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Volume 272, Number 13, Issue of March 28, 1997 pp. 8157-8160
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

COMMUNICATION:
Regulation of a Novel Gene Encoding a Lysyl Oxidase-related Protein in Cellular Adhesion and Senescence

(Received for publication, January 16, 1997)

Hiroshi Saito Dagger § , John Papaconstantinou Dagger , Hiroyuki Sato § and Samuel Goldstein §

From the Dagger  Department of Human Biological Chemistry and Genetics, University of Texas Medical Branch, Galveston, Texas 77555-0643 and the § Departments of Medicine and Biochemistry and Molecular Biology, University of Arkansas for Medical Sciences, and Geriatric Research Education and Clinic Center, John L. McClellan Memorial Veterans' Hospital, Little Rock, Arkansas 77205

We report here a novel cDNA clone with a predicted protein sequence similar to lysyl oxidase. This full-length cDNA clone of 3432 base pairs (WS9-14) was isolated from human fibroblasts on the basis of its overexpression in senescent cells. It encodes an 87-kDa polypeptide, whose protein is a member of the scavenger receptor cysteine-rich family, because it contains four scavenger receptor cysteine-rich domains that are found in several secreted or cell surface proteins. The WS9-14 protein has a 48% identity with both lysyl oxidase and lysyl oxidase-like protein at a region corresponding to exons 2-6, implying the existence of a lysyl oxidase gene family. The pattern of WS9-14 gene expression by fibroblasts parallels pro-collagen I-alpha 1 expression. Its mRNA level is induced by transforming growth factor beta -1 and indomethacin and inhibited by phorbol ester and retinoic acid. WS9-14 is abundantly expressed in all tumor cell lines examined that attach to culture dishes but not in cell lines that grow in suspension and is also up-regulated in senescent fibroblasts. These results suggest that WS9-14 gene encodes an extracellular protein that may be specifically involved in cell adhesion and senescence.


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