pubmed-article:1707917 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:1707917 | lifeskim:mentions | umls-concept:C0001443 | lld:lifeskim |
pubmed-article:1707917 | lifeskim:mentions | umls-concept:C1622844 | lld:lifeskim |
pubmed-article:1707917 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
pubmed-article:1707917 | pubmed:issue | 8 | lld:pubmed |
pubmed-article:1707917 | pubmed:dateCreated | 1991-5-21 | lld:pubmed |
pubmed-article:1707917 | pubmed:abstractText | We have investigated the effects of cAMP on Ig-induced human eosinophil activation. Stimulation of human normodense eosinophils with IgG- or secretory IgA (sIgA)-coated Sepharose beads induced cellular degranulation, as measured by the release of the granule protein, eosinophil-derived neurotoxin (EDN). Pretreatment with cAMP analogs (N6,O2,-dibutyryl adenosine-3,':5' cyclic monophosphate; 8-bromoadenosine 3':5' cyclic monophosphate; or N6-benzoyladenosine 3':5' cyclic monophosphate) or cAMP phosphodiesterase-inhibitors (theophylline or isobutylmethyl xanthine (IBMX] strongly inhibited Ig-induced human eosinophil degranulation. The beta-adrenoceptor agonists, isoproterenol and salbutamol, induced relatively low level increases in intracellular cAMP, and weakly suppressed EDN release induced by IgG-coated beads. However, cellular pretreatment with IBMX synergistically enhanced the inhibitory effects of isoproterenol or salbutamol on both IgG and sIgA-induced eosinophil degranulation. Similarly, PGE2 treatment increased intracellular cAMP concentrations in eosinophils and correspondingly inhibited the Ig-dependent cellular degranulation response: co-incubation with IBMX further enhanced both effects of PGE2. Finally, cholera toxin, which irreversibly activates the stimulatory guanine nucleotide-binding protein linked to adenylyl cyclase, strongly inhibited the release of EDN from IgG- or sIgA-stimulated eosinophils. The time-dependent accumulation of cAMP in cholera toxin-treated cells closely paralleled the time courses of inhibition of IgG- and sIgA-induced EDN release after toxin exposure. These data indicate that the cAMP-dependent signal transduction mechanism in eosinophils exerts a negative modulatory effect on the cellular degranulation responses induced by sIgA or IgG. The inhibitory effects of cAMP on eosinophil activation may provide an important physiologic and a clinically relevant therapeutic mechanism for limiting the release of eosinophil-derived cytotoxic proteins during certain allergic or inflammatory responses in vivo. | lld:pubmed |
pubmed-article:1707917 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1707917 | pubmed:language | eng | lld:pubmed |
pubmed-article:1707917 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1707917 | pubmed:citationSubset | AIM | lld:pubmed |
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pubmed-article:1707917 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:1707917 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:1707917 | pubmed:month | Apr | lld:pubmed |
pubmed-article:1707917 | pubmed:issn | 0022-1767 | lld:pubmed |
pubmed-article:1707917 | pubmed:author | pubmed-author:KitaHH | lld:pubmed |
pubmed-article:1707917 | pubmed:author | pubmed-author:GleichG JGJ | lld:pubmed |
pubmed-article:1707917 | pubmed:author | pubmed-author:AbrahamR TRT | lld:pubmed |
pubmed-article:1707917 | pubmed:author | pubmed-author:Abu-GhazalehR... | lld:pubmed |
pubmed-article:1707917 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:1707917 | pubmed:day | 15 | lld:pubmed |
pubmed-article:1707917 | pubmed:volume | 146 | lld:pubmed |
pubmed-article:1707917 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:1707917 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:1707917 | pubmed:pagination | 2712-8 | lld:pubmed |
pubmed-article:1707917 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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pubmed-article:1707917 | pubmed:year | 1991 | lld:pubmed |
pubmed-article:1707917 | pubmed:articleTitle | Regulation of Ig-induced eosinophil degranulation by adenosine 3',5'-cyclic monophosphate. | lld:pubmed |
pubmed-article:1707917 | pubmed:affiliation | Department of Immunology, Mayo Graduate School of Medicine, Rochester, MN 55905. | lld:pubmed |
pubmed-article:1707917 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:1707917 | pubmed:publicationType | In Vitro | lld:pubmed |
pubmed-article:1707917 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:1707917 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
pubmed-article:1707917 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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