دورية أكاديمية

VT68.2: An Antibody to Chondroitin Sulfate Proteoglycan 4 (CSPG4) Displays Reactivity against a Tumor-Associated Carbohydrate Antigen

التفاصيل البيبلوغرافية
العنوان: VT68.2: An Antibody to Chondroitin Sulfate Proteoglycan 4 (CSPG4) Displays Reactivity against a Tumor-Associated Carbohydrate Antigen
المؤلفون: Bernice Nounamo, Fariba Jousheghany, Eric Robb Siegel, Steven R. Post, Thomas Kelly, Soldano Ferrone, Thomas Kieber-Emmons, Behjatolah Monzavi-Karbassi
المصدر: International Journal of Molecular Sciences, Vol 24, Iss 3, p 2506 (2023)
بيانات النشر: MDPI AG, 2023.
سنة النشر: 2023
المجموعة: LCC:Biology (General)
LCC:Chemistry
مصطلحات موضوعية: CSPG4, TACAs, breast cancer, carbohydrate-mimicking peptide, Biology (General), QH301-705.5, Chemistry, QD1-999
الوصف: The anti-CSPG4 monoclonal antibodies (mAbs) have shown anti-tumor activity and therapeutic potential for treating breast cancer. In addition, CSPG4 is a dominant tumor-associated antigen that is also involved in normal-tissue development in humans. Therefore, the potential for off-tumor activity remains a serious concern when targeting CSPG4 therapeutically. Previous work suggested that glycans contribute to the binding of specific anti-CSPG4 antibodies to tumor cells, but the specificity and importance of this contribution are unknown. In this study, the reactivity of anti-CSPG4 mAbs was characterized with a peptide mimetic of carbohydrate antigens expressed in breast cancer. ELISA, flow cytometry, and microarray assays were used to screen mAbs for their ability to bind to carbohydrate-mimicking peptides (CMPs), cancer cells, and glycans. The mAb VT68.2 displayed a distinctly strong binding to a CMP (P10s) and bound to triple-negative breast cancer cells. In addition, VT68.2 showed a higher affinity for N-linked glycans that contain terminal fucose and fucosylated lactosamines. The functional assays demonstrated that VT68.2 inhibited cancer cell migration. These results define the glycoform reactivity of an anti-CSPG4 antibody and may lead to the development of less toxic therapeutic approaches that target tumor-specific glyco-peptides.
نوع الوثيقة: article
وصف الملف: electronic resource
اللغة: English
تدمد: 24032506
1422-0067
1661-6596
Relation: https://www.mdpi.com/1422-0067/24/3/2506; https://doaj.org/toc/1661-6596; https://doaj.org/toc/1422-0067
DOI: 10.3390/ijms24032506
URL الوصول: https://doaj.org/article/c18a9b4548914dad8796d2fc841c5fd0
رقم الأكسشن: edsdoj.18a9b4548914dad8796d2fc841c5fd0
قاعدة البيانات: Directory of Open Access Journals
الوصف
تدمد:24032506
14220067
16616596
DOI:10.3390/ijms24032506