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Murine epidermal lipoxygenase ( Aloxe ) encodes a 12‐lipoxygenase isoform 1
Author(s) -
Kinzig Andreas,
Fürstenberger Gerhard,
Bürger Friederike,
Vogel Sonja,
Müller-Decker Karin,
Mincheva Antoaneta,
Lichter Peter,
Marks Friedrich,
Krieg Peter
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(96)01517-7
Subject(s) - lipoxygenase , microbiology and biotechnology , gene isoform , epidermis (zoology) , complementary dna , recombinant dna , arachidonic acid , open reading frame , biology , biochemistry , arachidonate 5 lipoxygenase , chemistry , gene , peptide sequence , enzyme , anatomy
Using a combination of conventional screening procedures and polymerase chain reaction cloning, we have isolated a cDNA encoding an epidermis‐type 12‐lipoxygenase ( e12 ‐lipoxygenase) from mouse epidermis. The open reading frame corresponds to a protein of 662 amino acids and was found to be 99.8% identical to the ORF of an epidermal lipoxygenase gene Aloxe , described recently [Van Dijk et al. (1995) Biochim. Biophys. Acta 1259, 4–8]. When expressed in human embryonic kidney cells the recombinant protein could be shown to synthesize 12( S )‐HETE from arachidonic acid. By fluorescence in situ hybridization the e12 ‐lipoxygenase gene was localized to chromosome band 11 B1–B3.