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Cis-Reporting System Monitors Intracellular Calcium Mobilization


New PathDetect reporting system for studying NFAT activation

Li Xu Matthew Hsu Mary Buchanan Chao-Feng Zheng
Stratagene

Stratagenes new PathDetect cis-reporter plasmid, the pNFAT-Luc reporter plasmid, is designed for studying the activation of the nuclear factor of activated T-cell (NFAT) transcription factors. These interesting proteins, which play an essential role in inducible gene expression during immune responses, are activated by stimuli that increase free calcium levels in the cytoplasm. NFAT transcription factors are studied intensively as potential targets for newer and safer immunosuppressive drugs and for assessing cellular signal transduction pathways that are responsive to calcium mobilization.

Proteins that comprise the family of transcription factors known as nuclear factor of activated T cells play an essential role in inducible gene expression during immune responses. Although first identified in T cells, these proteins have also been detected in many other tissues and cell types. NFAT transcription factors are regulated by calcineurin, a calcium/calmodulin-dependent phosphatase. NFAT proteins, as substrates for calcineurin, mediate the effects of cyclosporin A (CsA) and FK506, two immunosuppresive drugs that revolutionized transplant surgery in 1983.1

Members of the NFAT family are divided according to primary structure homology into four subgroups: NFAT1 (1A, 1B, and 1C), NFAT2 (NFATc.a and NFATc.b), NFAT3, and NFAT4 (4a, 4b, 4c, and NFATx). NFAT proteins vary in size from NFAT4a (708 amino acid residues) to NFATx (1075 amino acid residues). Two major regions of homology exist among these subgroups: the DNA-binding domain (dbd) and the NFAT homology region (NHR). The dbd is positioned within amino acid residues ~400 and ~700 in the known isoforms of NFAT and shows some similarity to the dbd o
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