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The interaction between Cyclophilin A (CypA, also known as peptidyl-prolyl cis-trans isomerase A or PPIA) and Basigin (CD147) is a critical protein–protein interaction central to multiple human pathophysiologies. CypA, a highly conserved intracellular enzyme with chaperone and folding functions, can be secreted under inflammatory conditions, at which point it binds to its receptor CD147 (Basigin) on the cell surface. This interaction triggers various downstream effects, including immune cell recruitment, matrix metalloproteinase induction (contributing to tissue remodeling and metastasis), and facilitation of viral infectivity—notably, HIV-1 and coronaviruses. The interaction is implicated in cardiovascular disease, cancer, inflammatory disorders, and neurodegeneration. The interaction is also a validated therapeutic target, with cyclosporin A and related molecules under investigation for blocking the interaction to treat infection, inflammation, or cancer[4][5][7].
Immunosuppression by inhibiting the CypA–calcineurin interaction (Cyclosporin A)\nBlockade of the CypA–CD147 interaction to reduce viral infection, inflammation, and cancer metastasis\nModulation of the protein folding and chaperone activities
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See how Gosset can support your research on Cyclophilin A interaction with Basigin (There is no standard abbreviation for this interaction per se. For the molecules involved, Cyclophilin A is abbreviated as CypA or PPIA, and Basigin is also known as CD147.).