Document Detail


Role of PKA and PKC in histamine H1 receptor-mediated activation of catecholamine neurotransmitter synthesis.
MedLine Citation:
PMID:  16978782     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Activation of the histamine H1 receptor stimulates tyrosine hydroxylase (TH) to increase catecholamine neurotransmitter synthesis in mammalian brain and adrenal tissues. Histamine non-selectively activates both H1-linked phospholipase (PL) C/inositol phosphates (IP)/diacylglycerol (DAG) signaling and adenylyl cyclase (AC)/adenosine 3',5'-cyclic monophosphate (cAMP) signaling, confounding determination of signaling events involved in H(1)-mediated TH activation. This research uses two new functionally-selective H1 agonists, cis-PAB and trans-PAT, that selectively activate H1/PLC/IP/DAG and H1/AC/cAMP signaling, respectively, to characterize H(1)-mediated activation of TH in rat striatum and bovine adrenal chromaffin (BAC) cells. Histamine, cis-PAB, and trans-PAT produced a two-fold maximal TH activation by an H1 receptor mechanism in rat striatum and BAC cells. Histamine is more potent and efficacious in BAC cells (EC50 approximately 0.2 microM, Emax approximately 200% basal) versus rat striatum (EC50 approximately 0.4 microM; Emax approximately 150%). Cis-PAB and trans-PAT are more potent in rat striatum (EC50 approximately 0.1 microM for both agonists) versus BAC cells (EC50 approximately 1.0 microM for both), with similar efficacy in both preparations (Emax approximately 160% for both agonists). Signaling studies in BAC cells revealed that protein kinase (PK) A but not PKC is involved in H1 -mediated TH activation by trans-PAT and histamine, while, both PKA and PKC are involved for cis-PAB. Results for cis-PAB suggest H1/PLC/IP/DAG/PKC signaling activates PKA, downstream of cAMP formation, indicating apparent direct activation of PKA by PKC.
Authors:
Nader H Moniri; Raymond G Booth
Publication Detail:
Type:  In Vitro; Journal Article; Research Support, N.I.H., Extramural     Date:  2006-09-15
Journal Detail:
Title:  Neuroscience letters     Volume:  407     ISSN:  0304-3940     ISO Abbreviation:  Neurosci. Lett.     Publication Date:  2006 Oct 
Date Detail:
Created Date:  2006-09-25     Completed Date:  2006-11-27     Revised Date:  2014-09-19    
Medline Journal Info:
Nlm Unique ID:  7600130     Medline TA:  Neurosci Lett     Country:  Ireland    
Other Details:
Languages:  eng     Pagination:  249-53     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Adenylate Cyclase / physiology
Adrenal Medulla / cytology
Animals
Bicyclo Compounds / pharmacology
Catecholamines / biosynthesis*
Cattle
Chromaffin Cells / metabolism
Corpus Striatum / metabolism
Cyclic AMP / physiology
Cyclic AMP-Dependent Protein Kinases / physiology*
Diglycerides / physiology
Dimethylamines / pharmacology
Enzyme Activation
Histamine Agonists / pharmacology
Inositol Phosphates / physiology
Male
Protein Kinase C / physiology*
Rats
Rats, Sprague-Dawley
Receptors, Histamine H1 / physiology*
Signal Transduction
Tetrahydronaphthalenes / pharmacology
Type C Phospholipases / physiology
Tyrosine 3-Monooxygenase / metabolism
Grant Support
ID/Acronym/Agency:
MH068655/MH/NIMH NIH HHS; R01 MH068655/MH/NIMH NIH HHS
Chemical
Reg. No./Substance:
0/5-phenyl-7-dimethylamino-5,6,7,8-tetrahydro-9H-benzocycloheptane; 0/Bicyclo Compounds; 0/Catecholamines; 0/Diglycerides; 0/Dimethylamines; 0/Histamine Agonists; 0/Inositol Phosphates; 0/Receptors, Histamine H1; 0/Tetrahydronaphthalenes; 152786-06-6/1-phenyl-3-dimethylamino-1,2,3,4-tetrahydronaphthalene; E0399OZS9N/Cyclic AMP; EC 1.14.16.2/Tyrosine 3-Monooxygenase; EC 2.7.11.11/Cyclic AMP-Dependent Protein Kinases; EC 2.7.11.13/Protein Kinase C; EC 3.1.4.-/Type C Phospholipases; EC 4.6.1.1/Adenylate Cyclase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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