scholarly journals Decreased KCNE2 Expression Participates in the Development of Cardiac Hypertrophy by Regulation of Calcineurin–NFAT (Nuclear Factor of Activated T Cells) and Mitogen-Activated Protein Kinase Pathways

2017 ◽  
Vol 10 (6) ◽  
Author(s):  
Wenjuan Liu ◽  
Jianxin Deng ◽  
Wenwen Ding ◽  
Gang Wang ◽  
Yuanyuan Shen ◽  
...  
Keyword(s):  
T Cells ◽  
Protein Kinase ◽  
Cardiac Hypertrophy ◽  
Mitogen Activated Protein Kinase ◽  
Nuclear Factor ◽  
Activated T Cells ◽  
Mitogen Activated Protein

scholarly journals Nuclear Factor of Activated T Cells c Is a Target of p38 Mitogen-Activated Protein Kinase in T Cells

2003 ◽  
Vol 23 (18) ◽  
pp. 6442-6454 ◽  
Author(s):  
Chia-Cheng Wu ◽  
Shu-Ching Hsu ◽  
Hsiu-ming Shih ◽  
Ming-Zong Lai
Keyword(s):  
T Cells ◽  
Protein Kinase ◽  
P38 Mapk ◽  
T Cell Activation ◽  
Cell Activation ◽  
Mitogen Activated Protein Kinase ◽  
Nuclear Factor ◽  
Creb Binding Protein ◽  
Activated T Cells ◽  
Mitogen Activated Protein

ABSTRACT p38 mitogen activated protein kinase (MAPK) is essential for T-cell activation. Here we demonstrated that nuclear factor of activated T cells (NFAT) is a direct target of p38 MAPK. Inhibition of p38 MAPK led to selective inactivation of NFAT in T cells. We further linked a strict requirement of p38 MAPK to activation of NFATc. A stimulatory effect of p38 MAPK on at least four other stages of NFATc activation was found. First, the p38 MAPK cascade activated the NFATc promoter and induced the transcription of NFATc mRNA. Second, p38 MAPK mildly increased the mRNA stability of NFATc. Third, p38 MAPK enhanced the translation of NFATc mRNA. Fourth, p38 MAPK promoted the interaction of NFATc with the coactivator CREB-binding protein. In contrast, p38 MAPK moderately enhanced the expulsion of NFATc from the nucleus in T cells. Therefore, p38 MAPK has opposite effects on different stages of NFATc activation. All together, the overall effect of p38 MAPK on NFATc in T cells is clear activation.

scholarly journals Diketoacetonylphenalenone, Derived from Hawaiian Volcanic Soil-Associated Fungus Penicillium herquei FT729, Regulates T Cell Activation via Nuclear Factor-κB and Mitogen-Activated Protein Kinase Pathway

Molecules ◽  
2020 ◽  
Vol 25 (22) ◽  
pp. 5374
Author(s):  
Hyun-Su Lee ◽  
Jae Sik Yu ◽  
Ki Hyun Kim ◽  
Gil-Saeng Jeong
Keyword(s):  
T Cells ◽  
T Cell ◽  
Protein Kinase ◽  
T Cell Activation ◽  
Cell Activation ◽  
Cell Activity ◽  
Mitogen Activated Protein Kinase ◽  
Volcanic Soil ◽  
Activated T Cells ◽  
Mitogen Activated Protein

In immunological responses, controlling excessive T cell activity is critical for immunological homeostasis maintenance. Diketoacetonylphenalenone, derived from Hawaiian volcanic soil-associated fungus Penicillium herquei FT729, possesses moderate anti-inflammatory activity in RAW 264.7 cells but its immunosuppressive effect on T cell activation is unknown. In the present study, diketoacetonylphenalenone (up to 40 μM) did not show cytotoxicity in T cells. Western blot analysis showed treatment with diketoacetonylphenalenone did not alter the expression of anti-apoptotic proteins. Pretreatment with diketoacetonylphenalenone suppressed the interleukin-2 production in activated T cells induced by T cell receptor-mediated stimulation and PMA/A23187. The CFSE-proliferation assay revealed the inhibitory effect of diketoacetonylphenalenone on the proliferation of T cells. The expression of surface molecules on activated T cells was also reduced. We discovered the suppression of the TAK1-IKKα-NF-κB pathway by pretreatment with diketoacetonylphenalenone abrogated mitogen-activated protein kinase (MAPK) signaling in activated T cells. These results suggest that diketoacetonylphenalenone effectively downregulates T cell activity via the MAPK pathway and provides insight into the therapeutic potential of immunosuppressive reagents.

scholarly journals Activation of the mitogen-activated protein kinase pathway induces transcription of the PAC-1 phosphatase gene.

1996 ◽  
Vol 16 (6) ◽  
pp. 2913-2921 ◽  
Author(s):  
R J Grumont ◽  
J E Rasko ◽  
A Strasser ◽  
S Gerondakis
Keyword(s):  
T Cells ◽  
Protein Kinase ◽  
Phorbol Myristate Acetate ◽  
Transcription Initiation ◽  
Mitogen Activated Protein Kinase ◽  
Mrna Levels ◽  
Myristate Acetate ◽  
Activated T Cells ◽  
E Box ◽  
Mitogen Activated Protein

PAC-1, an early-response gene originally identified in activated T cells, encodes a dual-specificity mitogen-activated protein kinase phosphatase. Here we report on the regulation of PAC-1 expression in murine hemopoietic cells. PAC-1 mRNA levels rapidly increase in mitogen-stimulated lymphocytes, with the induced expression being transient in B cells but sustained in activated T cells. Transfection analysis of murine PAC-1 promoter-reporter constructs established that in T cells, sequences necessary for basal and induced transcription reside within a 200-bp region located immediately upstream of the transcription initiation sites. Basal transcription is regulated in part by an E-box element that binds a 53-kDa protein. PAC-1 transcription induced by phorbol myristate acetate stimulation and the expression of the v-ras or v-raf oncogene is mediated via the E-box motif and an AP-2-related site and coincides with increased binding activity of the constitutive 53-kDa E-box-binding protein and induced binding of AP-2. The ability of an interfering ERK-2 mutant to block phorbol myristate acetate and v-ras-dependent PAC-1 transcription indicates that mitogen-activated protein kinase activation is necessary for these stimuli to induce transcription of the PAC-1 gene in T cells.

scholarly journals Protein Kinase Cζ Phosphorylates Nuclear Factor of Activated T Cells and Regulates Its Transactivating Activity

2002 ◽  
Vol 277 (30) ◽  
pp. 27073-27080 ◽  
Author(s):  
Belén San-Antonio ◽  
Miguel A. Íñiguez ◽  
Manuel Fresno
Keyword(s):  
T Cells ◽  
Protein Kinase ◽  
Nuclear Factor ◽  
Activated T Cells

Modification of ischemia/reperfusion induced infarct size by ischemic preconditioning in hypertrophied hearts

2021 ◽  
Vol 99 (2) ◽  
pp. 218-223
Author(s):  
Mohamad Nusier ◽  
Mohammad Alqudah ◽  
Vijayan Elimban ◽  
Naranjan S. Dhalla
Keyword(s):  
Protein Kinase ◽  
Cardiac Hypertrophy ◽  
Infarct Size ◽  
P38 Mapk ◽  
Ischemic Preconditioning ◽  
Creatine Phosphokinase ◽  
Ischemia Reperfusion ◽  
Mitogen Activated Protein Kinase ◽  
Normal Heart ◽  
Mitogen Activated Protein

This study examined the effects of ischemic preconditioning (IP) on the ischemia/reperfusion (I/R) induced injury in normal and hypertrophied hearts. Cardiac hypertrophy in rabbits was induced by L-thyroxine (0.5 mg/kg/day for 16 days). Hearts with or without IP (3 cycles of 5 min ischemia and 10 min reperfusion) were subjected to I/R (60 min ischemia followed by 60 min reperfusion). IP reduced the I/R-induced infarct size from 68% to 24% and 57% to 33% in the normal and hypertrophied hearts, respectively. Leakage of creatine phosphokinase in the perfusate from the hypertrophied hearts due to I/R was markedly less than that form the normal hearts; IP prevented these changes. Although IP augmented the increase in phosphorylated p38-mitogen-activated protein kinase (p38-MAPK) content due to I/R, this effect was less in the hypertrophied than in the normal heart. These results suggest that reduced cardioprotection by IP of the I/R-induced injury in hypertrophied hearts may be due to reduced activation of p38-MAPK in comparison with normal hearts.

Sign in / Sign up

Export Citation Format

Share Document