Cloning and characterization of a murine macrophage lipoxygenase

Freire-Moar, José; Alavi-Nassab, A.; Ng, May C.; Mulkins, Mary A.; Sigal, Elliott

doi:10.1016/0005-2760(94)00199-9

Cited by 52 publications

(43 citation statements)

References 22 publications

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“…These compounds were presumed to be formed from anandamide by lipoxygenase since we observed inhibition of the formation of the products by NDGA, a lipoxygenase inhibitor. In accordance with this finding, mouse macrophages were reported to express 12-lipoxygenase [48]. Therefore, the assay with anandamide was performed in the presence of NDGA (Fig.…”

Section: Resultssupporting

confidence: 60%

Involvement of N-acylethanolamine-hydrolyzing acid amidase in the degradation of anandamide and other N-acylethanolamines in macrophages

Sun

Tsuboi

Zhao

et al. 2005

Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biolog

100

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Bioactive N-acylethanolamines including the endocannabinoid anandamide are known to be hydrolyzed to fatty acids and ethanolamine by fatty acid amide hydrolase (FAAH). In addition, we recently cloned an isozyme termed ''N-acylethanolamine-hydrolyzing acid amidase (NAAA)'', which is active only at acidic pH [Tsuboi, Sun, Okamoto, Araki, Tonai, Ueda, J. Biol. Chem. 285 (2005) 11082 -11092]. However, physiological roles of NAAA remained unclear. Here, we examined a possible contribution of NAAA to the degradation of various Nacylethanolamines in macrophage cells. NAAA mRNA as well as FAAH mRNA was detected in several macrophage-like cells, including RAW264.7, and mouse peritoneal macrophages. The homogenates of RAW264.7 cells showed both the NAAA and FAAH activities which were confirmed with the aid of their respective specific inhibitors, N-cyclohexanecarbonylpentadecylamine (CCP) and URB597. As analyzed with intact cells, RAW264.7 cells and peritoneal macrophages degraded anandamide, N-palmitoylethanolamine, N-oleoylethanolamine, and Nstearoylethanolamine. Pretreatment of the cells with CCP or URB597 partially inhibited the degradation, and a combination of the two compounds caused more profound inhibition. In contrast, the anandamide hydrolysis in mouse brain appeared to be principally attributable to FAAH despite the expression of NAAA in the brain. These results suggested that NAAA and FAAH cooperatively degraded various N-acylethanolamines in macrophages. D

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Section: Resultssupporting

confidence: 60%

Involvement of N-acylethanolamine-hydrolyzing acid amidase in the degradation of anandamide and other N-acylethanolamines in macrophages

Sun

Tsuboi

Zhao

et al. 2005

Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biolog

100

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“…developed primates such as modern and extinct humans (25,32,33), as well as orangutans (22,34), express 15-lipoxygenating ALOX15 orthologs, whereas less developed mammals (21,(35)(36)(37)(38), including lower primates, have 12-lipoxygenating enzymes. Although no functional data are currently available for most mammalian ALOX15 orthologs, multiple sequence alignments suggested that their reaction specificity was altered during late primate evolution from 12-to 15-lipoxygenation (3).…”

Section: Significancementioning

confidence: 99%

Evolutionary alteration of ALOX15 specificity optimizes the biosynthesis of antiinflammatory and proresolving lipoxins

Adel

Karst

González‐Lafont

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

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ALOX15 (12/15-lipoxygenase) orthologs have been implicated in maturational degradation of intracellular organelles and in the biosynthesis of antiinflammatory and proresolving eicosanoids. Here we hypothesized that lower mammals (mice, rats, pigs) express 12-lipoxygenating ALOX15 orthologs. In contrast, 15-lipoxygenating isoforms are found in higher primates (orangutans, men), and these results suggest an evolution of ALOX15 specificity. To test this hypothesis we first cloned and characterized ALOX15 orthologs of selected Catarrhini representing different stages of late primate evolution and found that higher primates (men, chimpanzees) express 15-lipoxygenating orthologs. In contrast, lower primates (baboons, rhesus monkeys) express 12-lipoxygenating enzymes. Gibbons, which are flanked in evolution by rhesus monkeys (12-lipoxygenating ALOX15) and orangutans (15-lipoxygenating ALOX15), express an ALOX15 ortholog with pronounced dual specificity. To explore the driving force for this evolutionary alterations, we quantified the lipoxin synthase activity of 12-lipoxygenating (rhesus monkey, mouse, rat, pig, humIle418Ala) and 15-lipoxygenating (man, chimpanzee, orangutan, rabbit, ratPhe353Ala) ALOX15 variants and found that, when normalized to their arachidonic acid oxygenase activities, the lipoxin synthase activities of 15-lipoxygenating ALOX15 variants were more than fivefold higher (P < 0.01). Comparative molecular dynamics simulations and quantum mechanics/molecular mechanics calculations indicated that, for the 15-lipoxygenating rabbit ALOX15, the energy barrier for C13-hydrogen abstraction (15-lipoxygenation) was 17 kJ/mol lower than for arachidonic acid 12-lipoxygenation. In contrast, for the 12-lipoxygenating Ile418Ala mutant, the energy barrier for 15-lipoxygenation was 10 kJ/mol higher than for 12-lipoxygenation. Taken together, our data suggest an evolution of ALOX15 specificity, which is aimed at optimizing the biosynthetic capacity for antiinflammatory and proresolving lipoxins.

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“…LOs are known to form a widely distributed family of lipid peroxidizing enzymes that insert molecular oxygen stereospecifically into polyunsaturated fatty acids, such as arachidonic acid or linoleic acid [12]. Increasing numbers of certain mammalian LO isoforms (5-, 12-or 15-LO) have been identified in various tissues [13,14], but, for most of them, the biological function and significance remain unclear [12,14,15]. Sigal and co-workers [13] have cloned and characterized a 12-LO isoform from cardiac muscle, and 12(S)-HETE was found to be the main LO metabolite in ventricular cardiomyocytes [16].…”

Section: Introductionmentioning

confidence: 99%

“…Increasing numbers of certain mammalian LO isoforms (5-, 12-or 15-LO) have been identified in various tissues [13,14], but, for most of them, the biological function and significance remain unclear [12,14,15]. Sigal and co-workers [13] have cloned and characterized a 12-LO isoform from cardiac muscle, and 12(S)-HETE was found to be the main LO metabolite in ventricular cardiomyocytes [16]. This isoform has also been described in a variety of rat, mouse and human tissues [17].…”

Section: Introductionmentioning

confidence: 99%

Eicosanoids participate in the regulation of cardiac glucose transport by contribution to a rearrangement of actin cytoskeletal elements

Dransfeld

Rakatzi

Sasson

et al. 2001

Biochemical Journal

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Intact actin microfilaments are required for insulin-regulated glucose transporter isoform 4 (GLUT4) translocation to the plasma membrane. Lipoxygenase (LO) metabolites have recently been shown to contribute to the regulation of actin cytoskeleton rearrangement. In the present investigation, ventricular cardiomyocytes were used to study the effects of two structurally different LO inhibitors (esculetin and nordihydroguaiaretic acid) on insulin signalling events, glucose uptake, GLUT4 translocation and the actin network organization. Insulin stimulation increased glucose uptake 3-fold in control cells, whereas LO inhibition completely blocked this effect. This was paralleled by a slight reduction in the insulin-induced tyrosine phosphorylation of insulin receptor substrate (IRS)-1 and IRS-2. However, inhibition of 12-LO did not affect the association of phosphatidylinositol 3-kinase with IRS-1 and the phosphorylation of Akt\protein kinase B in response to insulin. Addition of 12(S)-

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Cloning and characterization of a murine macrophage lipoxygenase

Cited by 52 publications

References 22 publications

Involvement of N-acylethanolamine-hydrolyzing acid amidase in the degradation of anandamide and other N-acylethanolamines in macrophages

Involvement of N-acylethanolamine-hydrolyzing acid amidase in the degradation of anandamide and other N-acylethanolamines in macrophages

Evolutionary alteration of ALOX15 specificity optimizes the biosynthesis of antiinflammatory and proresolving lipoxins

Eicosanoids participate in the regulation of cardiac glucose transport by contribution to a rearrangement of actin cytoskeletal elements

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