TY - JOUR
T1 - Dialdehyde-GDP blocks activity of cytosolic components of neutrophil NADPH oxidase
AU - Klinger, Eti
AU - Aviram, Irit
N1 - Funding Information:
Dr. H.L. Malech for probing our blots with his anti-p47 and antibodies. This research was supported in part by The U.S.-Israel Science Foundation.
PY - 1991/5/31
Y1 - 1991/5/31
N2 - Superoxide production by neutrophil NADPH oxidase activated in a cell-free system consisting of plasma membranes, cytosol and arachidonate is enhanced by nonhydrolyzable analogs of GTP and reduced by GDP. To characterize the interaction of guanine nucleotides with the system, dialdehyde analogs of GTP and GDP (oGTP and oGDP) were employed. oGDP or oGTP caused an irreversible and dose dependent inactivation of NADPH oxidase-supporting cytosolic activity. Cytosol was fractionated on S and Q Sepharose ion exchange columns into three fractions, combinations of which synergistically supported activation of NADPH oxidase. Two fractions shown by immunoblotting to contain the oxidase-linked p47 and p67 proteins were inactivated by oGDP. Labeling with [α-32P]-oGTP lead to incorporation of the label into several proteins.
AB - Superoxide production by neutrophil NADPH oxidase activated in a cell-free system consisting of plasma membranes, cytosol and arachidonate is enhanced by nonhydrolyzable analogs of GTP and reduced by GDP. To characterize the interaction of guanine nucleotides with the system, dialdehyde analogs of GTP and GDP (oGTP and oGDP) were employed. oGDP or oGTP caused an irreversible and dose dependent inactivation of NADPH oxidase-supporting cytosolic activity. Cytosol was fractionated on S and Q Sepharose ion exchange columns into three fractions, combinations of which synergistically supported activation of NADPH oxidase. Two fractions shown by immunoblotting to contain the oxidase-linked p47 and p67 proteins were inactivated by oGDP. Labeling with [α-32P]-oGTP lead to incorporation of the label into several proteins.
UR - http://www.scopus.com/inward/record.url?scp=0025820373&partnerID=8YFLogxK
U2 - 10.1016/0006-291X(91)92012-9
DO - 10.1016/0006-291X(91)92012-9
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AN - SCOPUS:0025820373
SN - 0006-291X
VL - 177
SP - 504
EP - 510
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 1
ER -