Protein kinase A-dependent activation of PDE4 (cAMP-specific cyclic nucleotide phosphodiesterase) in cultured bovine vascular smooth muscle cells
Ekholm, Dag ; Belfrage, Per LU ; Manganiello, Vincent and Degerman, Eva LU
(1997)
In Biochimica et Biophysica Acta
1356(1).
p.64-70
- Abstract
- Incubation of cultured bovine vascular smooth muscle cells (VSMC) with forskolin increased cAMP as measured by an increase in cAMP-dependent protein kinase (PKA) activation (PKA ratio). Forskolin also produced a concentration- and time-dependent increase in activity (3-5-fold within 15 min) of a PDE4 (cAMP-specific cyclic nucleotide phosphodiesterase). The increase in PDE4 activity was not affected by cycloheximide and thus not likely due to increased synthesis of the enzyme. Activation, which was preserved during partial purification of the enzyme by chromatography on Sephacryl S-200 and MonoQ, was most likely due to a covalent modification. Incubation of cell homogenates with the catalytic subunit of PKA (PKA(c)) induced a approximately... (More)
- Incubation of cultured bovine vascular smooth muscle cells (VSMC) with forskolin increased cAMP as measured by an increase in cAMP-dependent protein kinase (PKA) activation (PKA ratio). Forskolin also produced a concentration- and time-dependent increase in activity (3-5-fold within 15 min) of a PDE4 (cAMP-specific cyclic nucleotide phosphodiesterase). The increase in PDE4 activity was not affected by cycloheximide and thus not likely due to increased synthesis of the enzyme. Activation, which was preserved during partial purification of the enzyme by chromatography on Sephacryl S-200 and MonoQ, was most likely due to a covalent modification. Incubation of cell homogenates with the catalytic subunit of PKA (PKA(c)) induced a approximately 5-fold activation of PDE4 with a time course similar to that in intact cells after forskolin addition. The forskolin-mediated activation was reversed during incubation of homogenates at room temperature for two hours. Addition of PKA(c) resulted in rapid reactivation of PDE4. These data are consistent with the hypothesis that rapid, reversible activation of PDE4 in cultured VSMC is mediated by PKA. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1112183
- author
- Ekholm, Dag
; Belfrage, Per
LU
; Manganiello, Vincent
and Degerman, Eva
LU
- organization
- publishing date
- 1997
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Phosphodiesterase, Smooth muscle cells, cAMP dependent protein kinase, Rolipram, Forskolin
- in
- Biochimica et Biophysica Acta
- volume
- 1356
- issue
- 1
- pages
- 64 - 70
- publisher
- Elsevier
- external identifiers
-
- pmid:9099992
- scopus:0030970077
- ISSN
- 0006-3002
- DOI
- 10.1016/S0167-4889(96)00159-0
- language
- English
- LU publication?
- yes
- id
- 14d671d3-c213-4475-ba1e-a7d35451bbbd (old id 1112183)
- date added to LUP
- 2016-04-01 15:59:35
- date last changed
- 2022-02-05 05:07:10
@article{14d671d3-c213-4475-ba1e-a7d35451bbbd,
abstract = {{Incubation of cultured bovine vascular smooth muscle cells (VSMC) with forskolin increased cAMP as measured by an increase in cAMP-dependent protein kinase (PKA) activation (PKA ratio). Forskolin also produced a concentration- and time-dependent increase in activity (3-5-fold within 15 min) of a PDE4 (cAMP-specific cyclic nucleotide phosphodiesterase). The increase in PDE4 activity was not affected by cycloheximide and thus not likely due to increased synthesis of the enzyme. Activation, which was preserved during partial purification of the enzyme by chromatography on Sephacryl S-200 and MonoQ, was most likely due to a covalent modification. Incubation of cell homogenates with the catalytic subunit of PKA (PKA(c)) induced a approximately 5-fold activation of PDE4 with a time course similar to that in intact cells after forskolin addition. The forskolin-mediated activation was reversed during incubation of homogenates at room temperature for two hours. Addition of PKA(c) resulted in rapid reactivation of PDE4. These data are consistent with the hypothesis that rapid, reversible activation of PDE4 in cultured VSMC is mediated by PKA.}},
author = {{Ekholm, Dag and Belfrage, Per and Manganiello, Vincent and Degerman, Eva}},
issn = {{0006-3002}},
keywords = {{Phosphodiesterase; Smooth muscle cells; cAMP dependent protein kinase; Rolipram; Forskolin}},
language = {{eng}},
number = {{1}},
pages = {{64--70}},
publisher = {{Elsevier}},
series = {{Biochimica et Biophysica Acta}},
title = {{Protein kinase A-dependent activation of PDE4 (cAMP-specific cyclic nucleotide phosphodiesterase) in cultured bovine vascular smooth muscle cells}},
url = {{http://dx.doi.org/10.1016/S0167-4889(96)00159-0}},
doi = {{10.1016/S0167-4889(96)00159-0}},
volume = {{1356}},
year = {{1997}},
}