Spermine suppresses the activation of human neutrophil NADPH oxidase in cell-free and semi-recombinant systems

Ogata, Kenichi; Nishimoto, Naoya; Uhlinger, David J.; Igarashi, Kazuei; Takeshita, M; Tamura, Minoru

doi:10.1042/bj3130549

Cited by 25 publications

(21 citation statements)

References 36 publications

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“…These results strongly suggest that Spd acts as a cellular membrane protectant against chill-induced lipid peroxidation through prevention of superoxide-generating NADPH oxidase activation. Kitada et al (1979) and Ogata et al (1996) have observed that Spd and Spm inhibit NADPH oxidase activity in rat liver microsomes and human neutrophils, respectively. Kramer and Wang (1989) indicated that PAs could protect membrane lipids from chill-induced peroxidation.…”

Section: Discussionmentioning

confidence: 99%

“…It is known that PAs are capable of protecting membranes against ROSinduced lipid peroxidation (Kitada et al, 1979;Tadolini et al, 1984;Tadolini, 1988). Ogata et al (1996) recently found that PAs inhibited the activity of the superoxide-generating NADPH oxidases in human neutrophils. Their results provoked us to investigate the possible involvement of PAs in the chilling tolerance of cucumber cultivars.…”

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confidence: 99%

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Involvement of Polyamines in the Chilling Tolerance of Cucumber Cultivars

2000

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The possible involvement of polyamines (PAs) in the chilling tolerance of cucumber (Cucumis sativus L. cv Jinchun No. 3 and cv Suyo) was investigated. Plants with the first expanded leaves were exposed to 3°C or 15°C in the dark for 24 h (chilling), and then transferred to 28°C/22°C under a 12-h photoperiod for another 24 h (rewarming). Chilling-tolerant cv Jinchun No. 3 showed a marked increase of free spermidine (Spd) in leaves, once during chilling and again during rewarming. Putrescine increased significantly during rewarming, but the increase of spermine was slight. Any of these PAs did not increase in chilling-sensitive cv Suyo during either period. PA-biosynthetic enzyme activities appear to mediate these differences between cultivars. Pretreatment of Spd to cv Suyo prevented chill-induced increases in the contents of hydrogen peroxide in leaves and activities of NADPH oxidases and NADPH-dependent superoxide generation in microsomes and alleviated chilling injury. Pretreatment of methylglyoxal-bis-(guanylhydrazone), a PA biosynthesis inhibitor, to chilled cv Jinchun No. 3 prevented Spd increase and enhanced microsomal NADPH oxidase activity and chilling injury. The results suggest that Spd plays important roles in chilling tolerance of cucumber, probably through prevention of chill-induced activation of NADPH oxidases in microsomes.

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Section: Discussionmentioning

confidence: 99%

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confidence: 99%

Involvement of Polyamines in the Chilling Tolerance of Cucumber Cultivars

2000

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“…Von besonderem Interesse war die Identifizierung einer 14fachen Abnahme in der Expression von Ornithindekarboxylase, dem für die Produktion von Spermin und Spermidin verantwortlichen Antizym. Die ubiquitären Polyamine, welche in ihren höchsten Konzentrationen im Seminalplasma gefunden werden, sind Schlüs-selregulatoren der Spermatogenese [64] und Spermatidchromatinkondensation [65]; sie fungieren als Protektoren [66] und Radikalenfänger [67] der ROS. Interessanterweise verfügen sie auch über klar abgegrenzte AGE-Inhibitionseigenschaften, indem sie insbesondere Histone [68] schützen.…”

Section: Der Einfluss Des Dm Auf Die Spermatogeneseunclassified

Einfluss des Diabetes mellitus auf die Fertilität des Mannes

Mallidis¹,

Agbaje

McClure

et al. 2011

Urologe

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Whilst diabetes mellitus is known to have many systemic complications, male infertility, beyond impotence, retrograde ejaculation and hypogonadism, has not been widely recognised to be one of them. Due to the paucity of studies and inconsistencies regarding the condition's impact on semen quality, few fertility specialists consider the condition noteworthy. As a consequence little information exists as to its prevalence amongst infertile men. Recently the prevailing view has been challenged by findings showing that diabetes induces subtle molecular changes that are important for sperm quality and function. Diabetic men have been found to have a significantly higher percentage of sperm with nuclear DNA damage, a factor known to be associated with compromised fertility and increased miscarriage rates. The mechanism by which this diabetes-related sperm nDNA damage occurs remains unknown. The identification of high levels of advanced glycation end products (AGEs) and their receptor (RAGE) throughout the male reproductive tract coupled to changes in testicular metabolite levels and spermatogenic gene expression suggest that glycation may play an integral role in oxidative stress which in turn causes sperm nDNA damage. As glycation is a normal consequence of life and has been implicated in DNA fragmentation in a variety of seemingly unconnected conditions, it may constitute a common mechanism for the damage seen in sperm DNA.

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“…The separation of neutrophils and the fractionation of PM were performed as previously described (24).…”

Section: Methodsmentioning

confidence: 99%

Fused p47 and p67 Truncations Efficiently Reconstitute NADPH Oxidase with Higher Activity and Stability Than the Individual Components

Ebisu

Nagasawa

et al. 2001

Journal of Biological Chemistry

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Activation of the neutrophil NADPH oxidase occurs via assembly of the cytosolic regulatory proteins p47phox , p67 phox , and Rac with the membrane-associated flavocytochrome b 558 . Following cell-free activation, enzymatic activity is highly labile (Tamura, M., Takeshita, M., Curnutte, J. T., Uhlinger, D. J., and Lambeth, J. D. (1992) J. Biol. Chem. 267, 7529 -7538). To try to stabilize the activity and investigate the nature of the complex, fusion proteins between p47N-(1-286) and p67N-(1-210) were constructed. In a cell-free system, a fusion protein, p67N-p47N, had an 8-fold higher efficiency and produced a higher activity than the individual proteins, and also resulted in an 8-fold improved efficiency for Rac and a lowered K m for NADPH. O 2 . generating activity was remarkably stabilized by using p67N-p47N. The cytosolic proteins fused in the opposite orientation, p47N-p67N, showed similar activity and stability as individual proteins, but with a 4-fold improved efficiency compared with the individual cytosolic factors. In the system efficiency for Rac and affinity for NADPH were also higher than those with the nonfused components. Interestingly, the p67N-p47N showed nearly full activation in the absence of an anionic amphifile in a cell-free system containing cytochrome b 558 relipidated with phosphatidylinositol-or phosphatidylserine-enriched phospholipid mixtures. From the results we consider multiple roles of anionic amphifiles in a cell-free activation, which could be substituted by our system. The fact that a fusion produces a more stable complex indicates that interactions among components determine the longevity of the complex. Based on the findings we propose a model for the topology among p47N, p67N, and cytochrome b 558 in the active complex.The superoxide-generating phagocyte NADPH oxidase (Phox/Nox-2) functions in host defense against microbial infection (1, 2). The enzyme is dormant in resting cells and becomes active upon cell stimulation. The activation is thought to occur via assembly of cytosolic components, p47 phox (p47), 1 p67 phox (p67), and Rac with the membrane-associated flavocytochrome b 558 (cyt. b 558 ), which consists of p22 phox (p22) and gp91 phox (gp91) although the structure of the complex has remained unclear (3-6). Other two factors p40 phox and rap1A are also assumed to be involved in the enzyme regulation although they are not essential for the activation.The activated NADPH oxidase is highly labile, complicating investigations of the subunit structure and preventing isolation of the active enzyme complex (7). In a previous study (8) using a cell-free system consisting of cytosol and plasma membrane (PM) we showed that the stability is dramatically improved by chemical cross-linking, and suggested that the deactivation is caused by dissociation of proteins from the complex. Crosslinking was useful in stabilizing the oxidase, but it was difficult to isolate the active complex because the cross-linked complex resisted solubilization (8). We have also attempted cross-linkin...

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Spermine suppresses the activation of human neutrophil NADPH oxidase in cell-free and semi-recombinant systems

Cited by 25 publications

References 36 publications

Involvement of Polyamines in the Chilling Tolerance of Cucumber Cultivars

Involvement of Polyamines in the Chilling Tolerance of Cucumber Cultivars

Einfluss des Diabetes mellitus auf die Fertilität des Mannes

Fused p47 and p67 Truncations Efficiently Reconstitute NADPH Oxidase with Higher Activity and Stability Than the Individual Components

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