Some new aspects of molecular mechanisms of cyclosporin A effect on immune response

APMIS : Acta Pathologica, Microbiologica, Et Immunologica Scandinavica
V P Zav'yalovT Korpela

Abstract

A few protein targets were found to display a specific high-affinity interaction with the immunosuppressant cyclosporin A (CsA): cytosolic cyclophilins (CyP)A, B, C, D, E containing from 122 to 174 amino acid residues in a polypeptide chain, and secreted forms of CyP; CyP-40, 40-kDa CsA-binding polypeptide complexed with steroid receptor (SR); CyP-related 150-kDa receptor of natural killer (NK) cells; interleukin 8 (IL-8); actin; a family of molecular chaperones hsp70 and P-glycoprotein (P-GP). All CyPs possess peptidyl-prolyl cis-trans isomerase activity (PPIase) and may serve as ATP-independent molecular chaperone proteins. The CsA-CyP complexes are specific inhibitors of Ca(2+)-and calmodulin-dependent protein phosphatase calcineurin (CaN). The inhibition of CaN blocks the activation of genes of IL-2, IL-2R, IL-4, etc. in T cells. In addition, immunosuppressive and/or antiinflammatory activity of CsA can be executed via CyP-40 and hsp 70 complexed with SR, and following the interaction with CyP-related receptor of NK and with IL-8. CsA binding to CyPC, P-GP and actin may throw light on the biochemical events leading to nephrotoxicity and graft vessel disease, two major side effects produced by CsA. The discovery of the inter...Continue Reading

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Citations

Dec 21, 2002·International Journal of Dermatology·Pasquale PatroneGiuseppe Stinco
Apr 21, 2010·APMIS : Acta Pathologica, Microbiologica, Et Immunologica Scandinavica·Song-Dong ZhangQun Wei
Oct 28, 2016·European Journal of Pharmaceutical Sciences : Official Journal of the European Federation for Pharmaceutical Sciences·Hiroki SuzukiSatomi Onoue
Mar 10, 2011·New Directions for Child and Adolescent Development·Raymond A MarKatrina Fong
Oct 4, 2000·Physiological Reviews·F Rusnak, P Mertz

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