A family of secreted proteins contains homology to the cysteine-rich ligand-binding domain of frizzled receptors

Amir Rattner, Jen Chih Hsieh, Philip M. Smallwood, Debra J. Gilbert, Neil G. Copeland, Nancy A. Jenkins, Jeremy Nathans

Research output: Contribution to journalArticlepeer-review

Abstract

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.

Original languageEnglish (US)
Pages (from-to)2859-2863
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume94
Issue number7
DOIs
StatePublished - Apr 1 1997

ASJC Scopus subject areas

  • General

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