Targeting Tn-Antigen-Positive Human Tumors with a Recombinant Human Macrophage Galactose C-Type Lectin
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| Názov: | Targeting Tn-Antigen-Positive Human Tumors with a Recombinant Human Macrophage Galactose C-Type Lectin |
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| Autori: | Bulteau, François, Thépaut, Michel, Henry, Maxime, Hurbin, Amandine, Vanwonterghem, Laetitia, Vivès, Corinne, Le Roy, Aline, Ebel, Christine, Renaudet, Olivier, Fieschi, Franck, Coll, Jean-Luc |
| Prispievatelia: | Hurbin, Amandine, Institut de biologie structurale (IBS - UMR 5075), Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes (UGA), Institute for Advanced Biosciences / Institut pour l'Avancée des Biosciences (Grenoble) (IAB), Centre Hospitalier Universitaire CHU Grenoble (CHUGA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Etablissement français du sang - Auvergne-Rhône-Alpes (EFS)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes (UGA), Département de Chimie Moléculaire (DCM), Institut de Chimie - CNRS Chimie (INC-CNRS)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes (UGA), ANR-11-INBS-0006,FLI,France Life Imaging(2011) |
| Zdroj: | Molecular Pharmaceutics. 19:235-245 |
| Informácie o vydavateľovi: | American Chemical Society (ACS), 2021. |
| Rok vydania: | 2021 |
| Predmety: | 0301 basic medicine, Carbohydrate, MESH: Microscopy, [SDV.BBM.BS] Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM], MESH: HT29 Cells, Nude, Mice, Nude, MESH: Flow Cytometry, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, MESH: Recombinant Proteins, Mice, 03 medical and health sciences, MESH: Lectins, Spheroids, Cellular, Tn antigen, cancer, Animals, Humans, MESH: Animals, Antigens, Tumor-Associated, Carbohydrate, Lectins, C-Type, MESH: Mice, 0303 health sciences, MESH: Humans, Microscopy, Confocal, C-Type, Molecular Biology/Structural Biology [q-bio.BM], Tumor-Associated, Surface Plasmon Resonance, Flow Cytometry, Recombinant Proteins, MESH: Surface Plasmon Resonance, 3. Good health, C-type lectin, MESH: Spheroids, A549 Cells, Confocal, MESH: Antigens, Female, Cellular, MESH: A549 Cells, MESH: Female, HT29 Cells, MESH: Neoplasm Transplantation, Neoplasm Transplantation |
| Popis: | Alterations in glycosylation cause the emergence of tumor-associated carbohydrate antigens (TACAs) during tumorigenesis. Truncation of O-glycans reveals the Thomsen nouveau (Tn) antigen, an N-acetylgalactosamine (GalNAc) frequently attached to serine or threonine amino acids, that is accessible on the surface of cancer cells but not on healthy cells. Interestingly, GalNac can be recognized by macrophage galactose lectin (MGL), a type C lectin receptor expressed in immune cells. In this study, recombinant MGL fragments were tested in vitro for their cancer cell-targeting efficiency by flow cytometry and confocal microscopy and in vivo after administration of fluorescent MGL to tumor-bearing mice. Our results demonstrate the ability of MGL to target Tn-positive human tumors without inducing toxicity. This outcome makes MGL, a fragment of a normal human protein, the first vector candidate for in vivo diagnosis and imaging of human tumors and, possibly, for therapeutic applications. |
| Druh dokumentu: | Article |
| Popis súboru: | application/pdf |
| Jazyk: | English |
| ISSN: | 1543-8392 1543-8384 |
| DOI: | 10.1021/acs.molpharmaceut.1c00744 |
| Prístupová URL adresa: | https://pubmed.ncbi.nlm.nih.gov/34927439 https://hal.science/hal-03715094v1 https://hal.science/hal-03715094v1/document https://doi.org/10.1021/acs.molpharmaceut.1c00744 |
| Rights: | STM Policy #29 |
| Prístupové číslo: | edsair.doi.dedup.....4d8115bd4c42ccb6ab3a6a3fa5e5ab90 |
| Databáza: | OpenAIRE |
Nájsť tento článok vo Web of Science | Abstrakt: | Alterations in glycosylation cause the emergence of tumor-associated carbohydrate antigens (TACAs) during tumorigenesis. Truncation of O-glycans reveals the Thomsen nouveau (Tn) antigen, an N-acetylgalactosamine (GalNAc) frequently attached to serine or threonine amino acids, that is accessible on the surface of cancer cells but not on healthy cells. Interestingly, GalNac can be recognized by macrophage galactose lectin (MGL), a type C lectin receptor expressed in immune cells. In this study, recombinant MGL fragments were tested in vitro for their cancer cell-targeting efficiency by flow cytometry and confocal microscopy and in vivo after administration of fluorescent MGL to tumor-bearing mice. Our results demonstrate the ability of MGL to target Tn-positive human tumors without inducing toxicity. This outcome makes MGL, a fragment of a normal human protein, the first vector candidate for in vivo diagnosis and imaging of human tumors and, possibly, for therapeutic applications. |
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| ISSN: | 15438392 15438384 |
| DOI: | 10.1021/acs.molpharmaceut.1c00744 |