A Keratinocyte-specific Epoxygenase, CYP2B12, Metabolizes Arachidonic Acid with Unusual Selectivity, Producing a Single Major Epoxyeicosatrienoic Acid
| Autor: | Shozuo Wei, Colin Skinner, Diane S. Keeney, Michael R. Waterman, Thomas Friedberg |
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| Rok vydání: | 1998 |
| Předmět: |
Keratinocytes
Epoxygenase Transcription Genetic In situ hybridization Epoxyeicosatrienoic acid Biochemistry Substrate Specificity Rats Sprague-Dawley Sebaceous Glands chemistry.chemical_compound 8 11 14-Eicosatrienoic Acid Cytochrome P-450 Enzyme System Escherichia coli medicine Animals Northern blot Cloning Molecular CYP2C8 Molecular Biology Skin Arachidonic Acid biology Cell Biology Monooxygenase Recombinant Proteins Rats medicine.anatomical_structure Animals Newborn chemistry Organ Specificity biology.protein Arachidonic acid Keratinocyte |
| Zdroj: | Journal of Biological Chemistry. 273:9279-9284 |
| ISSN: | 0021-9258 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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