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Inhibition of the induction of nitric oxide synthase by spermine is modulated by aldehyde dehydrogenase.

Abstract：

:The observation that spermine inhibits the endotoxin (lipopolysaccharide; LPS) induced production of nitric oxide (NO) in macrophages has been ascribed to the conversion of SP to active metabolites by the action of enzymes, such as diamine oxidases, found, for example, in bovine sera. Inhibitory effect is also observed with the oxidised metabolite of spermine, spermine dialdehyde (SDA). Inhibition appears to be at the level of induction of the inducible isoform of NO synthase (iNOS). Here we show that the activity of endogenous aldehyde dehydrogenase present in the cells influences the degree of inhibition seen with either spermine or SDA. Most significantly, inhibition of aldehyde dehydrogenase activity greatly increases (100 fold) the ability of spermine to inhibit the production of nitrite by LPS- induced macrophages. This is presumably by preserving aldehyde metabolites of spermine and thus increasing its action on the induction of iNOS. Thus, inhibition of aldehyde dehydrogenase activity in vitro or in vivo may be a useful approach to enhance the inhibitory effect of polyamines or polyamine aldehydes on iNOS induction.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Southan GJ,Szabó C,Thiemermann C

doi

10.1006/bbrc.1994.2374

subject

Has Abstract

pub_date

1994-09-30 00:00:00

pages

1638-44

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(84)72374-6

journal_volume

203

pub_type

杂志文章

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