use of magnetic particles coated with antigen molecules.Materials and Methods. Commercially available magnetic particles coated with protein A have been used in our study. The antigen conjugated with the Fc fragment (PD-L1-Fc) was immobilized on the particles. The IRF value of 68 Ga radionuclide-labeled nanobodies (VHH) against PD-L1 ( 68 Ga-VHH-PD-L1) was determined using magnetic particles coated with antigen molecules and cells expressing the antigen on their surface. When VHH antibodies were conjugated to 68 Ga radionuclide, protein molecules were modified using bifunctional chelating agents: tetraazacyclododecanetetraacetic acid (DOTA) or deferoxamine (DFO). The magnitude of IRF was defined as the ratio of radioactivity specifically bound to particles or cells to the total radioactivity added to the sample.Results. The specificity of the 68 Ga-VHH-PD-L1 radioimmunoconjugate binding to the antigen-coated magnetic particles has been proved. Some special aspects, which should be taken into consideration when using this method, have been established. The comparison of the IRF estimates using the antigen-expressing cells and magnetic particles has not revealed any significant differences in the results obtained in our study. Nevertheless, the presented method based on magnetic particles with immobilized antigen molecules requires only 15 min to determine the radioimmunoconjugate IRF, which is of fundamental importance for the routine assessment of the specificity of radiopharmaceuticals containing short-lived isotopes.

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Direct technetium-99m labeling of anti-hepatoma monoclonal antibody fragment: a radioimmunoconjugate for hepatocellular carcinoma imaging

Cited by 13 publications

References 12 publications

Function of HAb18G/CD147 in Invasion of Host Cells by Severe Acute Respiratory Syndrome Coronavirus

Function of HAb18G/CD147 in Invasion of Host Cells by Severe Acute Respiratory Syndrome Coronavirus

Radioimmunoscintigraphy of pancreatic cancer in tumor-bearing athymic nude mice using 99mtechnetium-labeled anti-KL-6/MUC1 antibody

Application of Magnetic Particles for Fast Determination of Immunoreactive Fraction of 68Ga-Labelled VHH Antibodies to PD-L1

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