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Am J Physiol Lung Cell Mol Physiol (January 4, 2002). doi:10.1152/ajplung.00178.2001
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Articles in PresS, published online ahead of print January 4, 2002
Am J Physiol Lung Cell Mol Physiol, 10.1152/ajplung.00178.2001
Submitted on May 17, 2001
Accepted on December 17, 2001

Dopamine activates ERKs in alveolar epithelial cells via Ras-PKC dependent and Grb2/SOS independent mechanisms

Carmen Guerrero1, Liuska Pesce2, Emilia Lecuona2, Karen M Ridge2, and Jacob I Sznajder2*

1 Department of Surgery, University of Salamanca, Salamanca, Salamanca, Spain
2 Medicine, Northwestern University, Chicago, IL, USA

* To whom correspondence should be addressed. E-mail: j-sznajder{at}nwu.edu.

Recently, it has been described that dopamine (DA), via dopaminergic type 2 receptors (D2R), activates the mitogen-activated protein kinase (MAPK/ERK) proteins in alveolar epithelial cells (AEC), which results in the upregulation of the Na,K-ATPase. In the present report, we used AEC to investigate the signaling pathway that links DA with ERK activation. Incubation of AEC with DA resulted in a rapid and transient stimulation of ERK activity, which was mediated by Ras proteins and the serine/threonine kinase Raf-1. Pre-treatment of AEC with SH3b-P, a peptide that blocks the interaction between Grb2 and SOS, did not prevent DA activation of ERK. DAG-dependent PKC isoenzymes were involved in the DA-mediated activation of ERK proteins as pretreatment with either bisindolylmaleimide or Ro-31-8220 prevented the phosphorylation of Elk-1 and quinpirole, a dopaminergic-type 2 receptor activator, stimulates the translocation of PKC{epsilon}. Taken together the data suggest that DA activated MAPK/ERK via Ras, Raf-1 kinase and DAG-dependent PKC isoenzymes but, importantly and contrary to the classical model, this pathway did not involve the Grb2-SOS complex formation.




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