Proximity ligation assay to study protein-protein interactions of proteins on two different cells
Protein-protein interactions (PPI) by homo-, hetero- or oligo-merization in the cellular environment regulate cellular processes. PPI can be inhibited by antibodies, small molecules or peptides, and this inhibition has therapeutic value. A recently developed method, the proximity ligation assay (PLA...
Publié dans: | BioTechniques. - 1991. - 65(2018), 3 vom: 18. Sept., Seite 149-157 |
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Auteur principal: | |
Autres auteurs: | , , , , |
Format: | Article en ligne |
Langue: | English |
Publié: |
2018
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Accès à la collection: | BioTechniques |
Sujets: | Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't assays bioanalysis flourescence CD2 Antigens CD58 Antigens Histocompatibility Antigens Class II Membrane Proteins |
Résumé: | Protein-protein interactions (PPI) by homo-, hetero- or oligo-merization in the cellular environment regulate cellular processes. PPI can be inhibited by antibodies, small molecules or peptides, and this inhibition has therapeutic value. A recently developed method, the proximity ligation assay (PLA), provides detection of PPI in the cellular environment. However, most applications using this assay are for proteins expressed in the same cell. We employ PLA for the first time to study PPI of cell surface proteins on two different cells. Inhibition of PPI using a peptide inhibitor is also quantified using this assay; PLA is used to detect PPI of CD2 and CD58 between Jurkat cells (T cells) and human fibroblast-like synoviocyte-rheumatoid arthritis cells that are important in the immune response in the autoimmune disease rheumatoid arthritis. This assay provides direct evidence of inhibition of PPI of two proteins on different cell surfaces |
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Description: | Date Completed 31.07.2019 Date Revised 23.10.2019 published: Print Citation Status MEDLINE |
ISSN: | 1940-9818 |
DOI: | 10.2144/btn-2018-0049 |