Characterization of the 47-kilodalton autosomal chronic granulomatous disease protein: tissue-specific expression and transcriptional control by retinoic acid

Rodaway, Adam R and Teahan, Carmel G. and Casimir, Colin M. and Segal, Anthony W. and Bentley, David L. (1990) Characterization of the 47-kilodalton autosomal chronic granulomatous disease protein: tissue-specific expression and transcriptional control by retinoic acid. Molecular and cellular biology, 10 (10). pp. 5388-5396. ISSN 0270-7306

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Official URL: http://mcb.asm.org/cgi/content/abstract/10/10/5388

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Abstract

A full-length cDNA clone was isolated for the 47-kilodalton (kDa) subunit of the NADPH oxidase system, whose absence is responsible for the most common form of autosomally inherited chronic granulomatous disease (CGD). It encodes a 44.7-kDa polypeptide, which contains two src homology (SH3) domains and several possible sites for phosphorylation by protein kinase C. We speculate that the SH3 domains may interact with the Rap1 protein associated with cytochrome b-245 (M.T. Quinn, C.A. Parkes, L. Walker, S. Orkin, M. Dinauer, and A. Jesaitis, Nature [London] 342:198-200, 1989). An antiserum raised to the predicted C terminus of the protein detects a polypeptide with an apparent molecular mass of 47 kDa in normal neutrophil granulocytes but not in those from patients with autosomal CGD. The antibody has been used to show that the protein associates with the vacuolar membrane and is phosphorylated in response to phorbol ester treatment. Analysis of a number of tissue types and cell lines shows that expression of the gene is confined to phagocytic cells and B lymphocytes. This observation suggests that patients with CGD may also have a defect in lymphocyte function. p47 protein and mRNA levels increase during retinoic acid-induced neutrophil differentiation of HL60 cells. Nuclear run-on transcription assays show that the gene for p47 is induced at the transcriptional level in a cycloheximide-insensitive manner. These data indicate that this gene is a primary target for regulation by retinoic acid.

Item Type:Article
Research Areas:Middlesex University Schools and Centres > School of Science and Technology > Natural Sciences
Middlesex University Schools and Centres > School of Science and Technology > Natural Sciences > Molecular Biology group
Citations on ISI Web of Science:73
ID Code:3302
Deposited On:02 Dec 2009 09:07
Last Modified:10 Dec 2014 16:29

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