Functional and phenotypic characterization of monoclonal antibodies to bovine L-selectin
- Author
- Y Wang, Max Paape (UGent) , L Leino, Anthony Capuco (UGent) and H Narva
- Organization
- Abstract
- Objective-To characterize 2 bovine neutrophil monoclonal antibodies (MAB) as to effects on bovine neutrophil function and their binding antigens on the cell surface of bovine neutrophils. Animals-16 healthy, lactating Holstein cattle, 1 calf with leukocyte adhesion deficiency, and 1 age-matched control calf, 2 healthy ewes, and 2 healthy human beings as neutrophil sources. Procedure-Neutrophil chemotactic and respiratory burst activities and calcium influx, and binding properties of the 2 MAB were determined. Molecular mass of corresponding cell surface antigens also was determined, as was binding of human L-selectin MAB DREG56 to molecules recognized by MAB 11G10 and 2G8 on the surface of bovine neutrophils. Results-MAB 11G10 and 2G8 inhibited chemotactic activity of bovine neutrophils, up-regulated amplitude of native chemiluminescence, and shortened the time to reach maximal chemiluminescence induced by serum-opsonized zymosan. Crosslinking both MAB with a second antibody induced rapid increase in intracellular free calcium concentration. Binding density of MAB 11G10 and 2G8 to bovine neutrophils treated with trypsin was increased (P < 0.05), compared with that of untreated neutrophils. Neutrophils treated with phosphatidylinositol-specific phospholipase C had decreased (P < 0.05) binding density of MAB 11G10 and 2G8. Binding of the various MAB to neutrophils from calves with bovine leukocyte adhesion deficiency was lower (P < 0.05) than binding to neutrophils from healthy calves. Expression of antigens recognized by the aforementioned MAB on the surface of bovine neutrophils was decreased (P < 0.05) within 10 minutes. Conclusion-MAB 11G10 and 2G8 recognized L-selectin molecules on bovine neutrophil membrane. L-Selectin (CD62L) is involved in low-affinity adhesion reactions between leukocytes and L-selectin ligand on postcapillary venular endothelial cells.
- Keywords
- CYTOPLASMIC DOMAIN, NODE HOMING RECEPTOR, HUMAN NEUTROPHILS, ADHESION, EXPRESSION, INTEGRINS, MIGRATION, PROTEINS, INVIVO, MAC-1
Citation
Please use this url to cite or link to this publication: http://hdl.handle.net/1854/LU-820961
- MLA
- Wang, Y., et al. “Functional and Phenotypic Characterization of Monoclonal Antibodies to Bovine L-Selectin.” AMERICAN JOURNAL OF VETERINARY RESEARCH, vol. 58, no. 12, 1997, pp. 1392–401.
- APA
- Wang, Y., Paape, M., Leino, L., Capuco, A., & Narva, H. (1997). Functional and phenotypic characterization of monoclonal antibodies to bovine L-selectin. AMERICAN JOURNAL OF VETERINARY RESEARCH, 58(12), 1392–1401.
- Chicago author-date
- Wang, Y, Max Paape, L Leino, Anthony Capuco, and H Narva. 1997. “Functional and Phenotypic Characterization of Monoclonal Antibodies to Bovine L-Selectin.” AMERICAN JOURNAL OF VETERINARY RESEARCH 58 (12): 1392–1401.
- Chicago author-date (all authors)
- Wang, Y, Max Paape, L Leino, Anthony Capuco, and H Narva. 1997. “Functional and Phenotypic Characterization of Monoclonal Antibodies to Bovine L-Selectin.” AMERICAN JOURNAL OF VETERINARY RESEARCH 58 (12): 1392–1401.
- Vancouver
- 1.Wang Y, Paape M, Leino L, Capuco A, Narva H. Functional and phenotypic characterization of monoclonal antibodies to bovine L-selectin. AMERICAN JOURNAL OF VETERINARY RESEARCH. 1997;58(12):1392–401.
- IEEE
- [1]Y. Wang, M. Paape, L. Leino, A. Capuco, and H. Narva, “Functional and phenotypic characterization of monoclonal antibodies to bovine L-selectin,” AMERICAN JOURNAL OF VETERINARY RESEARCH, vol. 58, no. 12, pp. 1392–1401, 1997.
@article{820961,
abstract = {{Objective-To characterize 2 bovine neutrophil monoclonal antibodies (MAB) as to effects on bovine neutrophil function and their binding antigens on the cell surface of bovine neutrophils.
Animals-16 healthy, lactating Holstein cattle, 1 calf with leukocyte adhesion deficiency, and 1 age-matched control calf, 2 healthy ewes, and 2 healthy human beings as neutrophil sources.
Procedure-Neutrophil chemotactic and respiratory burst activities and calcium influx, and binding properties of the 2 MAB were determined. Molecular mass of corresponding cell surface antigens also was determined, as was binding of human L-selectin MAB DREG56 to molecules recognized by MAB 11G10 and 2G8 on the surface of bovine neutrophils.
Results-MAB 11G10 and 2G8 inhibited chemotactic activity of bovine neutrophils, up-regulated amplitude of native chemiluminescence, and shortened the time to reach maximal chemiluminescence induced by serum-opsonized zymosan. Crosslinking both MAB with a second antibody induced rapid increase in intracellular free calcium concentration. Binding density of MAB 11G10 and 2G8 to bovine neutrophils treated with trypsin was increased (P < 0.05), compared with that of untreated neutrophils. Neutrophils treated with phosphatidylinositol-specific phospholipase C had decreased (P < 0.05) binding density of MAB 11G10 and 2G8. Binding of the various MAB to neutrophils from calves with bovine leukocyte adhesion deficiency was lower (P < 0.05) than binding to neutrophils from healthy calves. Expression of antigens recognized by the aforementioned MAB on the surface of bovine neutrophils was decreased (P < 0.05) within 10 minutes.
Conclusion-MAB 11G10 and 2G8 recognized L-selectin molecules on bovine neutrophil membrane. L-Selectin (CD62L) is involved in low-affinity adhesion reactions between leukocytes and L-selectin ligand on postcapillary venular endothelial cells.}},
author = {{Wang, Y and Paape, Max and Leino, L and Capuco, Anthony and Narva, H}},
issn = {{0002-9645}},
journal = {{AMERICAN JOURNAL OF VETERINARY RESEARCH}},
keywords = {{CYTOPLASMIC DOMAIN,NODE HOMING RECEPTOR,HUMAN NEUTROPHILS,ADHESION,EXPRESSION,INTEGRINS,MIGRATION,PROTEINS,INVIVO,MAC-1}},
language = {{eng}},
number = {{12}},
pages = {{1392--1401}},
title = {{Functional and phenotypic characterization of monoclonal antibodies to bovine L-selectin}},
volume = {{58}},
year = {{1997}},
}