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J Biol Chem, Vol. 274, Issue 25, 17777-17788, June 18, 1999
From the A cDNA encoding a new cytochrome P450 was
isolated from a mouse liver library. Sequence analysis reveals that
this 1,886-base pair cDNA encodes a 501-amino acid polypeptide that
is 69-74% identical to CYP2J subfamily P450s and is designated
CYP2J5. Recombinant CYP2J5 was co-expressed with NADPH-cytochrome P450
oxidoreductase in Sf9 cells using a baculovirus system.
Microsomal fractions of CYP2J5/NADPH-cytochrome P450
oxidoreductase-transfected cells metabolize arachidonic acid to 14,15-, 11,12-, and 8,9-epoxyeicosatrienoic acids and 11- and
15-hydroxyeicosatetraenoic acids (catalytic turnover, 4.5 nmol of
product/nmol of cytochrome P450/min at 37 °C); thus CYP2J5 is
enzymologically distinct. Northern analysis reveals that CYP2J5
transcripts are most abundant in mouse kidney and present at lower
levels in liver. Immunoblotting using a polyclonal antibody against a
CYP2J5-specific peptide detects a protein with the same electrophoretic
mobility as recombinant CYP2J5 most abundantly in mouse kidney
microsomes. CYP2J5 is regulated during development in a tissue-specific
fashion. In the kidney, CYP2J5 is present before birth and reaches
maximal levels at 2-4 weeks of age. In the liver, CYP2J5 is absent
prenatally and during the early postnatal period, first appears at 1 week, and then remains relatively constant. Immunohistochemical
staining of kidney sections with anti-human CYP2J2 IgG reveals that
CYP2J protein(s) are present primarily in the proximal tubules and
collecting ducts, sites where the epoxyeicosatrienoic acids are known
to modulate fluid/electrolyte transport and mediate hormonal action.
In situ hybridization confirms abundant CYP2J5 mRNA
within tubules of the renal cortex and outer medulla.
Epoxyeicosatrienoic acids are endogenous constituents of mouse kidney
thus providing direct evidence for the in vivo metabolism
of arachidonic acid by the mouse renal epoxygenase(s). Based on these
data, we conclude that CYP2J5 is an enzymologically distinct,
developmentally regulated, protein that is localized to specific
nephron segments and contributes to the oxidation of endogenous renal
arachidonic acid pools. In light of the well documented effects of
epoxyeicosatrienoic acids in modulating renal tubular transport
processes, we postulate that CYP2J5 products play important functional
roles in the kidney.
Molecular Cloning, Enzymatic Characterization, Developmental
Expression, and Cellular Localization of a Mouse Cytochrome P450
Highly Expressed in Kidney
,,,
,, and
Laboratories of Pulmonary
Pathobiology, § Structural Biology, and
¶ Experimental Pathology, NIEHS, National Institutes of
Health, Research Triangle Park, North Carolina 27709 and the
Department of Medicine, Vanderbilt University,
Nashville, Tennessee 37232
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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