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J Biol Chem, Vol. 274, Issue 27, 19465-19472, July 2, 1999
From the In an effort to isolate novel growth factors, we
identified a human protein, designated Sk, that co-eluted with
Neuregulin during chromatographic separation of conditioned medium from
the SK-LMS-1 human leiomyosarcoma cell line. Degenerate
oligonucleotides based on amino-terminal sequence analysis of the
purified protein were used to isolate the corresponding cDNA from a
library generated from this cell line. Sk is a novel 266-amino acid
protein that contains a signal peptide sequence and two cysteine-rich
domains with no similarity to other known growth factors. A single
major 2-kilobase transcript was expressed in several embryonic tissues. Transfection of mammalian cells demonstrated that the protein was
secreted and expressed as a doublet of approximately 35 kDa. In
vitro translation and endoglycosylase analysis indicated that this doublet, which was also observed in cells expressing the endogenous protein, arises from posttranslational modification. A
search of the GenBankTM data base revealed a match of Sk
with Dkk-1, which is a novel secreted protein required for head
induction in amphibian embryos and a potent Wnt inhibitor. When
coexpressed with Wnt-2 in NIH3T3 cells, human Sk/Dkk-1 caused reversion
of Wnt-2 induced morphological alterations and inhibited the Wnt-2
induced increase in uncomplexed
Isolation and Biochemical Characterization of the Human Dkk-1
Homologue, a Novel Inhibitor of Mammalian Wnt Signaling
,,,
,,
Derald H. Ruttenberg Cancer Center, Mount
Sinai School of Medicine; New York, New York, 10029, the
¶ Holland Laboratory, American Red Cross,
Rockville, Maryland 20855, the Laboratory of Cellular and
Molecular Biology, National Cancer Institute,
Bethesda, Maryland 20892, and the ** Department of Experimental
Oncology, European Institute of Oncology, Milano 20141, Italy
-catenin levels. These results
provide biochemical evidence that human Sk/Dkk-1 antagonizes Wnt
signaling upstream of its effect on -catenin regulation.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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