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CFR

[cysteine-rich FGF receptor] Also: CFR-1 [cysteine-rich FGF receptor-1]. A 150 kDa integral membrane glycoprotein purified originally as an FGF-binding protein from embryonic chick (Burrus and Olwin, 1989). The rat protein has been cloned as a Golgi-specific protein designated MG-160 (Gonatas et al, 1995; Mourelatos et al, 1996). GLG1 [Golgi complex-localized glycoprotein-1] and a splice variant, termed GLG2, are two isoforms that show different cell- and species-specific expression patterns (Ahn et al, 2005). The human homolog has been identified as ESL-1 [E-selectin ligand-1] but requires (1,3)-fucosylation for binding (Steegmaier et al, 1995; Zollner and Vestweber, 1996). Steegmaier et al (1997) have reported that ESL-1 is located in the Golgi as well as on microvilli on the cell surface. Antoine et al (2009) have shown that a substantial proportion of CFR is secreted after successive endoproteolytical processing of the protein in the Golgi complex. The secreted protein binds to heparan sulphate proteoglycan and can trap fibroblast growth factors and thereby directly compete with tyrosine kinase receptors for FGF binding.

CFR has been shown to bind FGF-1 (aFGF), FGF-2 (bFGF), FGF-4 (hst), (Burrus et al, 1992), and FGF-3 (int-2) (Kohl et al, 2000). It shows no recognizable sequence homology to the four known FGF tyrosine kinase receptors, FGFR1, FGFR2, FGFR3, FGFR4, or FGF proteoglycan coreceptors. CFR may be involved in intracellular trafficking of aFGF, bFGF, int-2, and hst, because its presence alters the levels of intracellular aFGF and bFGF (Burrus et al, 1992; Zuber et al, 1997; Kohl et al, 2000). CFR does not bind PDGF-BB, EGF, insulin, or IGF-2, but forms a secreted complex with TGF-beta (Burrus et al, 1992; Olofsson et al, 1997).

Yamaguchi et al (2003) have reported that high levels of CFR are found in low-grade astrocytomas and low levels in malignant astrocytomas.

LAST MODIFIED: December 2009

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