Regular ArticleCYP3A4 Gene Polymorphisms Influence Testosterone 6β-hydroxylation
References (33)
- et al.
Human liver microsomal steroid metabolism: identification of the major microsomal steroid hormone 6 β-hydroxylase cytochrome P-450 enzyme
Arch. Biochem. Biophys.
(1988) - et al.
Distinct effects of phenobarbital and its N-methylated derivative on liver cytochrome P450 induction
Arch. Biochem. Biophys.
(1996) - et al.
Analysis of four residues within substrate recognition site 4 of human cytochrome P450 3A4: role in steroid hydroxylase activity and a-naphthoflavone stimulation
Arch. Biochem. Biohys.
(1998) - et al.
Highresolution crystal structure of cytochrome P450cam
J. Mol. Biol.
(1987) - et al.
The 2.6-crystal structure of Pseudomonas putida cytochrome P-450
J. Biol. Chem.
(1985) - et al.
Mammalian microsomal cytochrome P450 monooxygenase: structural adaptations for membrane binding and functional diversity
Mol. Cell.
(2000) Substrate recognition sites in cytochrome P450 family 2 (CYP2) proteins inferred from comparative analyses of amino acid and coding nucleotide sequences
J. Biol. Chem.
(1992)- et al.
Engineering microsomal cytochrome P450 2C5 to be a soluble, monomeric enzyme. Mutations that alter aggregation, phospholipid dependence of catalysis, and membrane binding
J. Biol. Chem.
(2000) Structure, Mechanism and Biochemistry
- et al.
Evidence for cytochrome P-450NF, the nifedipine oxidase, being the principal enzyme involved in the bioactivation of aflatoxins in human liver
Proc. Natl. Acad. Sci. U S A
(1989)
Non-invasive tests of CYP3A enzymes
Pharmacogenetics
Use of in vitro and in vivo data to estimate the likelihood of metabolic pharmacokinetic interactions
Clin. Pharmacokinet.
Pharmacogenomics: Translating Functional Genomics into Rational Therapeutics
Science
Characterization of an allelic variant in the nifedipine-specific element of CYP3A4: ethnic distribution and implications for prostate cancer risk. Mutations in brief no. 191. Online
Hum Mutat.
CYP3A4 allelic variants with amino acid substitutions in exons 7 and 12: evidence for an allelic variant with altered catalytic activity
Clinical Pharmacol. Ther.
Molecular genetics of the Finnish disease heritage
Hum. Mol. Genet.
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2019, Cell MetabolismCitation Excerpt :Additionally, levels of urea production were similarly unchanged (Figure S1A), and no obvious morphological alterations were observed in the various conditions (data not shown). Loss of CYP3A4 activity after RNAi-mediated silencing was further confirmed by exposure to a natural substrate, testosterone, which is mainly metabolized into 6β-hydroxytestosterone by this enzyme (Figure S1B) (Murayama et al., 2002; Waxman et al., 1988). A short incubation with testosterone was sufficient to differentiate between the function of the CYP3A4 siRNA treated and controls, with a 50% reduction in 6β-hydroxytestosterone production and secretion (Figure S1B).
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2019, Biomedicine and PharmacotherapyCitation Excerpt :The effect of missense mutations can only be assessed by functional expression of both the wild-type (WT) enzyme and the variant followed by activity studies using a variety of substrates. In this context it is worthwhile to mention that designations such as “activating mutant” or “inactivating mutant” need to be used with caution, as an increase in activity by an enzyme variant may well be restricted to certain substrates and might not be found with others [33–36]. By contrast, nonsense mutations almost always lead to inactive proteins, and the functional consequences of either gene amplifications or deletions are also rather foreseeable.
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