Abstract
The cAMP-dependent protein kinase (PKA) transduces signals in the heart initiated by β1-adrenergic, G-protein-coupled receptors after norepinephrine, sympathetic stimulation. Signaling through this pathway results in a characteristic set of cellular responses, including increases in ion fluxes and contractile strength, mobilization of energy stores, and changes in gene expression. Not all receptors that activate adenylate cyclase and increase cAMP levels, however, cause the cardiac myocyte to react in this manner. Research in the field of signal transduction over the last 25 years has addressed this issue of specificity in signaling by diffusable second messengers. PKA is in part targeted to discrete cellular locations by A-kinase anchoring proteins. Through anchoring and formation of multienzyme complexes, specific, localized signal transduction is possible. I discuss in this review recent advances in the understanding of PKA signaling complexes in the cardiac myocyte.
| Original language | English |
|---|---|
| Pages (from-to) | 193-199 |
| Number of pages | 7 |
| Journal | Molecular Pharmacology |
| Volume | 62 |
| Issue number | 2 |
| DOIs | |
| State | Published - Aug 3 2002 |
| Externally published | Yes |
Fingerprint
ASJC Scopus subject areas
- Pharmacology
Cite this
Contributions of protein kinase A anchoring proteins to compartmentation of cAMP signaling in the heart. / Kapiloff, Michael S.
In: Molecular Pharmacology, Vol. 62, No. 2, 03.08.2002, p. 193-199.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Contributions of protein kinase A anchoring proteins to compartmentation of cAMP signaling in the heart
AU - Kapiloff, Michael S
PY - 2002/8/3
Y1 - 2002/8/3
N2 - The cAMP-dependent protein kinase (PKA) transduces signals in the heart initiated by β1-adrenergic, G-protein-coupled receptors after norepinephrine, sympathetic stimulation. Signaling through this pathway results in a characteristic set of cellular responses, including increases in ion fluxes and contractile strength, mobilization of energy stores, and changes in gene expression. Not all receptors that activate adenylate cyclase and increase cAMP levels, however, cause the cardiac myocyte to react in this manner. Research in the field of signal transduction over the last 25 years has addressed this issue of specificity in signaling by diffusable second messengers. PKA is in part targeted to discrete cellular locations by A-kinase anchoring proteins. Through anchoring and formation of multienzyme complexes, specific, localized signal transduction is possible. I discuss in this review recent advances in the understanding of PKA signaling complexes in the cardiac myocyte.
AB - The cAMP-dependent protein kinase (PKA) transduces signals in the heart initiated by β1-adrenergic, G-protein-coupled receptors after norepinephrine, sympathetic stimulation. Signaling through this pathway results in a characteristic set of cellular responses, including increases in ion fluxes and contractile strength, mobilization of energy stores, and changes in gene expression. Not all receptors that activate adenylate cyclase and increase cAMP levels, however, cause the cardiac myocyte to react in this manner. Research in the field of signal transduction over the last 25 years has addressed this issue of specificity in signaling by diffusable second messengers. PKA is in part targeted to discrete cellular locations by A-kinase anchoring proteins. Through anchoring and formation of multienzyme complexes, specific, localized signal transduction is possible. I discuss in this review recent advances in the understanding of PKA signaling complexes in the cardiac myocyte.
UR - http://www.scopus.com/inward/record.url?scp=0036073345&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0036073345&partnerID=8YFLogxK
U2 - 10.1124/mol.62.2.193
DO - 10.1124/mol.62.2.193
M3 - Article
C2 - 12130668
AN - SCOPUS:0036073345
VL - 62
SP - 193
EP - 199
JO - Molecular Pharmacology
JF - Molecular Pharmacology
SN - 0026-895X
IS - 2
ER -