Abstract
Although it is now established that immunocompetent cells produce catecholamines (CA), which in turn may act as autocrine/paracrine mediators, little is known about the mechanisms regulating CA production in these cells. In the present study, evidence is provided that stimulation of human cultured peripheral blood mononuclear cells (PBMCs) with phytohaemagglutinin (PHA) induces the expression of tyrosine hydroxylase (TH) mRNA and subsequently increases intracellular CA levels through protein kinase C (PKC) activation and the contribution of intracellular Ca(++)-dependent mechanisms. Increased production of CA in PHA-stimulated PBMCs suggests a preferential involvement of catecholaminergic pathways in the functional modulation of activated cells. These findings may help to better define the role of immunocompetent cell-derived CA in the neuroimmune network.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Calcium / metabolism*
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Catecholamines / biosynthesis*
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Cells, Cultured
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Chelating Agents / pharmacology
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Egtazic Acid / analogs & derivatives*
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Egtazic Acid / pharmacology
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Enzyme Inhibitors / pharmacology
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Gene Expression Regulation, Enzymologic / drug effects
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Gene Expression Regulation, Enzymologic / immunology
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Humans
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Leukocytes, Mononuclear / cytology
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Leukocytes, Mononuclear / drug effects
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Leukocytes, Mononuclear / enzymology*
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Neuroimmunomodulation / physiology
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Phytohemagglutinins / pharmacology*
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Protein Kinase C / antagonists & inhibitors
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Protein Kinase C / metabolism*
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RNA, Messenger / analysis
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Tyrosine 3-Monooxygenase / genetics
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Tyrosine 3-Monooxygenase / metabolism
Substances
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Catecholamines
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Chelating Agents
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Enzyme Inhibitors
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Phytohemagglutinins
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RNA, Messenger
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1,2-bis(2-aminophenoxy)ethane N,N,N',N'-tetraacetic acid acetoxymethyl ester
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Egtazic Acid
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Tyrosine 3-Monooxygenase
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Protein Kinase C
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Calcium