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J. Biol. Chem., Vol. 275, Issue 46, 36341-36349, November 17, 2000
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From the Lysyl oxidase is an extracellular enzyme that
controls the maturation of collagen and elastin. Lysyl oxidase and
collagen III often show similar expression patterns in fibrotic
tissues. Therefore, we investigated the influence of lysyl oxidase
overexpression on the promoter activity of human COL3A1 gene. Our
results showed that when COS-7 cells overexpressed the mature form of
lysyl oxidase, the activity of the human COL3A1 promoter was increased
up to an average of 12 times when tested by luciferase reporter assay. The effect was specific, because other promoters were not affected. Moreover, lysyl oxidase effect was abolished by
Lysyl Oxidase Activates the Transcription Activity of Human
Collagene III Promoter
POSSIBLE INVOLVEMENT OF Ku ANTIGEN*
,,,,,
Department of Nephrology and
§ Fondo Malattie Renali del Bambino, Gaslini Children's
Hospital and ¶ Laboratory of Molecular Genetics, Gaslini
Children's Hospital, Genova and Department of Oncology, Biology and
Genetics, University of Genova, 16147 Genova, Italy
-aminopropionitrile, a specific inhibitor of its catalytic activity. Electrophoretic mobility shift assay showed a binding activity in the region from 
101
to 77 that was significantly increased by lysyl oxidase overexpression. The binding was specifically competed by the cold probe, and the mutagenesis of this region abolished both the binding activity in gel retardation and lysyl oxidase stimulation of COL3A1 promoter in transfection experiments. We identified the binding activity as Ku antigen in its two components: Ku80 and Ku70. This study
suggests a new coordinated mechanism by which lysyl oxidase might
control the development of fibrosis.
*
The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Laboratory of
Nephrology, Istituto G. Gaslini, Largo G. Gaslini, 5, 16147 Genova, Italy. Tel.: 39-010-380742; Fax: 39-010-395214; E-mail:
a-dido@usa.net.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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