Source:http://linkedlifedata.com/resource/pubmed/id/10766874
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
16
|
pubmed:dateCreated |
2000-5-10
|
pubmed:abstractText |
The N-terminal portion of phosphodiesterase (PDE) 3 was arbitrarily divided into region 1 (amino acids 1-300), which contains a large hydrophobic domain with six predicted transmembrane helices, and region 2 (amino acids 301-500), with a smaller hydrophobic domain ( approximately 50 residues). To analyze these regions, full-length human (H)PDE3A and mouse (M)PDE3B and a series of N-terminal truncated mutants were synthesized in Sf9 cells. Activities of HPDE3A, H3A-Delta189, MPDE3B, and M3B-Delta196, which retained all or part of the hydrophobic domain in region 1, were recovered almost entirely in particulate fractions. H3A-Delta321 and M3B-Delta302, containing region 2, were recovered essentially equally in particulate and cytosolic fractions. H3A-Delta397 and H3A-Delta457, lacking both hydrophobic domains, were predominantly cytosolic. H3A-Delta510 and M3B-Delta604, lacking both regions 1 and 2, were virtually completely cytosolic. M3B-Delta196 eluted as a large aggregated complex during gel filtration. With removal of greater amounts of N-terminal sequence, aggregation of PDE3 decreased, and H3A-Delta607, H3A-Delta721, and M3B-Delta604 eluted as dimers. Truncated HPDE3A proteins were more sensitive than full-length HPDE3A to inhibition by lixazinone. These results suggest that the hydrophobic domains in regions 1 and 2 contain structural determinants important for association of PDE3 with intracellular membranes, as well for self-association or aggregation during gel filtration and sensitivity to a specific inhibitor.
|
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 Nucleotide...,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/PDE3A protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/PDE3B protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Pde3a protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Pde3b protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Quinazolines,
http://linkedlifedata.com/resource/pubmed/chemical/lixazinone
|
pubmed:status |
MEDLINE
|
pubmed:month |
Apr
|
pubmed:issn |
0021-9258
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
21
|
pubmed:volume |
275
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
12331-8
|
pubmed:dateRevised |
2007-11-15
|
pubmed:meshHeading |
pubmed-meshheading:10766874-3',5'-Cyclic-AMP Phosphodiesterases,
pubmed-meshheading:10766874-Animals,
pubmed-meshheading:10766874-Blotting, Western,
pubmed-meshheading:10766874-Cyclic Nucleotide Phosphodiesterases, Type 3,
pubmed-meshheading:10766874-Humans,
pubmed-meshheading:10766874-Isoenzymes,
pubmed-meshheading:10766874-Kinetics,
pubmed-meshheading:10766874-Mice,
pubmed-meshheading:10766874-Mutagenesis, Site-Directed,
pubmed-meshheading:10766874-Protein Conformation,
pubmed-meshheading:10766874-Quinazolines,
pubmed-meshheading:10766874-Sequence Deletion,
pubmed-meshheading:10766874-Solubility,
pubmed-meshheading:10766874-Structure-Activity Relationship
|
pubmed:year |
2000
|
pubmed:articleTitle |
Functions of the N-terminal region of cyclic nucleotide phosphodiesterase 3 (PDE 3) isoforms.
|
pubmed:affiliation |
Pulmonary/Critical Care Medicine Branch, NHLBI, National Institutes of Health, Bethesda, Maryland 20892, USA.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|