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Methods to study phosphorylation and activation of the hormone-sensitive adipocyte phosphodiesterase type 3B in rat adipocytes

Degerman, Eva LU orcid ; Resjö, Svante LU ; Landström, Tova LU and Manganiello, Vincent (2001) In Methods in Molecular Biology 155. p.167-180
Abstract
Cyclic nucleotide phosphodiesterases (PDEs) include a large group of structurally related enzymes that are responsible for the hydrolysis of cyclic adenosine monophosphate (cAMP) and cyclic guanosine monophosphate (cGMP). These enzymes belong to at least nine related gene families (PDEs 1–9) (1–5), which differ in their primary structures, affinities for cAMP and cGMP, responses to specific effectors, sensitivities to specific inhibitors, and regulatory mechanisms. The PDE3 family (6) consists of two subfamilies, PDE3A and PDE3B, which exhibit tissue-specific distribution; grossly, PDE3A enzymes are expressed in the cardiovascular system, and PDE3B enzymes in insulin-sensitive cells, such as hepatocytes (7) and adipocytes (6), and also in... (More)
Cyclic nucleotide phosphodiesterases (PDEs) include a large group of structurally related enzymes that are responsible for the hydrolysis of cyclic adenosine monophosphate (cAMP) and cyclic guanosine monophosphate (cGMP). These enzymes belong to at least nine related gene families (PDEs 1–9) (1–5), which differ in their primary structures, affinities for cAMP and cGMP, responses to specific effectors, sensitivities to specific inhibitors, and regulatory mechanisms. The PDE3 family (6) consists of two subfamilies, PDE3A and PDE3B, which exhibit tissue-specific distribution; grossly, PDE3A enzymes are expressed in the cardiovascular system, and PDE3B enzymes in insulin-sensitive cells, such as hepatocytes (7) and adipocytes (6), and also in pancreatic β-cells (8). One characteristic of PDE3s involves their phosphorylation and activation in response to insulin, as well as to agents that increase cAMP in adipocytes (6), hepatocytes (7), and platelets (9–11), and in response to insulin-like growth factor-1 (IGF-)1 in pancreatic β-cells (8). (Less)
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author
; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Methods in Molecular Biology
volume
155
pages
167 - 180
publisher
Springer
external identifiers
  • pmid:11293069
  • scopus:0035222384
ISSN
1940-6029
DOI
10.1385/1-59259-231-7:167
language
English
LU publication?
yes
id
246aaea6-fea7-4731-9521-fd7a78b16b9d (old id 1119824)
date added to LUP
2016-04-01 11:52:19
date last changed
2025-04-04 15:33:44
@article{246aaea6-fea7-4731-9521-fd7a78b16b9d,
  abstract     = {{Cyclic nucleotide phosphodiesterases (PDEs) include a large group of structurally related enzymes that are responsible for the hydrolysis of cyclic adenosine monophosphate (cAMP) and cyclic guanosine monophosphate (cGMP). These enzymes belong to at least nine related gene families (PDEs 1–9) (1–5), which differ in their primary structures, affinities for cAMP and cGMP, responses to specific effectors, sensitivities to specific inhibitors, and regulatory mechanisms. The PDE3 family (6) consists of two subfamilies, PDE3A and PDE3B, which exhibit tissue-specific distribution; grossly, PDE3A enzymes are expressed in the cardiovascular system, and PDE3B enzymes in insulin-sensitive cells, such as hepatocytes (7) and adipocytes (6), and also in pancreatic β-cells (8). One characteristic of PDE3s involves their phosphorylation and activation in response to insulin, as well as to agents that increase cAMP in adipocytes (6), hepatocytes (7), and platelets (9–11), and in response to insulin-like growth factor-1 (IGF-)1 in pancreatic β-cells (8).}},
  author       = {{Degerman, Eva and Resjö, Svante and Landström, Tova and Manganiello, Vincent}},
  issn         = {{1940-6029}},
  language     = {{eng}},
  pages        = {{167--180}},
  publisher    = {{Springer}},
  series       = {{Methods in Molecular Biology}},
  title        = {{Methods to study phosphorylation and activation of the hormone-sensitive adipocyte phosphodiesterase type 3B in rat adipocytes}},
  url          = {{http://dx.doi.org/10.1385/1-59259-231-7:167}},
  doi          = {{10.1385/1-59259-231-7:167}},
  volume       = {{155}},
  year         = {{2001}},
}