scholarly journals Beta-Like Importins Mediate the Nuclear Translocation of Mitogen-Activated Protein Kinases

2013 ◽  
Vol 34 (2) ◽  
pp. 259-270 ◽  
Author(s):  
E. Zehorai ◽  
R. Seger
Keyword(s):  
Protein Kinases ◽  
Nuclear Translocation ◽  
Mitogen Activated Protein Kinases ◽  
Mitogen Activated Protein

scholarly journals Interleukin-8 Secretion from Mycobacterium tuberculosis-Infected Monocytes Is Regulated by Protein Tyrosine Kinases but Not by ERK1/2 or p38 Mitogen-Activated Protein Kinases

2002 ◽  
Vol 70 (8) ◽  
pp. 4743-4746 ◽  
Author(s):  
Clara Ameixa ◽  
Jon S. Friedland
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Protein Kinases ◽  
Tyrosine Kinases ◽  
Nuclear Translocation ◽  
Interleukin 8 ◽  
Protein Tyrosine Kinases ◽  
Human Monocytes ◽  
Mitogen Activated Protein Kinases ◽  
Mitogen Activated Protein ◽  
Posttranscriptional Processing

ABSTRACT Mycobacterium tuberculosis upregulates NF-κB binding and interleukin-8 (IL-8) gene expression and secretion in primary human monocytes. Inhibition of tyrosine protein kinases but not of ERK1/2 or p38 mitogen-activated protein kinases downregulates tuberculosis-induced IL-8 secretion. The inhibitor genistein decreased NF-κB nuclear translocation and IL-8 gene transcription in addition to acting on posttranscriptional processing.

Mitogen-Activated Protein Kinases Are Differently Activated in Early Hypertrophic Response to Acute Pressure Overload in Rat Myocardium

Hypertension ◽  
2000 ◽  
Vol 36 (suppl_1) ◽  
pp. 703-703
Author(s):  
Wilson Nadruz Junior ◽  
Mario A Saad
Keyword(s):  
Protein Kinases ◽  
Mammalian Cells ◽  
Time Course ◽  
Nuclear Translocation ◽  
Pressure Overload ◽  
Rat Myocardium ◽  
Mitogen Activated Protein Kinases ◽  
Hypertrophic Response ◽  
Mitogen Activated Protein

P55 Mitogen-activated protein kinases (MAPKs) have been reported as important signaling molecules mediating cardiomyocyte hypertrophic response to various stimuli. Four subfamilies of MAPKs have been described in mammalian cells: c-jun NH2 terminal kinases (JNKs), p38-MAPKs (p38), extracellular response kinases (ERKs) and big MAP-kinase (BMK). Our objective was to study the activation of these kinases in the early phases of hypertrophic response, which is currently obscure. Transverse aorta constriction (TAC) was performed in male Wistar rats (160-200g) and left ventricles were studied up to 3 h following the surgery. To study the activation of ERKs, JNKs and p38, heart homogenates were separated into cytosolic (C) and nuclear (N) fractions and their kinase activities were determined by Western Blot using anti p-ERK, p-JNK and p-p38 antibodies. The membranes were then stripped and blotted with anti-ERK, anti-JNK and anti-p38 to determine the protein contents. The amount of BMK was studied in total homogenates using anti-BMK antibody and its activity was studied by measuring its in vitro autophosphorylation. ERK1/2 were transiently activated in both subcellular fractions, reaching a maximum 30 min after TAC (ERK1 - 236% in C and 196% in N; ERK2 - 280% in C and 248% in N) and returning toward basal levels after 1 h. p38 showed a sustained increase in its activity only in C (to 259%) but not in N after 1 h of TAC. JNKs showed a biphasic response with an early and major increase in their activities after 10 min (to 313% for JNK1 and to 288% for JNK2 in C) and a second and minor one following 3 h of TAC. In parallel, TAC induced a significant nuclear translocation of JNK1. The total amount of BMK remained stable during the studied period. We observed a progressive increase in its kinase activity which was directly related to TAC time course (45% in 10 min; 159% in 1 h and 173 % in 2h). These results indicate that pressure overload induces an early activation of the four subfamilies of MAPKs. Differences in their time course activation suggest that they might play different roles in the early hypertrophic response in adult rat myocardium.

scholarly journals Targeted Deletion of the Integrin β4 Signaling Domain Suppresses Laminin-5-Dependent Nuclear Entry of Mitogen-Activated Protein Kinases and NF-κB, Causing Defects in Epidermal Growth and Migration

2005 ◽  
Vol 25 (14) ◽  
pp. 6090-6102 ◽  
Author(s):  
Sotiris N. Nikolopoulos ◽  
Pamela Blaikie ◽  
Toshiaki Yoshioka ◽  
Wenjun Guo ◽  
Claudia Puri ◽  
...  
Keyword(s):  
Protein Kinases ◽  
Nuclear Translocation ◽  
Mitogen Activated Protein Kinases ◽  
Laminin 5 ◽  
Targeted Deletion ◽  
Mitogen Activated Protein ◽  
Signaling Domain ◽  
Epidermal Growth ◽  
And Migration ◽  
Mutant Cells

ABSTRACT The α6β4 integrin—a laminin-5 receptor—mediates assembly of hemidesmosomes and recruitment of Shc and phosphoinositide 3-kinase through the unique cytoplasmic extension of β4. Mice carrying a targeted deletion of the signaling domain of β4 develop normally and do not display signs of skin fragility. The epidermis of these mice contains well-structured hemidesmosomes and adheres stably to the basement membrane. However, it is hypoplastic due to reduced proliferation of basal keratinocytes and undergoes wound repair at a reduced rate. Keratinocytes from β4 mutant mice undergo extensive spreading but fail to proliferate and migrate in response to epidermal growth factor (EGF) on laminin-5. EGF causes significant phosphorylation of extracellular signal-regulated kinase (ERK) and Jun N-terminal protein kinase (JNK) and phosphorylation and degradation of IκB in β4 mutant cells adhering to laminin-5. Unexpectedly, however, ERK, JNK, and NF-κB remain in the cytoplasm in β4 mutant cells on laminin-5, whereas they enter effectively into the nucleus in the same cells on fibronectin or in wild-type cells on both matrix proteins. Inhibitor studies indicate that α6β4 promotes keratinocyte proliferation and migration through its effect on NF-κB and P-JNK. These findings provide evidence that β4 signaling promotes epidermal growth and wound healing through a previously unrecognized effect on nuclear translocation of NF-κB and mitogen-activated protein kinases.

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