Identification of a peptide fragment of DSCR1 that competitively inhibits calcineurin activity in vitro and in vivo
Autor: | Garrett Greenan, Tom Ellenberger, Frank McKeon, Betty Liwah Chan |
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Rok vydání: | 2005 |
Předmět: |
T cell
Calcineurin Inhibitors Phosphatase Active Transport Cell Nucleus Muscle Proteins Biology Protein Structure Secondary Cell Line Organophosphorus Compounds In vivo Cricetinae Protein Interaction Mapping medicine Animals Humans Transcription factor Aniline Compounds Binding Sites Multidisciplinary NFATC Transcription Factors Calcineurin Calcipressin Intracellular Signaling Peptides and Proteins Nuclear Proteins NFAT Exons Biological Sciences Peptide Fragments Cell biology DNA-Binding Proteins Kinetics medicine.anatomical_structure Biochemistry Nuclear localization sequence Protein Binding Transcription Factors |
Zdroj: | Proceedings of the National Academy of Sciences. 102:13075-13080 |
ISSN: | 1091-6490 0027-8424 |
DOI: | 10.1073/pnas.0503846102 |
Popis: | Calcineurin phosphatase activity regulates the nuclear localization of the nuclear factor of activated T cells (NFAT) family of transcription factors during immune challenge. Calcineurin inhibitors, such as the cyclosporin A–cyclophilin A and FK506–FKBP12 complexes, regulate this enzymatic activity noncompetitively by binding at a site distinct from the enzyme active site. A family of endogenous protein inhibitors of calcineurin was recently identified and shown to block calcineurin-mediated NFAT nuclear localization and transcriptional activation. One such inhibitor, Down Syndrome Critical Region 1 (DSCR1), functions in T cell activation, cardiac hypertrophy, and angiogenesis. We have identified a small region of DSCR1 that is a potent inhibitor of calcineurin activity in vitro and in vivo . |
Databáze: | OpenAIRE |
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