Characterization of a murine monoclonal antibody specific for swine beta1 integrin
| Autor: | Jean-François Bouhours, Marie-Jeanne Loirat, Oominique Blanchard, Jeanne Naulet, Béatrice Charreau, Karen Thibaudeau, Jean-Paul Soulillou, Christelle Richard |
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| Rok vydání: | 1998 |
| Předmět: |
Blood Platelets
Graft Rejection Integrins Receptors Collagen medicine.drug_class Swine Immunology Integrin Transplantation Heterologous Platelet Membrane Glycoproteins Biology Platelet membrane glycoprotein Monoclonal antibody CD49b Mice Affinity chromatography Antigen Species Specificity Antibody Specificity medicine Animals Humans Amino Acid Sequence Transplantation Hybridomas Sequence Homology Amino Acid Integrin beta1 Antibodies Monoclonal Molecular biology Immunohistochemistry biology.protein Endothelium Vascular Antibody Clone (B-cell biology) |
| Zdroj: | Europe PubMed Central |
| ISSN: | 0908-665X |
| Popis: | Murine monoclonal antibodies were raised against porcine platelets in order to provide tools for investigating interactions of human blood cells and natural antibodies with porcine tissues. Hybridomas were screened by cellular ELISA on porcine platelets and endothelial cells. Positive clones were tested by flow cytometry for reactivity with isolated endothelial cells. One clone, NaM160-1A3, produced an antibody that stained porcine but not human endothelial cells and lymphocytes. The antibody bound to a 116 kDa glycoprotein on Western blot of both platelets and endothelial cells. The antigen was purified from a platelet lysate by affinity chromatography, first on a ConA column and then on a column presenting the immobilized NaM160-1A3 antibody. Two glycoproteins were obtained: one (116 kDa) was recognized by the antibody and one (150 kDa) was not. The 116 kDa protein had an internal decapeptide identical with human beta 1 integrin, and the 150 kDa protein had an internal amino acid sequence belonging to porcine alpha 2 integrin. Therefore, the NaM160-1A3 antibody was directed against porcine beta 1 integrin and allowed the purification of the complex alpha 2 beta 1, also termed Very Late Antigen 2 (VLA-2). It did not recognize human beta 1 integrin. |
| Databáze: | OpenAIRE |
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