NDLI: Tyrosine cross-linking of extracellular matrix is catalyzed by Duox, a multidomain oxidase/peroxidase with homology to the phagocyte oxidase subunit gp91phox

Content Provider	PubMed Central
Author	Edens, William A. Lisa, Sharling Cheng, Guangjie Shapira, Raymond Kinkade, Joseph M. Lee, Taehoon Edens, Heather A. Tang, Xuexin Cameron, Sullards Flaherty, Denise B. Benian, Guy M. Lambeth, J. David
Abstract	High molecular weight homologues of gp91phox, the superoxide-generating subunit of phagocyte nicotinamide adenine dinucleotide phosphate (NADPH)-oxidase, have been identified in human (h) and Caenorhabditis elegans (Ce), and are termed Duox for “dual oxidase” because they have both a peroxidase homology domain and a gp91phox domain. A topology model predicts that the enzyme will utilize cytosolic NADPH to generate reactive oxygen, but the function of the ecto peroxidase domain was unknown. Ce-Duox1 is expressed in hypodermal cells underlying the cuticle of larval animals. To investigate function, RNA interference (RNAi) was carried out in C. elegans. RNAi animals showed complex phenotypes similar to those described previously in mutations in collagen biosynthesis that are known to affect the cuticle, an extracellular matrix. Electron micrographs showed gross abnormalities in the cuticle of RNAi animals. In cuticle, collagen and other proteins are cross-linked via di- and trityrosine linkages, and these linkages were absent in RNAi animals. The expressed peroxidase domains of both Ce-Duox1 and h-Duox showed peroxidase activity and catalyzed cross-linking of free tyrosine ethyl ester. Thus, Ce-Duox catalyzes the cross-linking of tyrosine residues involved in the stabilization of cuticular extracellular matrix.
Related Links	http://dx.doi.org/10.1083/jcb.200103132
Ending Page	892
Page Count	14
Starting Page	879
File Format	PDF
ISSN	00219525
e-ISSN	15408140
Journal	The Journal of Cell Biology
Issue Number	4
Volume Number	154
Language	English
Publisher	The Rockefeller University Press
Publisher Date	2001-08-20
Access Restriction	Open
Rights Holder	The Rockefeller University Press
Subject Keyword	Cell Biology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Cell Biology Medicine

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