Document Detail

Absence of adrenaline neurons in the guinea pig brain: a combined immunohistochemical and high-performance liquid chromatography study.
MedLine Citation:
PMID:  2869455     Owner:  NLM     Status:  MEDLINE    
The distributions of catecholamine (CA) neurons in the medulla oblongata of the guinea pig and rat were compared using immunohistochemistry with rabbit antisera against the CA synthesizing enzymes, tyrosine hydroxylase (TH), dopamine-beta-hydroxylase (D beta H) and phenylethanolamine-N-methyltransferase (PNMT). TH and D beta H distributions were similar in the two species. In contrast, the central nervous systems of both normal and colchicine-treated guinea pigs failed to demonstrate immunoreactivity for PNMT, the synthetic enzyme for adrenaline. The concentrations of biogenic amines in the hypothalamus and medulla were determined in guinea pig and rat tissues by high-performance liquid chromatography with electrochemical detection. No adrenaline was detected in the guinea pig brain. Thus it appears that guinea pigs lack central neurons capable of synthesizing adrenaline.
P Cumming; M Von Krosigk; P B Reiner; E G McGeer; S R Vincent
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Neuroscience letters     Volume:  63     ISSN:  0304-3940     ISO Abbreviation:  Neurosci. Lett.     Publication Date:  1986 Jan 
Date Detail:
Created Date:  1986-04-03     Completed Date:  1986-04-03     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  7600130     Medline TA:  Neurosci Lett     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  125-30     Citation Subset:  IM    
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MeSH Terms
Adrenergic Fibers
Biogenic Amines / analysis
Brain / cytology*,  enzymology
Brain Chemistry
Chromatography, High Pressure Liquid
Dopamine beta-Hydroxylase / metabolism
Guinea Pigs
Immunoenzyme Techniques
Phenylethanolamine N-Methyltransferase / metabolism
Tyrosine 3-Monooxygenase / metabolism
Reg. No./Substance:
0/Biogenic Amines; EC 3-Monooxygenase; EC beta-Hydroxylase; EC N-Methyltransferase

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

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