Document Detail


Differential regulation of phenylethanolamine N-methyltransferase expression in two distinct subpopulations of bovine chromaffin cells.
MedLine Citation:
PMID:  8752129     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Chromaffin cells were isolated from bovine adrenal glands and fractionated into two distinct subpopulations by density gradient centrifugation on Percoll. Cells in the more dense fraction stored epinephrine (E) as their predominant catecholamine (81% of total catecholamines), contained high levels of phenylethanolamine N-methyltransferase (PNMT) activity, and exhibited intense PNMT immunoreactivity. This population of chromaffin cells was termed the E-rich cell population. Cells in the less dense fraction, the norepinephrine (NE)-rich cell population, stored predominantly NE (75% of total catecholamines). Although the NE-rich cells had only 3% as much PNMT activity as did the E-rich cells, 20% of the NE-rich cells were PNMT immunoreactive. This suggested that the PNMT-positive cells in the NE-rich cell cultures contained less PNMT per cell than did E-rich cells and may not be typical adrenergic cells. The regulation of PNMT mRNA levels and PNMT activity in primary cultures of E-rich and NE-rich cells was compared. At the time the cells were isolated, PNMT mRNA levels in NE-rich cells were approximately 20% of those in E-rich cells; within 48 h in culture, PNMT mRNA in both populations declined to almost undetectable levels. Treatment with dexamethasone increased PNMT mRNA levels and PNMT activity in both populations. In E-rich cells, dexamethasone restored PNMT mRNA to the level seen in freshly isolated cells and increased PNMT activity twofold. In NE-rich cells, dexamethasone increased PNMT mRNA to levels twice those found in freshly isolated cells and increased PNMT activity sixfold. Cycloheximide blocked the effects of dexamethasone on PNMT mRNA expression in NE-rich cells but had little effect in E-rich cells. Angiotensin II, forskolin, and phorbol 12,13-dibutyrate elicited large increases in PNMT mRNA levels in E-rich cells but had no effect in NE-rich cells. Our data suggest that PNMT expression is regulated differently in the two chromaffin cell subpopulations.
Authors:
A L Cahill; A L Eertmoed; D Mangoura; R L Perlman
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Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Journal of neurochemistry     Volume:  67     ISSN:  0022-3042     ISO Abbreviation:  J. Neurochem.     Publication Date:  1996 Sep 
Date Detail:
Created Date:  1996-10-02     Completed Date:  1996-10-02     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  2985190R     Medline TA:  J Neurochem     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  1217-24     Citation Subset:  IM    
Affiliation:
Department of Pediatrics, University of Chicago, IL 60637, USA.
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MeSH Terms
Descriptor/Qualifier:
Adrenal Glands / cytology,  enzymology
Animals
Antibody Specificity
Cattle
Cell Separation
Cells, Cultured / chemistry,  cytology,  enzymology
Centrifugation
Chromaffin System / chemistry,  cytology*,  enzymology
Colloids
Cycloheximide / pharmacology
Dexamethasone / pharmacology
Epinephrine / analysis,  secretion
Gene Expression / drug effects
Immunohistochemistry
Norepinephrine / analysis,  secretion
Phenylethanolamine N-Methyltransferase / genetics,  immunology,  metabolism*
Povidone
Protein Synthesis Inhibitors / pharmacology
RNA, Messenger / analysis
Silicon Dioxide
Tyrosine 3-Monooxygenase / metabolism
Grant Support
ID/Acronym/Agency:
HD 09402/HD/NICHD NIH HHS; T32 GM 07839/GM/NIGMS NIH HHS; T32 NS 07195/NS/NINDS NIH HHS
Chemical
Reg. No./Substance:
0/Colloids; 0/Protein Synthesis Inhibitors; 0/RNA, Messenger; 50-02-2/Dexamethasone; 51-41-2/Norepinephrine; 51-43-4/Epinephrine; 65455-52-9/Percoll; 66-81-9/Cycloheximide; 7631-86-9/Silicon Dioxide; 9003-39-8/Povidone; EC 1.14.16.2/Tyrosine 3-Monooxygenase; EC 2.1.1.28/Phenylethanolamine N-Methyltransferase

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


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