A Family of Secreted Proteins Contains Homology to the Cysteine-Rich Ligand-Binding Domain of Frizzled Receptors

This paper describes the identification of a new family of mammalian genes that encode secreted proteins containing homology to the cysteine-rich ligand-binding domain found in the frizzled family of transmembrane receptors. The secreted frizzled-related proteins (sFRPs) are approximately 30 kDa in...

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Bibliographic Details
Published in:	Proceedings of the National Academy of Sciences - PNAS Vol. 94; no. 7; pp. 2859 - 2863
Main Authors:	Rattner, Amir, Hsieh, Jen-Chih, Smallwood, Philip M., Gilbert, Debra J., Copeland, Neil G., Jenkins, Nancy A., Nathans, Jeremy
Format:	Journal Article
Language:	English
Published:	United States National Academy of Sciences of the United States of America 01-04-1997 National Acad Sciences The National Academy of Sciences of the USA
Subjects:	Amino Acid Sequence Animals Biological Sciences Cell lines Chromosome Mapping Chromosomes Complementary DNA DNA, Complementary Drosophila Drosophila Proteins Female Frizzled Receptors Genes Genetic loci Genomics Kidney cells Male Membrane Proteins - genetics Mice Mice, Inbred C57BL Molecular Sequence Data Protein Binding Protein Sorting Signals - genetics Proto-Oncogene Proteins - genetics Proto-Oncogene Proteins - metabolism Receptors, G-Protein-Coupled RNA RNA, Messenger - genetics Sequence Homology, Amino Acid Wnt1 Protein
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Summary:	This paper describes the identification of a new family of mammalian genes that encode secreted proteins containing homology to the cysteine-rich ligand-binding domain found in the frizzled family of transmembrane receptors. The secreted frizzled-related proteins (sFRPs) are approximately 30 kDa in size, and each contains a putative signal sequence, a frizzled-like cysteine-rich domain, and a conserved hydrophilic carboxy-terminal domain. The sFRPs are not the products of differential splicing of the known frizzled genes. Glycosylphosphatidylinositol-anchored derivatives of sFRP-2 and sFRP-3 produced in transfected human embryonic kidney cells confer cell-surface binding by the Drosophila Wingless protein. These observations suggest that sFRPs may function in vivo to modulate Wnt signaling, or, alternatively, as novel ligands for as yet unidentified receptors.
Bibliography:	ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2 To whom reprint requests should be addressed at: 805 Preclinical Teaching Building, 725 North Wolfe Street, Johns Hopkins University School of Medicine, Baltimore, MD 21205. Jeremy Nathans
ISSN:	0027-8424 1091-6490
DOI:	10.1073/pnas.94.7.2859