Document Detail


Immunohistochemical localization of catecholamine biosynthetic enzymes in the adrenal gland of the domestic fowl (Gallus domesticus).
MedLine Citation:
PMID:  20634527     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The present study investigated the cellular localization of 3 catecholamine biosynthetic enzymes, tyrosine hydroxylase (TH), dopamine beta-hydroxylase (DBH), and phenylethanolamine N-methyltransferase (PNMT) to identify and analyze the localization of norepinephrine (NE) and epinephrine (E) cells in the adrenal gland in the chicken using peroxidase-antiperoxidase immunohistochemical techniques. Tyrosine hydroxylase immunoreactivity (IR) was observed in almost all adrenal medullary cells of the adult chicken. Dopamine beta-hydroxylase IR coincided with that of TH. Many medullary cells also exhibited PNMT IR, but PNMT-immunonegative cells were also observed. Tyrosine hydroxylase IR was localized in the E- and NE-containing cells, but PNMT IR was localized only in the E-containing cells. Approximately 69% of medullary cells were E-containing, and the remaining were NE-containing cells. The ratio of E- and NE-containing cells between the subcapsular and central zone was statistically significant (P < 0.01). Although cortical cells of the adrenal gland did not show TH-, DBH-, or PNMT-positive reactions, ganglia close to the adrenal gland showed TH, DBH, and PNMT immunoreactivities. These findings indicated the cellular localization of 3 catecholamine-biosynthesizing enzymes in chicken adrenal medulla and suggest that the majority of medullary cell are E-containing cells. The ratio of E cells to NE cells varies among the 3 zones in the adrenal glands of the chicken.
Authors:
A K M H Kober; M Aoyama; S Sugita
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Poultry science     Volume:  89     ISSN:  0032-5791     ISO Abbreviation:  Poult. Sci.     Publication Date:  2010 Aug 
Date Detail:
Created Date:  2010-07-16     Completed Date:  2010-12-03     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0401150     Medline TA:  Poult Sci     Country:  United States    
Other Details:
Languages:  eng     Pagination:  1709-15     Citation Subset:  IM    
Affiliation:
Department of Animal Science, Faculty of Agriculture, Utsunomiya University, Utsunomiya-shi, Tochigi 321-8505, Japan.
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MeSH Terms
Descriptor/Qualifier:
Adrenal Medulla / anatomy & histology,  enzymology,  metabolism*
Animals
Catecholamines / biosynthesis*
Chickens / metabolism*
Dopamine beta-Hydroxylase / metabolism
Epinephrine / metabolism
Female
Immunoenzyme Techniques
Immunohistochemistry
Male
Norepinephrine / metabolism
Phenylethanolamine N-Methyltransferase / metabolism
Tyrosine 3-Monooxygenase / metabolism
Chemical
Reg. No./Substance:
0/Catecholamines; 51-41-2/Norepinephrine; 51-43-4/Epinephrine; EC 1.14.16.2/Tyrosine 3-Monooxygenase; EC 1.14.17.1/Dopamine beta-Hydroxylase; 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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