Phorbol ester effects on α1-adrenoceptor binding and phosphatidylinositol metabolism in cultured vascular smooth muscle cells
(1985) In Life Sciences 37(25). p.2389-2398- Abstract
Tumor promoting phorbol esters stimulate Ca++ phospholipid-dependent protein kinase C. It has been suggested that this enzyme regulates the functional properties of different cell membrane receptors. In this study we investigated the effect of phorbol esters on α1-adrenoceptor binding and phosphatidylinositol metabolism in cultured smooth muscle cells derived from rabbit aorta. Treatment of these cells with biologically active phorbol esters for 15 min. to 2 hours caused a marked decrease of norepinephrine stimulation of inositol phospholipid metabolism and a 3 fold decrease in agonist affinity for 125I-HEAT binding to α1-adrenoceptors in the intact smooth muscle cells. The ability of phorbol... (More)
Tumor promoting phorbol esters stimulate Ca++ phospholipid-dependent protein kinase C. It has been suggested that this enzyme regulates the functional properties of different cell membrane receptors. In this study we investigated the effect of phorbol esters on α1-adrenoceptor binding and phosphatidylinositol metabolism in cultured smooth muscle cells derived from rabbit aorta. Treatment of these cells with biologically active phorbol esters for 15 min. to 2 hours caused a marked decrease of norepinephrine stimulation of inositol phospholipid metabolism and a 3 fold decrease in agonist affinity for 125I-HEAT binding to α1-adrenoceptors in the intact smooth muscle cells. The ability of phorbol esters to modulate α1-adrenoceptor responsiveness suggests that activation of protein kinase C may represent an important mechanism regulating α1-adrenergic receptor functional properties.
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- author
- Cotecchia, Susanna ; Leeb-Lundberg, L. M.Fredrik LU ; Hagen, Per Otto ; Lefkowitz, Robert J. and Caron, Marc G.
- publishing date
- 1985-12-23
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Life Sciences
- volume
- 37
- issue
- 25
- pages
- 2389 - 2398
- publisher
- Elsevier
- external identifiers
-
- scopus:0022367653
- pmid:3001461
- ISSN
- 0024-3205
- DOI
- 10.1016/0024-3205(85)90106-7
- language
- English
- LU publication?
- no
- id
- 7e772038-3654-4990-93b1-6f7fc8699700
- date added to LUP
- 2019-06-04 14:42:30
- date last changed
- 2024-01-01 09:17:30
@article{7e772038-3654-4990-93b1-6f7fc8699700,
abstract = {{<p>Tumor promoting phorbol esters stimulate Ca<sup>++</sup> phospholipid-dependent protein kinase C. It has been suggested that this enzyme regulates the functional properties of different cell membrane receptors. In this study we investigated the effect of phorbol esters on α<sub>1</sub>-adrenoceptor binding and phosphatidylinositol metabolism in cultured smooth muscle cells derived from rabbit aorta. Treatment of these cells with biologically active phorbol esters for 15 min. to 2 hours caused a marked decrease of norepinephrine stimulation of inositol phospholipid metabolism and a 3 fold decrease in agonist affinity for <sup>125</sup>I-HEAT binding to α<sub>1</sub>-adrenoceptors in the intact smooth muscle cells. The ability of phorbol esters to modulate α<sub>1</sub>-adrenoceptor responsiveness suggests that activation of protein kinase C may represent an important mechanism regulating α<sub>1</sub>-adrenergic receptor functional properties.</p>}},
author = {{Cotecchia, Susanna and Leeb-Lundberg, L. M.Fredrik and Hagen, Per Otto and Lefkowitz, Robert J. and Caron, Marc G.}},
issn = {{0024-3205}},
language = {{eng}},
month = {{12}},
number = {{25}},
pages = {{2389--2398}},
publisher = {{Elsevier}},
series = {{Life Sciences}},
title = {{Phorbol ester effects on α<sub>1</sub>-adrenoceptor binding and phosphatidylinositol metabolism in cultured vascular smooth muscle cells}},
url = {{http://dx.doi.org/10.1016/0024-3205(85)90106-7}},
doi = {{10.1016/0024-3205(85)90106-7}},
volume = {{37}},
year = {{1985}},
}