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Originally published In Press as doi:10.1074/jbc.M004014200 on August 16, 2000

J. Biol. Chem., Vol. 275, Issue 45, 35540-35547, November 10, 2000
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Structure-Expression Relationships of the 15-kDa Selenoprotein Gene
POSSIBLE ROLE OF THE PROTEIN IN CANCER ETIOLOGY*

Easwari KumaraswamyDagger , Andrey Malykh§, Konstantin V. Korotkov, Sergei Kozyavkin§, Yajun Hu||, So Yeon Kwon**, Mohamed E. MoustafaDagger , Bradley A. CarlsonDagger , Marla J. BerryDagger Dagger , Byeong J. Lee**, Dolph L. HatfieldDagger , Alan M. Diamond||, and Vadim N. Gladyshev§§

From the Dagger  Section on the Molecular Biology of Selenium, Basic Research Laboratory, NCI, National Institutes of Health, Bethesda, Maryland 20892, § Fidelity Systems, Inc., Gaithersburg, Maryland 20879,  Department of Biochemistry, University of Nebraska, Lincoln, Nebraska 68588, || University of Illinois, Chicago, Illinois 60612, ** Laboratory of Molecular Genetics, IMBG, Seoul National University, Seoul 151-742, Korea, and Dagger Dagger  Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts 02115

Selenium has been implicated in cancer prevention, but the mechanism and possible involvement of selenoproteins in this process are not understood. To elucidate whether the 15-kDa selenoprotein may play a role in cancer etiology, the complete sequence of the human 15-kDa protein gene was determined, and various characteristics associated with expression of the protein were examined in normal and malignant cells and tissues. The 51-kilobase pair gene for the 15-kDa selenoprotein consisted of five exons and four introns and was localized on chromosome 1p31, a genetic locus commonly mutated or deleted in human cancers. Two stem-loop structures resembling selenocysteine insertion sequence elements were identified in the 3'-untranslated region of the gene, and only one of these was functional. Two alleles in the human 15-kDa protein gene were identified that differed by two single nucleotide polymorphic sites that occurred within the selenocysteine insertion sequence-like structures. These 3'-untranslated region polymorphisms resulted in changes in selenocysteine incorporation into protein and responded differently to selenium supplementation. Human and mouse 15-kDa selenoprotein genes manifested the highest level of expression in prostate, liver, kidney, testis, and brain, and the level of the selenoprotein was reduced substantially in a malignant prostate cell line and in hepatocarcinoma. The expression pattern of the 15-kDa protein in normal and malignant tissues, the occurrence of polymorphisms associated with protein expression, the role of selenium in differential regulation of polymorphisms, and the chromosomal location of the gene may be relevant to a role of this protein in cancer.

* This work was supported by a grant from the Cancer Research Foundation of America (to V. N. G) and in part by a grant from the American Institute for Cancer Research (to A. M. D.).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.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF288992 (human 15-kDa protein gene), AF288991 (extended human 15-kDa protein cDNA), and AF288740 (mouse 15-kDa protein cDNA).

§§ To whom correspondence should be addressed: Dept. of Biochemistry, The Beadle Center, University of Nebraska, Lincoln, NE 68588-0664. Tel.: 402-472-4948; Fax: 402-472-7842; E-mail: vgladyshev1@unl.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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