A family of secreted proteins contains homology to the cysteine-rich ligand-binding domain of frizzled receptors
| Autor: | Nancy A. Jenkins, Amir Rattner, Philip M. Smallwood, Jeremy Nathans, N. G. Copeland, Debra J. Gilbert, Jen Chih Hsieh |
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| Rok vydání: | 1997 |
| Předmět: |
Male
Signal peptide Frizzled DNA Complementary Molecular Sequence Data Wnt1 Protein Protein Sorting Signals Biology Receptors G-Protein-Coupled Mice Secreted frizzled-related protein 1 Proto-Oncogene Proteins Animals Drosophila Proteins Amino Acid Sequence RNA Messenger Peptide sequence Multidisciplinary Sequence Homology Amino Acid Wnt signaling pathway Chromosome Mapping Membrane Proteins LRP6 Biological Sciences Molecular biology Frizzled Receptors Cell biology Mice Inbred C57BL Membrane protein Female SFRP4 Protein Binding |
| Zdroj: | Proceedings of the National Academy of Sciences. 94:2859-2863 |
| ISSN: | 1091-6490 0027-8424 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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