Cyclosporin A is a cyclic undecapeptide from an extract of soil fungi. It is a powerful immunosupressant with a specific action on T-lymphocytes. It can bind to the cyclophilin and then inhibits calcineurin. Thus, it is widely used in organ transplantation to prevent rejection.
CAT No: 10-101-77
CAS No:59865-13-3
Synonyms/Alias:Cyclosporine; Ciclosporin; Cyclosporin; Cyclosporin A; Cyclosporine A; Neoral; OL 27-400; Restasis; Sandimmun; Sandimmune
Chemical Name:(3S,6S,9S,12R,15S,18S,21S,24S,30S,33S)-30-ethyl-33-[(E,1R,2R)-1-hydroxy-2-methylhex-4-enyl]-1,4,7,10,12,15,19,25,28-nonamethyl-6,9,18,24-tetrakis(2-methylpropyl)-3,21-di(propan-2-yl)-1,4,7,10,13,16,19,22,25,28,31-undecazacyclotritriacontane-2,5,8,11,14,17,20,23,26,29,32-undecone
Cyclosporin A, also known as CsA, is a cyclic undecapeptide that has garnered significant attention in the field of biochemical research due to its unique molecular structure and potent biological activities. Isolated originally from the fungus Tolypocladium inflatum, Cyclosporin A is characterized by its hydrophobic nature and ability to interact with specific intracellular proteins, making it a valuable tool in various scientific studies. Its mechanism centers around the inhibition of calcineurin, a calcium/calmodulin-dependent serine/threonine phosphatase, which underlies many of its downstream effects. Researchers have leveraged its specificity and stability to probe complex cellular pathways, modulate immune responses in vitro, and investigate the intricate balance of signaling cascades within cells. The versatility of Cyclosporin A extends across multiple disciplines, making it indispensable in both basic and applied research environments.
Immunology research: In immunological investigations, Cyclosporin A serves as a critical agent for dissecting T-cell activation and signaling. By binding to cyclophilin, a cytosolic protein, it forms a complex that inhibits calcineurin, thereby preventing the dephosphorylation and nuclear translocation of NF-AT (nuclear factor of activated T-cells). This mechanism enables researchers to modulate immune cell activation in vitro, facilitating the study of cytokine production, cell proliferation, and pathways involved in immune tolerance. The use of CsA in these settings has advanced our understanding of immune regulation and the molecular basis of immune-mediated diseases.
Transplantation biology: Within transplantation research, CsA is extensively utilized to model and study the molecular mechanisms underlying graft acceptance and rejection. By suppressing T-cell mediated responses in cell cultures and animal models, it allows scientists to evaluate the efficacy of novel immunomodulatory strategies and to dissect the cellular interactions that dictate transplant outcomes. Its unique mode of action provides a platform for investigating tolerance induction and the prevention of allograft rejection, contributing to the development of innovative approaches in the field of transplantation science.
Cell signaling studies: The application of Cyclosporin A in cell signaling research has proven invaluable for elucidating calcium-dependent pathways. Its inhibition of calcineurin enables the selective modulation of downstream transcription factors, such as NF-AT, which are pivotal in gene expression regulation. Investigators utilize CsA to dissect the roles of these pathways in diverse cellular processes, including differentiation, apoptosis, and metabolic regulation. By providing a means to selectively inhibit specific signaling events, it facilitates the mapping of complex intracellular networks and the identification of novel therapeutic targets.
Neuroscience research: In neuroscience, CsA has emerged as a powerful tool for studying neuronal signaling, synaptic plasticity, and neuroprotection. The peptide's ability to modulate calcium-dependent phosphatase activity allows researchers to investigate the roles of calcineurin in neuronal development, memory formation, and neurodegenerative processes. Experimental models employing CsA have shed light on the molecular underpinnings of synaptic transmission and the contribution of immune-related pathways to neural health, thereby advancing the field of neurobiology.
Drug discovery and screening: CsA is frequently employed in drug screening assays to evaluate the immunomodulatory potential of new compounds. By serving as a reference inhibitor of calcineurin, it enables the comparative assessment of candidate molecules in terms of efficacy and specificity. High-throughput screening platforms often incorporate CsA to identify small molecules or biologics that modulate similar signaling pathways, expediting the discovery of novel agents for research applications. Its well-characterized mode of action and robust performance in cellular assays make it a benchmark compound in pharmaceutical and biotechnological research.
Molecular biology tool: As a molecular biology reagent, Cyclosporin A is used to manipulate intracellular signaling environments, allowing for precise control over gene expression and cellular responses. Scientists exploit its inhibitory effects to create defined experimental conditions, facilitating the study of gene regulation, protein interactions, and the functional consequences of signaling perturbations. Through its diverse applications, Cyclosporin A continues to enable breakthroughs across immunology, cell biology, neuroscience, and drug discovery, underscoring its enduring value as a research compound.
Cyclosporin A (CyA) is a powerful immunosuppressive agent whose lack of myelotoxicity makes it unique among nonsteroidal drugs currently given for immunosuppression. It has been used with initial success in recipients of kidney, liver, bone marrow and pancreas transplants, and it may also have clinical application in the treatment of autoimmune disorders. In regard to its use in transplant recipients, there are many remaining questions about its mechanism of action, the optimum dose, whether it should be used alone or with other immunosuppressants, whether it can suppress chronic rejection and what its long-term side effects may be. These questions can only be answered by further careful laboratory investigation and controlled clinical trials. Until then, CyA should only be administered in centres experienced in its use.
Laupacis, A., Keown, P. A., Ulan, R. A., McKenzie, N., & Stiller, C. R. (1982). Cyclosporin A: a powerful immunosuppressant. Canadian Medical Association Journal, 126(9), 1041.
CsA, FK-506, and rapamycin are microbial products with potent immunosuppressive properties that result primarily from a selective inhibition of T lymphocyte activation. Although chemically unrelated, CsA and FK-506 affect a similar subset of calcium-associated signaling events involved in the regulation of lymphokine gene expression, activation-driven T-cell death and exocytosis. Rapamycin has structural similarity with FK-506 but suppresses T-cell activation at a different level, mainly through inhibition of proliferation induced by growth-promoting lymphokines. CsA interacts with an abundant 17 kDa protein, termed cyclophilin, that possesses peptidyl-prolyl cis-trans isomerase (PPIase) activity. Additional, minor cyclophilin-like molecules have been identified. Both FK-506 and rapamycin interact with FKBP, a 12 kDa protein, which, although unrelated to cyclophilin, is also abundant and ubiquitous, has a similar enzymatic activity, and is a member of a larger family of FKBPs.
Sigal, N. H., & Dumont, F. J. (1992). Cyclosporin A, FK-506, and rapamycin: pharmacologic probes of lymphocyte signal transduction. Annual review of immunology, 10(1), 519-560.
The site of action of the immunosuppressive drug cyclosporin A in in vitro cytotoxic allograft responses has been localized. General cytotoxic effects of the drug on proliferating T cells became apparent at concentrations of 500-1000 ng/ml, while selective effects were observed at concentrations of 10-100 ng/ml. The selective effects included a blockade of interleukin 2 release from activated T helper cells on the one hand and inhibition of interleukin 1 release from splenic adherent cells on the other. While cyclosporin A did not interfere with the intracellular events required for the activation and subsequent clonal expansion of alloreactive T cells, the lack of interleukin 1 and interleukin 2 induced by cyclosporin A results in an inability of T responder cells to mount cytotoxic allograft responses in vitro.
Bunjes, D., Hardt, C., Röllinghoff, M., & Wagner, H. (1981). Cyclosporin A mediates immunosuppression of primary cytotoxic T cell responses by impairing the release of interleukin 1 and interleukin 2. European journal of immunology, 11(8), 657-661.
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