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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1-2
|
| pubmed:dateCreated |
1998-9-16
|
| pubmed:abstractText |
cDNAs encoding two PDE-3 or cyclic GMP-inhibited (cGI) cyclic nucleotide phosphodiesterase (PDE) isoforms, RPDE-3B (RcGIP1) and HPDE-3A (HcGIP2), were cloned from rat (R) adipose tissue and human (H) heart cDNA libraries. Deletion and N- and C-terminal truncation mutants were expressed in Escherichia coli in order to define their catalytic core. Active mutants of both RPDE-3B and HPDE-3A included the domain conserved among all PDEs plus additional upstream and downstream sequences. An RPDE-3B mutant consisting of the conserved domain alone and one from which the RPDE-3B 44-amino acid insertion was deleted exhibited little or no activity. All active recombinants exhibited a high affinity (< 1 microM) for cyclic AMP (cAMP) and cyclic GMP (cGMP), were inhibited by cAMP, cGMP, and cilostamide, but not by rolipram, and were photolabeled with [32P]-cGMP. The IC50 values for cGMP inhibition of cAMP hydrolysis were lower for HPDE-3A than for RPDE-3B recombinants. The deduced amino acid sequences of HPDE-3A and RPDE-3B catalytic domains are very similar except for the 44-amino acid insertion not found in other PDEs. It is possible that this insertion may not only distinguish PDE-3 catalytic domains from other PDEs and identify catalytic domains of PDE-3 subfamilies or conserved members of the PDE-3 gene family, but may also be involved in the regulation of sensitivity of PDE-3s to cGMP.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/3',5'-Cyclic-AMP Phosphodiesterases,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclic AMP,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclic GMP,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclic Nucleotide...,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins
|
| pubmed:status |
MEDLINE
|
| pubmed:issn |
1085-9195
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
29
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
89-111
|
| pubmed:dateRevised |
2007-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:9631240-3',5'-Cyclic-AMP Phosphodiesterases,
pubmed-meshheading:9631240-Animals,
pubmed-meshheading:9631240-Binding Sites,
pubmed-meshheading:9631240-Blotting, Western,
pubmed-meshheading:9631240-Catalysis,
pubmed-meshheading:9631240-Cyclic AMP,
pubmed-meshheading:9631240-Cyclic GMP,
pubmed-meshheading:9631240-Cyclic Nucleotide Phosphodiesterases, Type 3,
pubmed-meshheading:9631240-Enzyme Activation,
pubmed-meshheading:9631240-Escherichia coli,
pubmed-meshheading:9631240-Humans,
pubmed-meshheading:9631240-Isoenzymes,
pubmed-meshheading:9631240-Molecular Sequence Data,
pubmed-meshheading:9631240-Mutagenesis, Insertional,
pubmed-meshheading:9631240-Protein Structure, Tertiary,
pubmed-meshheading:9631240-Rats,
pubmed-meshheading:9631240-Recombinant Fusion Proteins,
pubmed-meshheading:9631240-Sequence Deletion
|
| pubmed:year |
1998
|
| pubmed:articleTitle |
Expression and characterization of deletion recombinants of two cGMP-inhibited cyclic nucleotide phosphodiesterases (PDE-3).
|
| pubmed:affiliation |
Department of Cellular and Molecular Biology, Lund University, Sweden.
|
| pubmed:publicationType |
Journal Article
|