Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
1996-7-2
pubmed:databankReference
pubmed:abstractText
A cDNA encoding a human cytochrome P450 arachidonic acid epoxygenase was isolated from a human liver cDNA library. Sequence analysis revealed that this 1,876-base pair cDNA contained an open reading frame and encoded a new 502-amino acid protein designated CYP2J2. Blot hybridization analysis of RNA prepared from human tissues revealed that CYP2J2 was highly expressed in the heart. Recombinant CYP2J2 protein was prepared using the baculovirus expression system and purified to near electrophoretic homogeneity. The enzyme metabolized arachidonic acid predominantly via olefin epoxidation to all four regioisomeric cis-epoxyeicosatrienoic acids (catalytic turnover 65 pmol of product formed/nmol of cytochrome P450/min at 30 degrees C). Epoxidation of arachidonic acid by CYP2J2 at the 14,15-olefin was highly enantioselective for (14R, 15S)-epoxyeicosatrienoic acid (76% optical purity). Immunoblotting of microsomal fractions prepared from human tissues using a polyclonal antibody raised against the recombinant hemoprotein confirmed primary expression of CYP2J2 protein in human heart. The in vivo significance of CYP2J2 was suggested by documenting the presence of epoxyeicosatrienoic acids in the human heart using gas chromatography/mass spectroscopy. Importantly, the chirality of CYP2J2 products matched that of the epoxyeicosatrienoic acid enantiomers present, in vivo, in human heart. We propose that CYP2J2 is one of the enzymes responsible for epoxidation of endogenous arachidonic acid pools in human heart and that epoxyeicosatrienoic acids may, therefore, play important functional roles in cardiac physiology.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
16
pubmed:volume
271
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3460-8
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:8631948-Amino Acid Sequence, pubmed-meshheading:8631948-Animals, pubmed-meshheading:8631948-Base Sequence, pubmed-meshheading:8631948-Cloning, Molecular, pubmed-meshheading:8631948-Cytochrome P-450 Enzyme System, pubmed-meshheading:8631948-DNA, Complementary, pubmed-meshheading:8631948-Gene Expression, pubmed-meshheading:8631948-Gene Library, pubmed-meshheading:8631948-Humans, pubmed-meshheading:8631948-Isomerism, pubmed-meshheading:8631948-Kinetics, pubmed-meshheading:8631948-Male, pubmed-meshheading:8631948-Molecular Sequence Data, pubmed-meshheading:8631948-Myocardium, pubmed-meshheading:8631948-Oligonucleotide Probes, pubmed-meshheading:8631948-Open Reading Frames, pubmed-meshheading:8631948-Organ Specificity, pubmed-meshheading:8631948-Oxygenases, pubmed-meshheading:8631948-Rabbits, pubmed-meshheading:8631948-Rats, pubmed-meshheading:8631948-Recombinant Proteins, pubmed-meshheading:8631948-Substrate Specificity
pubmed:year
1996
pubmed:articleTitle
Molecular cloning and expression of CYP2J2, a human cytochrome P450 arachidonic acid epoxygenase highly expressed in heart.
pubmed:affiliation
Laboratory of Pulmonary Pathobiology, NIEHS, National Institutes of Health, Research Triangle Park, North Carolina 27709, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.