ArticleInternational journal of molecular sciences2020
Inhibitory Monoclonal Antibodies and Their Recombinant Derivatives Targeting Surface-Exposed Carbonic Anhydrase XII on Cancer Cells.
Article in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 14 citations in OpenAlex.
- PEPAD: A Promising Therapeutic Approach for the Treatment of Murine Melanoma (B16F10-Nex2).Pharmaceuticals (Basel, Switzerland) · 2025Article
- Broadly reactive monoclonal antibodies against beta-lactamases for immunodetection of bacterial resistance to antibiotics.Scientific reports · 2025Article
- Article
- Structural properties of immune complexes formed by viral antigens and specific antibodies shape the inflammatory response of macrophages.Cell & bioscience · 2024Article
- Inhibitory Effect of Human Anti-CA I Autoantibodies and Development of Monoclonal Antibody mAb 2B8 Targeting Carbonic Anhydrase I.Mediators of inflammation · 2024Article
- Carbonic Anhydrase and Biomarker Research: New Insights.International journal of molecular sciences · 2023Article
- Picomolar fluorescent probes for compound affinity determination to carbonic anhydrase IX expressed in live cancer cells.Scientific reports · 2022Article
- Proanthocyanidins fromPlants (Basel, Switzerland) · 2022Article
- The Effect of 1,2,4-Triazole-3-thiol Derivatives Bearing Hydrazone Moiety on Cancer Cell Migration and Growth of Melanoma, Breast, and Pancreatic Cancer Spheroids.Pharmaceuticals (Basel, Switzerland) · 2022Article
- Article
- Carbonic Anhydrase XII is a Clinically Significant, Molecular Tumor-Subtype Specific Therapeutic Target in Glioma with the Potential to Combat Invasion of Brain Tumor Cells.OncoTargets and therapy · 2021Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Monoclonal and recombinant antibodies are widely used for the diagnostics and therapy of cancer. They are generated to interact with cell surface proteins which are usually involved in the development and progression of cancer. Carbonic anhydrase XII (CA XII) contributes to the survival of tumors under hypoxic conditions thus is considered a candidate target for antibody-based therapy. In this study, we have generated a novel collection of monoclonal antibodies (MAbs) against the recombinant extracellular domain of CA XII produced in HEK-293 cells. Eighteen out of 24 MAbs were reactive with cellular CA XII on the surface of live kidney and lung cancer cells as determined by flow cytometry. One MAb 14D6 also inhibited the enzymatic activity of recombinant CA XII as measured by the stopped-flow assay. MAb 14D6 showed the migrastatic effect on human lung carcinoma A549 and renal carcinoma A498 cell lines in a 'wound healing' assay. It did not reduce the growth of multicellular lung and renal cancer spheroids but reduced the cell viability by the ATP Bioluminescence assay. Epitope mapping revealed the surface-exposed amino acid sequence (35-FGPDGENS-42) close to the catalytic center of CA XII recognized by the MAb 14D6. The variable regions of the heavy and light chains of MAb 14D6 were sequenced and their complementarity-determining regions were defined. The obtained variable sequences were used to generate recombinant antibodies in two formats: single-chain fragment variable (scFv) expressed in
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