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• W1486128119 endingPage "599" @default.
• W1486128119 startingPage "589" @default.
• W1486128119 abstract "Histone deacetylase inhibitor n-butyrate induced proliferative unresponsiveness in antigen-stimulated murine CD4(+) T cells. T cells anergized by n-butyrate demonstrated reduced interleukin-2 (IL-2) secretion and decreased activating protein 1 (AP-1) activity upon restimulation. Mechanistic studies determined that the cyclin-dependent kinase (cdk) inhibitor p21(Cip1) was up-regulated in the anergic CD4(+) T cells. p21(Cip1) is known to inhibit the cell cycle through its interaction with cdk, proliferating cell nuclear antigen (PCNA) or c-Jun N-terminal kinase (JNK). p21(Cip1) did not preferentially associate with PCNA or cdk in anergic T helper type 1 (Th1) cells. Instead, among the three interaction partners, p21(Cip1) was found to interact with phospho-JNK and phospho-c-jun selectively in the anergic CD4(+) T cells. The activity of c-jun and downstream transcription factor AP-1 were suppressed in the anergic Th1 cells. In contrast, p21(Cip1) and the two phospho-proteins were never detected concurrently in the control CD4(+) T cells. The n-butyrate-induced p21(Cip1)-mediated inhibition of JNK and c-jun represents a novel potential mechanism by which proliferative unresponsiveness was maintained in CD4(+) T cells." @default.
• W1486128119 created "2016-06-24" @default.
• W1486128119 creator A5057277608 @default.
• W1486128119 creator A5059882916 @default.
• W1486128119 date "2009-09-11" @default.
• W1486128119 modified "2023-09-25" @default.
• W1486128119 title "p21Cip1 up-regulated during histone deacetylase inhibitor-induced CD4+ T-cell anergy selectively associates with mitogen-activated protein kinases" @default.
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• W1486128119 doi "https://doi.org/10.1111/j.1365-2567.2009.03161.x" @default.
• W1486128119 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2842505" @default.
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