Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions |
umls-concept:C0006104,
umls-concept:C0006556,
umls-concept:C0009015,
umls-concept:C0017262,
umls-concept:C0031640,
umls-concept:C0034861,
umls-concept:C0035696,
umls-concept:C0040287,
umls-concept:C0086418,
umls-concept:C0185117,
umls-concept:C0205474,
umls-concept:C0220927,
umls-concept:C1880022,
umls-concept:C2911684
|
| pubmed:issue |
9
|
| pubmed:dateCreated |
1993-4-22
|
| pubmed:databankReference | |
| pubmed:abstractText |
We have isolated cDNA clones from human frontal cortex cDNA libraries that encode a unique subtype of the low-Km, cAMP-specific phosphodiesterases (PDEs IV). The 564-amino acid sequence of the protein (human brain PDE IV (hPDE IVB)) shows significant homology to a PDE IV subtype expressed in human monocytes (hPDE IVA), particularly within the approximately 300-amino acid PDE IV catalytic domain. The degree of protein sequence identity is much greater between hPDE IVB and a homolog derived from rat brain (92% over 562 amino acids) than between hPDE IVB and hPDE IVA (76% over 538 amino acids), suggesting a greater subtype-specific versus species-specific conservation of protein sequence. Analysis of the distribution of hPDE IVB mRNA expression revealed a restricted pattern, with an approximately 4-kilobase mRNA detected in brain, heart, lung, and skeletal muscle and not in placenta, liver, kidney, or pancreas. An additional approximately 5-kilobase hPDE IVB-related mRNA species was detected in brain tissue. Recombinant hPDE IVB displayed all of the expected kinetic characteristics for a PDE IV, including sensitivity to the isozyme-selective inhibitor rolipram (Ki = 0.085 microM). Scatchard analysis of (R)-[3H]rolipram binding data suggested the presence of two noninteracting high affinity rolipram-binding sites (Kd = 0.4 and 6 nM) or a negatively cooperative interaction among multiple binding sites.
|
| 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/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/Pyrrolidinones,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Rolipram
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Mar
|
| pubmed:issn |
0021-9258
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
25
|
| pubmed:volume |
268
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
6470-6
|
| pubmed:dateRevised |
2007-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:8384210-3',5'-Cyclic-AMP Phosphodiesterases,
pubmed-meshheading:8384210-Amino Acid Sequence,
pubmed-meshheading:8384210-Animals,
pubmed-meshheading:8384210-Base Sequence,
pubmed-meshheading:8384210-Brain,
pubmed-meshheading:8384210-Cloning, Molecular,
pubmed-meshheading:8384210-DNA,
pubmed-meshheading:8384210-Humans,
pubmed-meshheading:8384210-Kinetics,
pubmed-meshheading:8384210-Molecular Sequence Data,
pubmed-meshheading:8384210-Organ Specificity,
pubmed-meshheading:8384210-Pyrrolidinones,
pubmed-meshheading:8384210-RNA, Messenger,
pubmed-meshheading:8384210-Rats,
pubmed-meshheading:8384210-Recombinant Proteins,
pubmed-meshheading:8384210-Rolipram,
pubmed-meshheading:8384210-Saccharomyces cerevisiae,
pubmed-meshheading:8384210-Sequence Homology, Amino Acid
|
| pubmed:year |
1993
|
| pubmed:articleTitle |
A low-Km, rolipram-sensitive, cAMP-specific phosphodiesterase from human brain. Cloning and expression of cDNA, biochemical characterization of recombinant protein, and tissue distribution of mRNA.
|
| pubmed:affiliation |
Department of Gene Expression Sciences, SmithKline Beecham Pharmaceuticals, King of Prussia, Pennsylvania 19406.
|
| pubmed:publicationType |
Journal Article
|