This gene represents a member of the 'frizzled' gene family, which encode 7-transmembrane domain proteins that are receptors for Wnt signaling proteins. The protein encoded by this family member contains a signal peptide, a cysteine-rich domain in the N-terminal extracellular region, and seven transmembrane domains, but unlike other family members, this protein does not contain a C-terminal PDZ domain-binding motif. This protein functions as a negative regulator of the canonical Wnt/beta-catenin signaling cascade, thereby inhibiting the processes that trigger oncogenic transformation, cell proliferation, and inhibition of apoptosis. Alternative splicing results in multiple transcript variants, some of which do not encode a protein with a predicted signal peptide.
Frizzled-7 is a member of the Frizzled family of unconventional G-protein-coupled glycoprotein receptors for the Wnt signaling pathway . The Wnt genes encode a large family of glycoproteins that are essential in development and tissue maintenance . Like other Frizzled family members, Frizzled-7 contains a divergent N-terminal signal peptide (amino acid (aa) 1-32), a highly conserved extracellular cysteine-rich domain (CRD, aa 44-169), a variable-length linker region (aa 170-256), a seven-pass transmembrane region (aa 257-549), and a variable-length C-terminal cytoplasmic domain (aa 550-574) (1-3). The CRD, which comprises the binding site for Wnts and other ligands such as Syndecan 4 and fibronectin, spans about 130 amino acid residues and contains ten invariant cysteine residue
Frizzled-8 is one of at least ten seven-transmembrane (7TM) glycoproteins of the Frizzled family of Wnt receptors. Frizzled proteins are thought to be G-protein-coupled. Wnt engagement, with low density lipoprotein receptor-related proteins LRP-5 or LRP-6 acting as co-receptors, stabilizes beta -catenin and promotes gene transcription that is important in development and tissue maintenance. Component of the Wnt-Fzd-LRP5-LRP6 complex that triggers beta-catenin signaling through inducing aggregation of receptor-ligand complexes into ribosome-sized signalosomes. The beta-catenin canonical signaling pathway leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes. These ligands bind the extracellular CRD of Frizzled-8, blocking Wnt binding. The recombinant Frizzled-8 CRD has also been used to block Wnt signaling and inhibit growth of teratocarcinomas.
FRZB also known as sFRP-3, is a secreted protein containing a domain similar to the putative Wnt-binding region of the frizzled family of transmembrane receptors. FRZB is widely expressed in adult mammalian tissues. In the Xenopus gastrula, FRZB is regulated as a typical Spemann organizer component. FRZB also functions as a competitor for the cell-surface G-protein receptor Frizzled. It is espically important in embryonic development. Defects in FRZB gene can cause female-specific osteoarthritis (OA) susceptibility. FRZB may serve an important role in determining hip shape and may modify the relationship between hip shape and OA.
Glycoprotein hormones alpha chain, also known as CGA, belongs to the glycoprotein hormones subunit alpha family. The subunit of CGA is a heterodimer consists of a common alpha chain and a unique beta chain which confers biological specificity to thyrotropin, lutropin, follitropin and gonadotropin. It has positive regulation of cell migration, cell proliferation and transcription from RNA polymerase II promoter and participates in the peptide hormone processing and signal transduction.
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