Michael Waterman
Faculty Member
Last active: 2/12/2015

A keratinocyte-specific epoxygenase, CYP2B12, metabolizes arachidonic acid with unusual selectivity, producing a single major epoxyeicosatrienoic acid.

Keeney DS, Skinner C, Wei S, Friedberg T, Waterman MR
J Biol Chem. 1998 273 (15): 9279-84

PMID: 9535921 · DOI:10.1074/jbc.273.15.9279

The CYP monooxygenase, CYP2B12, is the first identified skin-specific cytochrome P450 enzyme. It is characterized by high, constitutive expression in an extrahepatic tissue, the sebaceous glands of cutaneous tissues. It is expressed exclusively in a subset of differentiated keratinocytes called sebocytes, as demonstrated by Northern blot analysis, in situ hybridization, and polymerase chain reaction. The onset of its expression coincides with the morphological appearance of sebaceous glands in the neonatal rat. Recombinant CYP2B12 produced in Escherichia coli epoxidizes arachidonic acid to 11,12- and 8,9-epoxyeicosatrienoic acids (80 and 20% of total metabolites, respectively). The identification of arachidonic acid as a substrate for this skin-specific CYP monooxygenase suggests an endogenous function in keratinocytes in the generation of bioactive lipids and intracellular signaling.

MeSH Terms (16)

8,11,14-Eicosatrienoic Acid Animals Animals, Newborn Arachidonic Acid Cloning, Molecular Cytochrome P-450 Enzyme System Escherichia coli Keratinocytes Organ Specificity Rats Rats, Sprague-Dawley Recombinant Proteins Sebaceous Glands Skin Substrate Specificity Transcription, Genetic

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