Linked Life Data

7589403

Source:http://linkedlifedata.com/resource/pubmed/id/7589403

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
1995-12-7
pubmed:abstractText
Phophodiesterase (PDE) isoenzyme profiles of human cell preparations and tissues have been analysed by a semiquantitative method using selective PDE inhibitors and activators. Neutrophils, eosinophils and monocytes contain PDE IV exclusively. Lymphocytes, alveolar macrophages and endothelial cells contain PDE IV and PDE III, and in addition, PDE I is measured in macrophages and PDE II in endothelial cells. These basal cell-specific PDE isoenzyme profiles appear to be modified by: 1) substrate concentration; 2) kinase-dependent phosphorylation; and 3) regulated rate of synthesis. Therefore, PDE isoenzyme profiles represent dynamic patterns, which apparently adapt to pathological and environmental conditions. In parallel functional studies, the influence of mono-selective (rolipram, PDE IV; motapizone, PDE III), dual-selective (zardaverine) and non-selective (theophylline) PDE inhibitors were compared. Corresponding to isoenzyme analysis, it was demonstrated that both PDE III and PDE IV have to be inhibited for complete suppression of either tumour necrosis factor-alpha (TNF-alpha) release from macrophages, or lymphocyte proliferation (PDE III/IV cells). In eosinophils (PDE IV cells) platelet-activating factor (PAF)-induced chemotaxis or C5a-stimulated degranulation are only weakly inhibited by rolipram alone. After addition of a beta 2-agonist, however, the efficacy of rolipram is enhanced due to concomitant influence of synthesis and breakdown of cyclic adenosine monophosphate (cAMP). Theophylline inhibits PDE isoenzyme activities and functions of inflammatory cells with similar potency, and exhibits higher functional efficacy as compared to rolipram.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0903-1936
pubmed:author
pubmed:issnType
Print
pubmed:volume
8
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1179-83
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
PDE isoenzymes as targets for anti-asthma drugs.
pubmed:affiliation
Dept of Biochemistry, Byk Gulden, Konstanz, Germany.
pubmed:publicationType
Journal Article, Comparative Study, Review