scholarly journals Interleukin-1 stimulates de novo synthesis of mitogen-activated protein kinase in glomerular mesangial cells

FEBS Letters ◽  
1994 ◽  
Vol 350 (1) ◽  
pp. 135-138 ◽  
Author(s):  
Andrea Huwiler ◽  
Josef Pfeilschifter
Keyword(s):  
Protein Kinase ◽  
De Novo ◽  
Mesangial Cells ◽  
Interleukin 1 ◽  
Mitogen Activated Protein Kinase ◽  
Glomerular Mesangial Cells ◽  
De Novo Synthesis ◽  
Mitogen Activated Protein

scholarly journals Cellular signaling by endothelin peptides: pathways to the nucleus.

1992 ◽  
Vol 2 (10) ◽  
pp. S116
Author(s):  
M S Simonson ◽  
Y Wang ◽  
M J Dunn
Keyword(s):  
Protein Kinase ◽  
Mesangial Cells ◽  
Regulatory Peptides ◽  
Mitogen Activated Protein Kinase ◽  
Activator Protein 1 ◽  
Glomerular Mesangial Cells ◽  
Short Term ◽  
Activator Protein ◽  
Mitogen Activated Protein

Endothelins (ET) are potent regulatory peptides that evoke diverse responses in glomerular mesangial cells. These include short-term actions, such as contraction and secretion, and long-term, adaptive responses, such as cell growth. Although much attention has been focused on the second messenger cascades, which govern short-term effects, the pathways of cytosolic and nuclear signaling, which effect long-term changes, remain unclear. Several distal signaling events by ET receptors have been characterized in rat mesangial cells. These include activation of a cytosolic protein kinase, mitogen-activated protein kinase and an inducible transcription factor, activator protein-1 (AP-1). This review focuses on the activation of mitogen-activated protein kinase and activator protein-1 by ET and discusses the potential role of these third and fourth messengers in controlling long-term cellular adaptations. Characterization of these and other cytosolic and nuclear signals should provide important insights into the pleiotropic actions of ET peptides.

scholarly journals Sphingolipid metabolites differentially regulate extracellular signal-regulated kinase and stress-activated protein kinase cascades

1996 ◽  
Vol 316 (1) ◽  
pp. 13-17 ◽  
Author(s):  
Emmaneul CORONEOS ◽  
Yizheng WANG ◽  
James R. PANUSKA ◽  
Dennis J. TEMPLETON ◽  
Mark KESTER
Keyword(s):  
Protein Kinase ◽  
Mesangial Cells ◽  
Membrane Receptors ◽  
Mitogen Activated Protein Kinase ◽  
Glomerular Mesangial Cells ◽  
Extracellular Signal Regulated Kinase ◽  
Mapk Signalling Pathway ◽  
Extracellular Signal ◽  
Mitogen Activated Protein ◽  
Plasma Membrane Receptors

The mitogen-activated protein kinase (MAPK) signalling pathway serves to translocate information from activated plasma-membrane receptors to initiate nuclear transcriptional events. This cascade has recently been subdivided into two analogous pathways: the extracellular signal-regulated kinase (ERK) cascade, which preferentially signals mitogenesis, and the stress-activated protein kinase (SAPK) cascade, which is linked to growth arrest and/or cellular inflammation. In concurrent experiments utilizing rat glomerular mesangial cells (MCs), we demonstrate that growth factors or sphingosine activate ERK but not SAPK. In contrast, inflammatory cytokines or cell-permeable ceramide analogues activate SAPK but not ERK. Ceramide, but not sphingosine, induces interleukin-6 secretion, a marker of an inflamed phenotype. Moreover, ceramide can suppress growth factor- or sphingosine-induced ERK activation as well as proliferation. These studies implicate sphingolipid metabolites as opposing regulators of cell proliferation and inflammation through activation of separate kinase cascades.

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