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

  1. Author:
    Rattner, A.
    Hsieh, J. C.
    Smallwood, P. M.
    Gilbert, D. J.
    Copeland, N. G.
    Jenkins, N. A.
    Nathans, J.

  2. Author Address

    Nathans J JOHNS HOPKINS UNIV SCH MED DEPT MOL BIOL & GENET 805 PRECLIN TEACHING BLDG 725 N WOLFE ST BALTIMORE, MD 21205 USA JOHNS HOPKINS UNIV SCH MED DEPT MOL BIOL & GENET BALTIMORE, MD 21205 USA JOHNS HOPKINS UNIV SCH MED DEPT NEUROSCI BALTIMORE, MD 21205 USA JOHNS HOPKINS UNIV SCH MED DEPT OPHTHALMOL BALTIMORE, MD 21205 USA JOHNS HOPKINS UNIV SCH MED HOWARD HUGHES MED INST BALTIMORE, MD 21205 USA NCI FREDERICK CANC RES & DEV CTR MAMMALIAN GENET LAB ADV BIOSCI LAB BASIC RES PROGRAM FREDERICK, MD 21702 USA
    1. Year: 1997
  2. Journal: Proceedings of the National Academy of Sciences of the United States of America
    1. 94
    2. 7
    3. Pages: 2859-2863
  4. Type of Article: Article
  1. 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. [References: 37]

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