Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2 Pt 2 Suppl 1
pubmed:dateCreated
1975-7-7
pubmed:abstractText
Monooxygenases require NADPH and molecular oxygen during the metabolism of numerous endogenous hydrophobic substrates and carcinogenic and toxic exogenous chemicals. The complexity of these membrane-bound multicomponent drug-metabolizing enzyme systems is reviewed. What "aryl hydrocarbon (benzo[a]pyrene) hydroxylase activity" actually represents is reviewed and discussed. At least two forms of the hydroxylase activity exist and we suggest that they are associated with different molecular species of membrane-bound CO-binding hemoprotein (i.e., they are associated with different enzyme active-sties). At least two, and probably more than two, nonlinked loci are responsible for the genetic expression of new cytochrome P1450 formation and aryl hydrocarbon hydroxylase induction--and the stimulation of 10 other monooxygenase "activities"--in the mouse treated with certain aromatic hydrocarbons. The individual variability of hydroxylase activity in an inbred and in a random-bred strain of micr is illustrated. The basal hydroxylase activity appears to be inherited differently from the aromatic hydrocarbon-inducible hydroxylase activity. The potent inducer 2,3,7,8-tetrachlorodibenzo-p-dioxin can stimulate increases in these hepatic monooxygenase activities and p1450 formation in so-called "nonresponsive" mice, whereas inducers such as beta-naphthoflavone and 3-methylcholanthrene cannot. Thus, the genetically "nonresponsive" micr apparently possess the structural and regulatory genes necessary for expression of these inducible monooxygenase activities and associated new formation of cytochrome P1450. We suggest that a mutation has occurred in the "nonresponsive" inbred strains that results in production of an inducer-binding receptor having a diminished affinity for aromatic hydrocarbons.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0021-9541
pubmed:author
pubmed:issnType
Print
pubmed:volume
85
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
393-414
pubmed:dateRevised
2005-11-17
pubmed:meshHeading
pubmed-meshheading:1091656-Animals, pubmed-meshheading:1091656-Aryl Hydrocarbon Hydroxylases, pubmed-meshheading:1091656-Benzopyrenes, pubmed-meshheading:1091656-Crosses, Genetic, pubmed-meshheading:1091656-Cytochrome P-450 Enzyme System, pubmed-meshheading:1091656-Enzyme Induction, pubmed-meshheading:1091656-Enzyme Inhibitors, pubmed-meshheading:1091656-Genes, pubmed-meshheading:1091656-Genes, Regulator, pubmed-meshheading:1091656-Hydroxylation, pubmed-meshheading:1091656-Liver, pubmed-meshheading:1091656-Mice, pubmed-meshheading:1091656-Mice, Inbred Strains, pubmed-meshheading:1091656-Microsomes, Liver, pubmed-meshheading:1091656-Mitomycins, pubmed-meshheading:1091656-Models, Biological, pubmed-meshheading:1091656-Multienzyme Complexes, pubmed-meshheading:1091656-Oxygenases, pubmed-meshheading:1091656-Receptors, Drug, pubmed-meshheading:1091656-Tetrachlorodibenzodioxin
pubmed:year
1975
pubmed:articleTitle
Genetic expression of aryl hydrocarbon hydroxylase activity in the mouse.
pubmed:publicationType
Journal Article, Review