pubmed-article:2826188 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:2826188 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
pubmed-article:2826188 | lifeskim:mentions | umls-concept:C0007412 | lld:lifeskim |
pubmed-article:2826188 | lifeskim:mentions | umls-concept:C0023517 | lld:lifeskim |
pubmed-article:2826188 | lifeskim:mentions | umls-concept:C0001492 | lld:lifeskim |
pubmed-article:2826188 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
pubmed-article:2826188 | lifeskim:mentions | umls-concept:C1948023 | lld:lifeskim |
pubmed-article:2826188 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:2826188 | pubmed:dateCreated | 1988-2-2 | lld:pubmed |
pubmed-article:2826188 | pubmed:abstractText | The racemic 3-O-sulfates of epinephrine and norepinephrine as well as 4-O-sulfoconjugated dopamine were synthesized, highly purified and investigated with respect to their beta-adrenoceptor affinities and relative potencies in the receptor-coupled adenylate cyclase system in isolated human mononuclear leukocytes. The receptor affinities of all catecholamine sulfates were reduced at least 1,000-fold when compared to those of the free catecholamines. Furthermore, catecholamine sulfoconjugates did not produce intracellular cAMP signals. In contrast to the sulfated catecholamine metabolites, the 3-O-methylated catecholamines metanephrine and normetanephrine were found to behave as endogenous beta-adrenoceptor-competing agents with lower beta-receptor affinities than the corresponding free catecholamines. No beta-receptor agonist activity in the adenylate cyclase system was found with metanephrine and normetanephrine. Our data provide direct evidence that sulfoconjugation renders catecholamines inactive as beta-receptor ligands and must thus be regarded as a mechanism to control adrenergic action at the prereceptor level by a buffering of the concentration of free catecholamines. The physiological significance of a potential role of 3-O-methylated catecholamines as endogenous beta-receptor antagonists has to be further clarified. | lld:pubmed |
pubmed-article:2826188 | pubmed:language | eng | lld:pubmed |
pubmed-article:2826188 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2826188 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:2826188 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2826188 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2826188 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2826188 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2826188 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2826188 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2826188 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2826188 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:2826188 | pubmed:month | Nov | lld:pubmed |
pubmed-article:2826188 | pubmed:issn | 0014-2999 | lld:pubmed |
pubmed-article:2826188 | pubmed:author | pubmed-author:WeickerHH | lld:pubmed |
pubmed-article:2826188 | pubmed:author | pubmed-author:LenzTT | lld:pubmed |
pubmed-article:2826188 | pubmed:author | pubmed-author:WerleEE | lld:pubmed |
pubmed-article:2826188 | pubmed:author | pubmed-author:BiegerW PWP | lld:pubmed |
pubmed-article:2826188 | pubmed:author | pubmed-author:MichelG LGL | lld:pubmed |
pubmed-article:2826188 | pubmed:author | pubmed-author:LernhardtUU | lld:pubmed |
pubmed-article:2826188 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:2826188 | pubmed:day | 10 | lld:pubmed |
pubmed-article:2826188 | pubmed:volume | 143 | lld:pubmed |
pubmed-article:2826188 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:2826188 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:2826188 | pubmed:pagination | 179-88 | lld:pubmed |
pubmed-article:2826188 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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pubmed-article:2826188 | pubmed:year | 1987 | lld:pubmed |
pubmed-article:2826188 | pubmed:articleTitle | Sulfoconjugated catecholamines: lack of beta-adrenoceptor binding and adenylate cyclase stimulation in human mononuclear leukocytes. | lld:pubmed |
pubmed-article:2826188 | pubmed:affiliation | Department of Pathophysiology and Sport Medicine, University of Heidelberg, F.R.G. | lld:pubmed |
pubmed-article:2826188 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:2826188 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |