|
|
 Previous Article | Table of Contents | Next Article 
Phosphorylation of the oxidase-related 48K phosphoprotein family in the
unusual autosomal cytochrome-negative and X-linked cytochrome-positive
types of chronic granulomatous disease
N Okamura, SE Malawista, RL Roberts, H Rosen, HD Ochs, BM Babior and JT Curnutte
Department of Basic and Clinical Research, Research Institute of Scripps
Clinic, La Jolla, CA 92037.
Activation of 32P-loaded neutrophils with phorbol myristate acetate causes
the labeling of a family of three 48K proteins that focus near neutral pH.
The relationship between these phosphoproteins and the activation of the
respiratory burst has been supported by the previous finding that
phosphorylation was defective in the two most common types of chronic
granulomatous disease (CGD): X-linked cytochrome-negative (X/-) and
autosomal cytochrome-positive (A/+). In this report, these studies have now
been extended to the rare A/- and X/+ forms of the disease. In all three
patients with A/- CGD examined, the two most acidic 48K proteins failed to
undergo enhanced phosphorylation in response to phorbol stimulation, a
finding similar to that seen in X/- patients. In contrast, neutrophils from
two patients with X/+ CGD appeared to phosphorylate the neutral 48K
proteins in a normal fashion. It thus appears that the different
phosphorylation patterns seen in chronic granulomatous disease are a
reflection of the genetic heterogeneity of this disorder. These findings
lend further support to the conclusion that the 48K phosphoprotein family
is related to the respiratory burst, although not necessarily in a
straightforward manner.
Volume 72,
Issue 2,
pp. 811-816,
08/01/1988
Copyright © 1988 by The American Society of Hematology
 CiteULike  Connotea  Del.icio.us  Digg  Reddit  Technorati What's this?
This article has been cited by other articles:
|
|
|
|
 
F. R. DeLeo, L.-A. H. Allen, M. Apicella, and W. M. Nauseef
NADPH Oxidase Activation and Assembly During Phagocytosis
J. Immunol.,
December 15, 1999;
163(12):
6732 - 6740.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
L.-A. H. Allen, F. R. DeLeo, A. Gallois, S. Toyoshima, K. Suzuki, and W. M. Nauseef
Transient Association of the Nicotinamide Adenine Dinucleotide Phosphate Oxidase Subunits p47phox and p67phox With Phagosomes in Neutrophils From Patients With X-Linked Chronic Granulomatous Disease
Blood,
May 15, 1999;
93(10):
3521 - 3530.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
J. L. Freeman and J. D. Lambeth
NADPH Oxidase Activity Is Independent of p47phox in Vitro
J. Biol. Chem.,
September 13, 1996;
271(37):
22578 - 22582.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
A. R. Cross, P. G. Heyworth, J. Rae, and J. T. Curnutte
A Variant X-linked Chronic Granulomatous Disease Patient (X91[IMAGE]) with Partially Functional Cytochrome b
J. Biol. Chem.,
April 7, 1995;
270(14):
8194 - 8200.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
D. S. Regier, D. G. Greene, S. Sergeant, A. J. Jesaitis, and L. C. McPhail
Phosphorylation of p22phox Is Mediated by Phospholipase D-dependent and -independent Mechanisms. CORRELATION OF NADPH OXIDASE ACTIVITY AND p22phox PHOSPHORYLATION
J. Biol. Chem.,
September 8, 2000;
275(37):
28406 - 28412.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
