Title of article :
4-Hydroxynonenal inhibits Na+-K+-ATPase
Author/Authors :
Werner G. Siems، نويسنده , , Sharon J. Hapner، نويسنده , , Frederik J. G. M. Van Kuijk، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 1996
Pages :
9
From page :
215
To page :
223
Abstract :
4-Hydroxynonenal binds rapidly to Na+-K+-ATPase, and this was accompanied by a decrease in measurable sulfhydryl groups and a loss of enzyme activity. The I50 value for Na+-K+-ATPase inhibition by 4-hydroxynonenal was found to be 120 μM. Although the sulfhydryl groups could be completely restored with β-mercaptoethanol during the reaction of the Na+K+-ATPase-HNE-adduct, the Na+-K+-ATPase activity was only partially restored by this reducing agent. A combination of hydroxylamine and β-mercaptoethanol yielded the greatest recovery of enzyme activity, 85% of original. Thus, 4-hydroxynonenal binding to Na+-K+-ATPase led to an irreversible decrease of enzyme activity under the conditions employed. It is hypothesized that 4-hydroxynonenal reacts with sulfhydryls at sites on the enzyme that are inaccessible by β-mercaptoethanol. Furthermore, evidence was obtained that 4-hydroxynonenal reacts with other amino acids such as lysine to form adducts that also interfere with protein function.
Keywords :
Na+-K+-ATPase , 4-hydroxynonenal , Aldehydes , Lipid peroxidation , free radicals , sulfhydryl groups , ?-Mercapto-ethanol
Journal title :
Free Radical Biology and Medicine
Serial Year :
1996
Journal title :
Free Radical Biology and Medicine
Record number :
517254
Link To Document :
بازگشت