Phosphorylation of the Oxidase-Related 48K Phosphoprotein Family in the Unusual Autosomal Cytochrome-Negative and X-Linked Cytochrome-Positive Types of Chronic Granulomatous Disease

Activation of 32 P-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 phosphoryl...

Full description

Saved in:
Bibliographic Details
Published in:Blood 1988-08, Vol.72 (2), p.811-816
Main Authors: Okamura, Naoki, Malawista, Stephen E., Roberts, Robert L., Rosen, Henry, Ochs, Hans D., Babior, Bernard M., Curnutte, John T.
Format: Article
Language:English
Subjects:
Adult
Biological and medical sciences
Cytochromes - analysis
Female
Granulomatous Disease, Chronic - metabolism
Hematologic and hematopoietic diseases
Humans
Male
Medical sciences
Neutrophils - metabolism
Other diseases. Hematologic involvement in other diseases
Oxidoreductases - physiology
Phosphoproteins - metabolism
Phosphorylation
Citations: Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Activation of 32 P-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. © 1988 by Grune & Stratton, Inc.
ISSN:0006-4971
1528-0020
DOI:10.1182/blood.V72.2.811.811