Fig. 5.
Fig. 5. FcγRI-mediated activation of NADPH oxidase. / FcγRI-mediated activation of NADPH oxidase is dependent on PLD1 and not PLD2. (A) Superoxide production in response to FcγRI in control cells (XL control) compared with cells pretreated with antisense oligonucleotide (10 μM) to either PLD1 (XL a.s.PLD1) or PLD2 (a.s.PLD2). The trace results shown are typical from 3 separate experiments. (B) Superoxide production in response to FcγRIIa in control cells (XL FcγRIIa control) compared with cells pretreated with antisense (10 μM) to PLD1 (FcγRIIa a.s.PLD1) or PLD2 (FcγRIIa a.s.PL2). FcγRIIa was specifically aggregated by means of an anti-FcγRII–specific monoclonal antibody.7 The trace results shown are typical from 3 separate experiments.

FcγRI-mediated activation of NADPH oxidase.

FcγRI-mediated activation of NADPH oxidase is dependent on PLD1 and not PLD2. (A) Superoxide production in response to FcγRI in control cells (XL control) compared with cells pretreated with antisense oligonucleotide (10 μM) to either PLD1 (XL a.s.PLD1) or PLD2 (a.s.PLD2). The trace results shown are typical from 3 separate experiments. (B) Superoxide production in response to FcγRIIa in control cells (XL FcγRIIa control) compared with cells pretreated with antisense (10 μM) to PLD1 (FcγRIIa a.s.PLD1) or PLD2 (FcγRIIa a.s.PL2). FcγRIIa was specifically aggregated by means of an anti-FcγRII–specific monoclonal antibody.7 The trace results shown are typical from 3 separate experiments.

Close Modal

or Create an Account

Close Modal
Close Modal