Document Detail

The source of heme for vascular heme oxygenase I: heme uptake in rat aorta.
MedLine Citation:
PMID:  15181458     Owner:  NLM     Status:  MEDLINE    
During the last decade, heme oxygenase (HO) and carbon monoxide (CO) have garnered substantial research interest in terms of cell and organ regulation, especially as they bear on the central nervous system, organ transplantation, and the cardiovascular system. While the enzymatic mechanism, substrates, and products of HO are well known, it is not clear whether the cardiovascular system derives its supply of the heme substrate through de novo synthesis or uptake from the extracellular milieu. The objective of the present study was to test the latter possibility in rat aorta and to determine the influence of plasma proteins that bind heme in vivo, viz. hemopexin and albumin. Aortic tissue was exposed to [14C]heme in vitro, and the concentration and time dependence of heme uptake was assessed. The presence of hemopexin or albumin in the incubation medium dramatically decreased heme uptake by the aorta. Heme uptake by aortic tissue was not altered after induction of HO-1, which would be expected to increase tissue heme demand. In summary, the rat, isolated aorta was capable of obtaining heme from its external milieu, but this was obtunded in the presence of the plasma proteins hemopexin or albumin. For normal physiological situations, heme uptake may not be a usual source of substrate for vascular HO and hemoenzymes such as nitric oxide synthase, soluble guanylyl cyclase, and cyclooxygenase.
Loc Bui; Kimberly Rish; Kinga Jaronczyk; Stephane Bourque; Brian E McLaughlin; James F Brien; Gerald S Marks; Ann Smith; Kanji Nakatsu
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Canadian journal of physiology and pharmacology     Volume:  82     ISSN:  0008-4212     ISO Abbreviation:  Can. J. Physiol. Pharmacol.     Publication Date:  2004 Apr 
Date Detail:
Created Date:  2004-06-07     Completed Date:  2005-05-26     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0372712     Medline TA:  Can J Physiol Pharmacol     Country:  Canada    
Other Details:
Languages:  eng     Pagination:  209-17     Citation Subset:  IM    
Department of Pharmacology and Toxicology, Queen's University, Kingston, ON, Canada.
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MeSH Terms
Aorta, Thoracic / cytology,  drug effects,  metabolism*
Carbon Radioisotopes / diagnostic use
Heme / metabolism*
Heme Oxygenase (Decyclizing) / drug effects,  metabolism*
Heme Oxygenase-1
Hemopexin / pharmacology
Muscle, Smooth, Vascular / cytology,  drug effects,  metabolism*
Rats, Sprague-Dawley
S-Nitroso-N-Acetylpenicillamine / pharmacology
Serum Albumin / pharmacology
Reg. No./Substance:
0/Carbon Radioisotopes; 0/Serum Albumin; 14875-96-8/Heme; 79032-48-7/S-Nitroso-N-Acetylpenicillamine; 9013-71-2/Hemopexin; EC Oxygenase (Decyclizing); EC Oxygenase-1

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

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