“Soluble” adenylyl cyclase‐generated cyclic adenosine monophosphate promotes fast migration in PC12 cells
- 6 August 2007
- journal article
- research article
- Published by Wiley in Journal of Neuroscience Research
- Vol. 86 (1) , 118-124
- https://doi.org/10.1002/jnr.21458
Abstract
In a model for neuronal movement, PC12 cells undergo fast migration in response to nerve growth factor (NGF) and phorbol ester (PMA). We previously showed that NGF increases intracellular cAMP via activation of soluble adenylyl cyclase (sAC). In this report, we demonstrate that sAC activation is an essential component of NGF‐ + PMA‐induced fast migration in PC12 cells. Interestingly, PMA also raises intracellular cAMP but does so by stimulating transmembrane adenylyl cyclases (tmAC); however, this tmAC‐generated cAMP does not contribute to fast migration. Therefore, cells must possess independent pools of cAMP capable of modulating distinct functions.Keywords
This publication has 29 references indexed in Scilit:
- Soluble adenylyl cyclase is required for netrin-1 signaling in nerve growth conesNature Neuroscience, 2006
- Soluble Adenylyl Cyclase Mediates Nerve Growth Factor-induced Activation of Rap1Journal of Biological Chemistry, 2006
- Calcium-sensing soluble adenylyl cyclase mediates TNF signal transduction in human neutrophilsThe Journal of Experimental Medicine, 2005
- Compartmentalization of bicarbonate‐sensitive adenylyl cyclase in distinct signaling microdomainsThe FASEB Journal, 2002
- Signaling Pathways for PC12 Cell Differentiation: Making the Right ConnectionsScience, 2002
- Regulation of neural cell adhesion molecule polysialylation state by cell-cell contact and protein kinase C deltaJournal of Neuroscience Research, 2000
- Regulation of type V adenylyl cyclase by PMA‐sensitive and ‐insensitive protein kinase C isoenzymes in intact cellsFEBS Letters, 1996
- Phorbol ester stimulation of the type I and type III adenylyl cyclases in whole cellsBiochemistry, 1993
- Role of the cAMP‐dependent protein kinase and protein kinase C in regulating the morphological differentiation of PC12 cellsJournal of Neuroscience Research, 1990
- Calphostin C (UCN-1028C), a novel microbial compound, is a highly potent and specific inhibitor of protein kinase CBiochemical and Biophysical Research Communications, 1989