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    Biochim Biophys Acta. 1995 Jan 3;1254(1):112-6.

    Cloning and characterization of a murine macrophage lipoxygenase.

    Freire-Moar J, Alavi-Nassab A, Ng M, Mulkins M, Sigal E.

    Syntex Discovery Research, Department of Inflammation Biology and Immunology, Palo Alto, CA 94304.

    We have isolated a murine macrophage cDNA encoding a 12-lipoxygenase, that represents the homolog of the human 15-lipoxygenase. The predicted amino acid sequence of this lipoxygenase is highly similar to the rat 12-lipoxygenase isolated from brain and human 15-lipoxgenase. The recombinant enzyme expressed in Cos-7 cells oxidizes arachidonic acid to 12- and 15-HETE with a profile similar to that obtained from peritoneal macrophages. A polyclonal antibody generated against a putative peptide recognizes a 75 kDa protein in cell extracts from mouse peritoneal macrophages and transfected Cos-7 cells. The lipoxygenase cDNA hybridizes to a 2.5 kb mRNA present in peritoneal macrophages, lung, spleen, heart and liver. RT-PCR analysis indicates that the same lipoxygenase is expressed in mouse reticulocytes. A partial genomic clone for this lipoxygenase has also been characterized. Southern blot analysis of mouse genomic DNA indicates that this is a single copy gene.

    PMID: 7811740 [PubMed - indexed for MEDLINE]

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