The structural biology of the FGF19 subfamily

Advances in Experimental Medicine and Biology

Volumn 728, Issue , 2012, Pages 1-24

  Beenken, Andrew ^a   Mohammadi, Moosa ^a  

^a NEW YORK UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA KLOTHO PROTEIN; BETA KLOTHO PROTEIN; FIBROBLAST GROWTH FACTOR 1; FIBROBLAST GROWTH FACTOR 19; FIBROBLAST GROWTH FACTOR 21; FIBROBLAST GROWTH FACTOR 23; FIBROBLAST GROWTH FACTOR 4; FIBROBLAST GROWTH FACTOR 8; FIBROBLAST GROWTH FACTOR 9; FIBROBLAST GROWTH FACTOR RECEPTOR; FIBROBLAST GROWTH FACTOR RECEPTOR 1C; HEPARAN SULFATE; KERATINOCYTE GROWTH FACTOR; KLOTHO PROTEIN; UNCLASSIFIED DRUG; BETA GLUCURONIDASE; FIBROBLAST GROWTH FACTOR;

ARTICLE; BINDING AFFINITY; BINDING SITE; CRYSTAL STRUCTURE; ENDOCRINE FUNCTION; EPITHELIAL MESENCHYMAL TRANSITION; HUMAN; NONHUMAN; PARACRINE SIGNALING; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CARBOHYDRATE INTERACTION; PROTEIN DEGRADATION; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; RECEPTOR BINDING; REGULATORY MECHANISM; SIGNAL TRANSDUCTION; STRUCTURE ACTIVITY RELATION; TISSUE SPECIFICITY; AMINO ACID SEQUENCE; ANIMAL; CHEMISTRY; CLASSIFICATION; CYTOLOGY; ENDOCRINE SYSTEM; METABOLISM; MOLECULAR GENETICS; REVIEW;

AMINO ACID SEQUENCE; ANIMALS; ENDOCRINE SYSTEM; FIBROBLAST GROWTH FACTORS; GLUCURONIDASE; HUMANS; MOLECULAR SEQUENCE DATA; SIGNAL TRANSDUCTION; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 84859519654     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-4614-0887-1_1     Document Type: Article

References (140)

1. Eswarakumar VP, Lax I, Schlessinger J. Cellular signaling by fibroblast growth factor receptors. Cytokine Growth Factor Rev 2005; 16(2):139-149
2. Johnson DE, Williams LT. Structural and functional diversity in the FGF receptor multigene family. Adv Cancer Res 1993; 60:1-41
3. Mohammadi M, Olsen SK, Ibrahimi OA. Structural basis for fibroblast growth factor receptor activation. Cytokine Growth Factor Rev 2005; 16(2):107-137
4. Itoh N, Ornitz DM. Evolution of the Fgf and Fgfr gene families. Trends Genet 2004;20(11):563-569
5. Itoh N, Ornitz DM. Functional evolutionary history ofthe mouse Fgfgene family. Dev Dyn2008; 237(1):18-27
6. Popovici C, Roubin R, Coulier F et al. An evolutionary history of the FGF superfamily. Bioessays 2005; 27(8):849-857
7. Colvin JS, Green RP, Schmahl J et al. Male-to-female sex reversal in mice lacking fibroblast growth factor 9. Cell 2001; 104(6):875-889
8. Goriely A, Hansen RM, Taylor IB et al. Activating mutations in FGFR3 and HRAS reveal a shared genetic origin for congenital disorders and testicular tumors. Nat Genet 2009; 41(11):1247-1252
9. Goriely A, McVean GA, Rojmyr M et al. Evidence for selective advantage of pathogenic FGFR2 mutations in the male germ line. Science 2003; 301(5633):643-646
10. Kato S, Sekine K. FGF-FGFR signaling invertebrate organogenesis. Cell Mol Biol (Noisy-le-grand) 1999; 45(5):631-638
11. Niswander L, Tickle C, Vogel A et al. FGF-4 replaces the apical ectodermal ridge and directs outgrowth and patterning of the limb. Cell 1993; 75(3):579-587
12. Baker RE, Schnell S, Maini PK. A clock and wavefront mechanism for somite formation. Dev Biol 2006; 293(1):116-126
13. Dale JK, Malapert P, Chal J et al. Oscillations of the snail genes in the presomitic mesoderm coordinate segmental patterning and morphogenesis in vertebrate somitogenesis. Dev Cell 2006; 10(3):355-366
14. Dubrulle J, McGrew MJ, Pourquie O. FGF signaling controls somite boundary position and regulates segmentation clock control of spatiotemporal Hox gene activation. Cell 2001; 106(2):219-232
15. Pourquie O. The chick embryo: a leading model in somitogenesis studies. Mech Dev 2004; 121(9):1069-1079
16. Sawada A, Shinya M, Jiang YJ et al. Fgf/MAPK signalling is a crucial positional cue in somite boundary formation. Development2001; 128(23):4873-4880
17. Colvin JS, White AC, Pratt SJ et al. Lung hypoplasia and neonatal death in Fgf9-null mice identify this gene as an essential regulator of lung mesenchyme. Development 2001; 128(11):2095-2106
18. Itoh N. The Fgf families in humans, mice and zebrafish: their evolutional processes and roles in development, metabolism and disease. Biol Pharm Bull 2007; 30(10):1819-1825
19. Lu SY, Sheikh F, Sheppard PC et al. FGF-16 is required for embryonic heart development. Biochem Biophys Res Commun 2008; 373(2):270-274
20. Sugi Y, Ito N, Szebenyi G et al. Fibroblast growth factor (FGF)-4 can induce proliferation of cardiac cushion mesenchymal cells during early valve leaflet formation. Dev Biol 2003; 258(2):252-263
21. OLeary DD, Chou SJ, Sahara S. Area patterning of the mammalian cortex. Neuron 2007; 56(2):252-269
22. Kharitonenkov A, Shiyanova TL, Koester A et al. FGF-21 as a novel metabolic regulator. J Clin Invest 2005; 115(6):1627-1635
23. Fu L, John LM, Adams SH et al. Fibroblast growth factor 19 increases metabolic rate and reverses dietary and leptin-deficient diabetes. Endocrinology 2004; 145(6):2594-2603
24. Holt JA, Luo G, Billin AN et al. Definition of a novel growth factor-dependent signal cascade for the suppression ofbile acidbiosynthesis. Genes Dev 2003; 17(13):1581-1591
25. Tomlinson E, Fu L, John L et al. Transgenic mice expressing human fibroblast growth factor-19 display increased metabolic rate and decreased adiposity. Endocrinology 2002; 143(5):1741-1747
26. Yu X, White KE. FGF23 and disorders of phosphate homeostasis. Cytokine Growth Factor Rev 2005; 16(2):221-232
27. Goetz R, Dover K, Laezza F et al. Crystal structure of a fibroblast growth factor homologous factor (FHF) defines a conserved surface on FHFs for binding and modulation of voltage-gated sodium channels. J Biol Chem 2009; 284(26):17883-17896
28. Goldfarb M. Fibroblast growth factor homologous factors: evolution, structure and function. Cytokine Growth Factor Rev 2005; 16(2):215-220
29. Olsen SK, Garbi M, Zampieri N et al. Fibroblast growth factor (FGF) homologous factors share structural but not functional homology with FGFs. J Biol Chem 2003; 278(36):34226-34236
30. Eriksson AE, Cousens LS, Weaver LH et al. Three-dimensional structure of human basic fibroblast growth factor. Proc Natl Acad Sci USA 1991; 88(8):3441-3445
31. Zhang JD, Cousens LS, Barr PJ et al. Three-dimensional structure of human basic fibroblast growth factor, a structural homolog of interleukin 1 beta. Proc Natl Acad Sci USA 1991; 88(8):3446-3450
32. Zhu X, Komiya H, Chirino A et al. Three-dimensional structures of acidic and basic fibroblast growth factors. Science 1991; 251(4989):90-93
33. Olsen SK, Li JY, Bromleigh C et al. Structural basis by which alternative splicing modulates the organizer activity of FGF8 in the brain. Genes Dev 2006; 20(2):185-198
34. Plotnikov AN, Hubbard SR, Schlessinger J et al. Crystal structures of two FGF-FGFR complexes reveal the determinants ofligand-receptor specificity. Cell 2000; 101(4):413-424
35. Yeh BK, Igarashi M, Eliseenkova AV et al. Structural basis by which alternative splicing confers specificity in fibroblast growth factor receptors. Proc Natl Acad Sci USA 2003; 100(5):2266-2271
36. Lee PL, Johnson DE, Cousens LS et al. Purification and complementary DNA cloning of a receptor for basic fibroblast growth factor. Science 1989; 245(4913):57-60
37. Plotnikov AN, Schlessinger J, Hubbard SR et al. Structural basis for FGF receptor dimerization and activation. Cell 1999; 98(5):641-650
38. Stauber DJ, DiGabriele AD, Hendrickson WA. Structural interactions of fibroblast growth factor receptor with its ligands. Proc Natl Acad Sci USA 2000; 97(1):49-54
39. Olsen SK, Ibrahimi OA, Raucci A et al. Insights into the molecular basis for fibroblast growth factor receptor autoinhibition and ligand-binding promiscuity. Proc Natl Acad Sci USA 2004; 101(4):935-940
40. Wang F, Kan M, Yan G et al. Alternately spliced NH2-terminal immunoglobulin-like Loop I in the ectodomain of the fibroblast growth factor (FGF) receptor 1 lowers affinity for both heparin and FGF-1. J Biol Chem 1995; 270(17):10231-10235
41. Johnson DE, Lu J, Chen H et al. The human fibroblast growth factor receptor genes: a common structural arrangement underlies the mechanisms for generating receptor forms that differ in their third immunoglobulin domain. MolCellBiol 1991; 11(9):4627-4634
42. Miki T, Bottaro DP, Fleming TP et al. Determination ofligand-binding specificity by alternative splicing: two distinct growth factor receptors encoded by a single gene. Proc Natl Acad Sci USA 1992; 89(1):246-250
43. Orr-Urtreger A, Bedford MT, Burakova T et al. Developmental localization of the splicing alternatives of fibroblast growth factor receptor-2 (FGFR2). Dev Biol 1993; 158(2):475-486
44. Forsberg E, Kjellen L. Heparan sulfate: lessons from knockout mice. J Clin Invest 2001; 108(2):175-180
45. Lin X, Buff EM, Perrimon N et al. Heparan sulfate proteoglycans are essential for FGF receptor signaling during Drosophila embryonic development. Development 1999; 126(17):3715-3723
46. Ornitz DM, Yayon A, Flanagan JG et al. Heparin is required for cell-free binding of basic fibroblast growth factor to a soluble receptor and for mitogenesis in whole cells. Mol Cell Biol 1992; 12(1):240-247
47. Rapraeger AC, Krufka A, Olwin BB. Requirement of heparan sulfate for bFGF-mediated fibroblast growth and my oblast differentiation. Science 1991; 252(5013):1705-1708
48. Yayon A, Klagsbrun M, Esko JD et al. Cell surface, heparin-like molecules are required for binding of basic fibroblast growth factor to its high affinity receptor. Cell 1991; 64(4):841-848
49. Whitelock JM, Iozzo RV. Heparan sulfate: a complex polymer charged with biological activity. Chem Rev 2005; 105(7):2745-2764
50. Mohammadi M, Olsen SK, Goetz R. A protein canyon in the FGF-FGF receptor dimer selects from an a la carte menu of heparan sulfate motifs. Curr Opin Struct Biol 2005; 15(5):506-516
51. Makarenkova HP, Hoffman MP, Beenken A et al. Differential interactions of FGFs with heparan sulfate control gradient formation and branching morphogenesis.Sci Signal 2009; 2(88):ra55
52. Hacker U, Nybakken K, Perrimon N. Heparan sulphate proteoglycans: the sweet side of development. Nat Rev Mol Cell Biol 2005; 6(7):530-541
53. Saksela O, Moscatelli D, Sommer A et al. Endothelial cell-derived heparan sulfate binds basic fibroblast growth factor and protects it from proteolytic degradation. J Cell Biol 1988; 107(2):743-751
54. Ashikari-Hada S, Habuchi H, Kariya Y et al. Characterization of growth factor-binding structures in heparin/heparan sulfate using an octasaccharide library. J Biol Chem 2004; 279(13):12346-12354
55. Schlessinger J, Plotnikov AN, Ibrahimi OA et al. Crystal structure of a ternary FGF-FGFR-heparin complex reveals a dual role for heparin in FGFRbinding and dimerization. Mol Cell 2000; 6(3):743-750
56. Goetz R, Beenken A, Ibrahimi OA et al. Molecular insights into the klotho-dependent, endocrine mode of action of fibroblast growth factor 19 subfamily members. Mol Cell Biol 2007; 27(9):3417-3428
57. Chen H, Ma J, Li W et al. A molecular brake in the kinase hinge region regulates the activity of receptor tyrosine kinases. Mol Cell 2007; 27(5):717-730
58. Chen H, Xu CF, Ma J et al. A crystallographic snapshot of tyrosine trans-phosphorylation in action. Proc Natl Acad Sci USA 2008; 105(50):19660-19665
59. Furdui CM, Lew ED, Schlessinger J et al. Autophosphorylation of FGFR1 kinase is mediated by a sequential and precisely ordered reaction. Mol Cell 2006; 21(5):711-717
60. Mohammadi M, Dikic I, Sorokin A et al. Identification of six novel autophosphorylation sites on fibroblast growth factor receptor 1 and elucidation of their importance in receptor activation and signal transduction. Mol Cell Biol 1996; 16(3):977-989
61. Mohammadi M, Dionne CA, Li W et al. Point mutation in FGF receptor eliminates phosphatidylinositol hydrolysis without affecting mitogenesis. Nature 1992; 358(6388):681-684
62. Peters KG, Marie J, Wilson E et al. Point mutation of an FGF receptor abolishes phosphatidylinositol turnover and Ca2+ flux but not mitogenesis. Nature 1992; 358(6388):678-681
63. Seo JH, Suenaga A, Hatakeyama M et al. Structural and functional basis of a role for CRKL in a fibroblast growth factor 8-induced feed-forward loop. Mol Cell Biol 2009; 29(11):3076-3087
64. Divecha N, Irvine RF. Phospholipid signaling. Cell 1995; 80(2):269-278
65. Huang J, Mohammadi M, Rodrigues GA et al. Reduced activation ofRAF-1 and MAP kinase by a fibroblast growth factor receptor mutant deficient in stimulation of phosphatidylinositol hydrolysis. J Biol Chem 1995;270(10):5065- 5072
66. Schlessinger J. Cell signaling by receptor tyrosine kinases. Cell 2000; 103(2):211-225
67. Kouhara H, Hadari YR, Spivak-Kroizman T et al. A lipid-anchored Grb2-binding protein that links FGF-receptor activation to the Ras/MAPK signaling pathway. Cell 1997; 89(5):693-702
68. Dhalluin C, Yan KS, Plotnikova O et al. Structural basis of SNT PTB domain interactions with distinct neurotrophic receptors. Mol Cell 2000; 6(4):921-929
69. Ong SH, Guy GR, Hadari YR et al. FRS2 proteins recruit intracellular signaling pathways by binding to diverse targets on fibroblast growth factor and nerve growth factor receptors. Mol Cell Biol 2000; 20(3):979-989
70. Ong SH, Hadari YR, Gotoh N et al. Stimulation of phosphatidylinositol 3-kinase by fibroblast growth factor receptors is mediated by coordinated recruitment of multiple docking proteins. Proc Natl Acad Sci USA 2001; 98(11):6074-6079
71. Hadari YR, Kouhara H, Lax I et al. Binding of Shp2 tyrosine phosphatase to FRS2 is essential for fibroblast growth factor-induced PC12 cell differentiation. Mol Cell Biol 1998; 18(7):3966-3973
72. Dailey L, Ambrosetti D, Mansukhani A et al. Mechanisms underlying differential responses to FGF signaling. Cytokine Growth Factor Rev 2005; 16(2):233-247
73. Bellosta P, Iwahori A, Plotnikov AN et al. Identification of receptor and heparin binding sites in fibroblast growth factor 4 by structure-based mutagenesis. Mol Cell Biol 2001; 21(17):5946-5957
74. Kalinina J, Byron SA, Makarenkova HP et al. Homodimerization Controls the FGF9 Subfamilys Receptor Binding and Heparan Sulfate Dependent Diffusion in the Extracellular Matrix. Mol Cell Biol 2009
75. OsslundTD, SyedR, Singer E etal. Correlation between the 1.6 A crystal structure and mutational analysis ofkeratinocyte growth factor. Protein Sci 1998; 7(8):1681-1690
76. Plotnikov AN, Eliseenkova AV, Ibrahimi OA et al. Crystal structure of fibroblast growth factor 9 reveals regions implicated in dimerization and autoinhibition. J Biol Chem 2001; 276(6):4322-4329
77. Luo Y, Lu W, Mohamedali KA et al. The glycine box: a determinant of specificity for fibroblast growth factor. Biochemistry 1998; 37(47):16506-16515
78. DiGabriele AD, Lax I, Chen DI et al. Structure of a heparin-linked biologically active dimer of fibroblast growth factor. Nature 1998; 393(6687):812-817
79. Faham S, Hileman RE, Fromm JR et al. Heparin structure and interactions with basic fibroblast growth factor. Science 1996; 271(5252):1116-1120
80. Zhu X, Hsu BT, Rees DC. Structural studies of the binding of the anti-ulcer drug sucrose octasulfate to acidicfibroblastgrowthfactor. Structure 1993; 1(1):27-34
81. Hogan BL, Yingling JM. Epithelial/mesenchymal interactions and branching morphogenesis of the lung. Curr Opin Genet Dev 1998; 8(4):481-486
82. Jin C, Wang F, Wu X et al. Directionally specific paracrine communication mediated by epithelial FGF9 to stromal FGFR3 in two-compartment premalignant prostate tumors. Cancer Res 2004; 64(13):4555-4562
83. Pirvola U, Zhang X, Mantela J et al. Fgf9 signaling regulates inner ear morphogenesis through epithelial-mesenchymal interactions. Dev Biol 2004; 273(2):350-360
84. XuX, Weinstein M, Li C et al. Fibroblast growth factor receptor 2 (FGFR2)-mediated reciprocal regulation loop between FGF8 and FGF10is essential for limb induction. Development 1998; 125(4):753-765
85. Zhang X, Stappenbeck TS, White AC et al. Reciprocal epithelial- mesenchymal FGF signaling is required for cecal development. Development 2006; 133(1):173-180
86. Bellusci S, Grindley J, Emoto H et al. Fibroblast growth factor 10 (FGF10) and branching morphogenesis in the embryonic mouse lung. Development 1997; 124(23):4867-4878
87. Hoffman MP, Kidder BL, Steinberg ZL et al. Gene expression profiles of mouse submandibular gland development: FGFR1 regulates branching morphogenesis in vitro through BMP- and FGF-dependent mechanisms. Development2002; 129(24):5767-5778
88. Izvolsky KI, Shoykhet D, Yang Y et al. Heparan sulfate-FGF10 interactions during lung morphogenesis. Dev Biol 2003; 258(1):185-200
89. Makarenkova HP, Ito M, Govindarajan V et al. FGF10 is an inducer and Pax6 a competence factor for lacrimal gland development. Development 2000; 127(12):2563-2572
90. Sekine K, Ohuchi H, Fujiwara M et al. Fgf10 is essential for limb and lung formation. Nat Genet 1999; 21(1):138-141
91. Liu A, Joyner AL. Early anterior/posterior patterning of the midbrain and cerebellum. Annu Rev Neurosci 2001; 24:869-896
92. Sun X, Mariani FV, Martin GR. Functions of FGF signalling from the apical ectodermal ridge in limb development. Nature 2002; 418(6897):501-508
93. Autosomal dominant hypophosphataemic rickets is associated with mutations in FGF23. Nat Genet 2000; 26(3):345-348
94. Goetz R, Nakada Y, Hu MC et al. Isolated C-terminal tail of FGF23 alleviates hypophosphatemia by inhibiting FGF23-FGFR-Klotho complex formation. Proc Natl Acad Sci USA2009
95. Shimada T, Muto T, Urakawa I et al. Mutant FGF-23 responsible for autosomal dominant hypophosphatemic rickets is resistant to proteolytic cleavage and causes hypophosphatemia in vivo. Endocrinology 2002; 143(8):3179-3182
96. Shimada T, Mizutani S, Muto T et al. Cloning and characterization of FGF23 as a causative factor of tumor-induced osteomalacia. Proc Natl Acad Sci USA 2001; 98(11):6500-6505
97. Shiraki-Iida T, Aizawa H, Matsumura Y et al. Structure of the mouse klotho gene and its two transcripts encoding membrane and secreted protein. FEBS Lett 1998; 424(1-2):6-10
98. Kharitonenkov A, Dunbar JD, Bina HA et al. FGF-21/FGF-21 receptor interaction and activation is determined by betaKlotho. J Cell Physiol 2008; 215(1):1-7
99. Kurosu H, Choi M, Ogawa Y et al. Tissue-specific expression ofbetaKlotho and fibroblast growth factor (FGF) receptor isoforms determines metabolic activity of FGF19 and FGF21. J Biol Chem 2007; 282(37):26687-26695
100. Lin BC, Wang M, Blackmore C et al. Liver-specific activities of FGF19 require Klotho beta. J Biol Chem 2007; 282(37):27277-27284
101. Ogawa Y, Kurosu H, Yamamoto M et al. BetaKlotho is required for metabolic activity of fibroblast growth factor 21. Proc Natl Acad Sci USA 2007; 104(18):7432-7437
102. Suzuki M, Uehara Y, Motomura-Matsuzaka K et al. betaKlotho is required for fibroblast growth factor (FGF) 21 signaling through FGF receptor (FGFR) 1c and FGFR3c. Mol Endocrinol 2008; 22(4):1006-1014
103. Wu X, Ge H, Gupte J et al. Co-receptor requirements for fibroblast growth factor-19 signaling. J Biol Chem 2007; 282(40):29069-29072
104. Kurosu H, Ogawa Y, Miyoshi M et al. Regulation of fibroblast growth factor-23 signaling by klotho. J Biol Chem 2006; 281(10):6120-6123
105. Urakawa I, Yamazaki Y, Shimada T et al. Klotho converts canonical FGF receptor into a specific receptor for FGF23. Nature 2006; 444(7120):770-774
106. Kuro-o M, Matsumura Y, Aizawa H et al. Mutation of the mouse klotho gene leads to a syndrome resembling ageing. Nature 1997; 390(6655):45-51
107. Shimada T, Kakitani M, Yamazaki Y et al. Targeted ablation of Fgf23 demonstrates an essential physiological role ofFGF23 in phosphate and vitamin D metabolism. J Clin Invest 2004; 113(4):561-568
108. Inagaki T, Choi M, Moschetta A et al. Fibroblast growth factor 15 functions as an enterohepatic signal to regulate bile acid homeostasis. Cell Metab 2005; 2(4):217-225
109. Ito S, Fujimori T, Furuya A et al. Impaired negative feedback suppression ofbile acid synthesis in mice lacking betaKlotho. J Clin Invest 2005; 115(8):2202-2208
110. Yu C, Wang F, Kan M et al. Elevated cholesterol metabolism and bile acid synthesis in mice lacking membrane tyrosine kinase receptor FGFR4. J Biol Chem 2000; 275(20):15482-15489
111. Gattineni J, Bates C, Twombley K et al. FGF23 decreases renal NaPi-2a and NaPi-2c expression and induces hypophosphatemia in vivo predominantly via FGF receptor 1. Am J Physiol Renal Physiol 2009; 297(2):F282-291
112. Bai XY, Miao D, Goltzman D et al. The autosomal dominant hypophosphatemic rickets R176Q mutation in fibroblast growth factor 23 resists proteolytic cleavage and enhances in vivo biological potency. J Biol Chem 2003; 278(11):9843-9849
113. Fukumoto S. Physiological regulation and disorders of phosphate metabolism-pivotal role of fibroblast growth factor 23. Intern Med 2008; 47(5):337-343
114. Larsson T, Marsell R, Schipani E et al. Transgenic mice expressing fibroblast growth factor 23 under the control of the alpha1(I) collagen promoter exhibit growth retardation, osteomalacia and disturbed phosphatehomeostasis. Endocrinology2004; 145(7):3087-3094
115. Liu S, Guo R, Simpson LG et al. Regulation of fibroblastic growth factor 23 expression but not degradation by PHEX. J Biol Chem 2003; 278(39):37419-37426
116. Riminucci M, Collins MT, Fedarko NS et al. FGF-23 in fibrous dysplasia ofbone and its relationship to renal phosphate wasting. J Clin Invest 2003; 112(5):683-692
117. Saito H, Kusano K, Kinosaki M et al. Human fibroblast growth factor-23 mutants suppress Na+-dependent phosphate cotransport activity and 1alpha,25-dihydroxyvitamin D3 production. J Biol Chem 2003; 278(4):2206-2211
118. Segawa H, Kawakami E, Kaneko I et al. Effect ofhydrolysis-resistant FGF23-R179Q on dietary phosphate regulation of the renal type-II Na/Pi transporter. Pflugers Arch 2003; 446(5):585-592
119. Lundasen T, Galman C, Angelin B et al. Circulating intestinal fibroblast growth factor 19 has a pronounced diurnal variation and modulates hepatic bile acid synthesis in man. J Intern Med 2006; 260(6):530-536
120. Choi M, Moschetta A, Bookout AL et al. Identification of a hormonal basis for gallbladder filling. Nat Med 2006; 12(11):1253-1255
121. NishimuraT, Nakatake Y, Konishi M et al. Identification ofanovel FGF, FGF-21, preferentially expressed in the liver. Biochim Biophys Acta 2000; 1492(1):203-206
122. Badman MK, Pissios P, Kennedy AR et al. Hepatic fibroblast growth factor 21 is regulated by PPARalpha and is a key mediator of hepatic lipid metabolism in ketotic states. Cell Metab 2007; 5(6):426-437
123. Galman C, Lundasen T, Kharitonenkov A et al. The circulating metabolic regulator FGF21 is induced by prolonged fasting and PPARalpha activation in man. Cell Metab 2008; 8(2):169-174
124. Inagaki T, Dutchak P, Zhao G et al. Endocrine regulation of the fasting response by PPARalpha-mediated induction of fibroblast growth factor21. Cell Metab 2007; 5(6):415-425
125. Palou M, Priego T, Sanchez J et al. Sequential changes in the expression of genes involved in lipid metabolism in adipose tissue and liver in response to fasting. Pflugers Arch 2008; 456(5):825-836
126. Coskun T, Bina HA, Schneider MA et al. Fibroblast growth factor 21 corrects obesity in mice. Endocrinology 2008; 149(12): 6018-27
127. Kharitonenkov A, Wroblewski VJ, Koester A et al. The metabolic state of diabetic monkeys is regulated by fibroblast growth factor-21. Endocrinology 2007; 148(2):774-781
128. Wente W, Efanov AM, Brenner M et al. Fibroblast growth factor-21 improves pancreatic beta-cell function and survival by activation of extracellular signal-regulated kinase 1/2 and Akt signaling pathways. Diabetes 2006; 55(9):2470-2478
129. Kharitonenkov A, Shanafelt AB. Fibroblast growth factor-21 as a therapeutic agent for metabolic diseases. BioDrugs 2008; 22(1):37-44
130. Jonsson KB, Zahradnik R, Larsson T et al. Fibroblast growth factor 23 in oncogenic osteomalacia and X-linked hypophosphatemia. N Engl J Med 2003; 348(17):1656-1663
131. Yamazaki Y, Okazaki R, ShibataM etal. Increased circulatory level ofbiologically active full-length FGF-23 in patients with hypophosphatemic rickets/osteomalacia. J Clin Endocrinol Metab 2002; 87(11):4957-4960
132. Araya K, Fukumoto S, Backenroth R et al. A novel mutation in fibroblast growth factor 23 gene as a cause of tumoral calcinosis. J Clin Endocrinol Metab 2005; 90(10):5523-5527
133. Benet-Pages A, Orlik P, Strom TM et al. An FGF23 missense mutation causes familial tumoral calcinosis with hyperphosphatemia. Hum Mol Genet 2005; 14(3):385-390
134. Larsson T, Yu X, Davis SI et al. A novel recessive mutation in fibroblast growth factor-23 causes familial tumoral calcinosis. J Clin Endocrinol Metab 2005; 90(4):2424-2427
135. Lyles KW, Burkes EJ, Ellis GJ et al. Genetic transmission of tumoral calcinosis: autosomal dominant with variable clinical expressivity. J Clin Endocrinol Metab 1985; 60(6):1093-1096
136. Gutierrez OM, Mannstadt M, Isakova T et al. Fibroblast growth factor 23 and mortality among patients undergoing hemodialysis. N Engl J Med 2008; 359(6):584-592
137. Harmer NJ, Pellegrini L, Chirgadze D et al. The crystal structure of fibroblast growth factor (FGF) 19 reveals novel features of the FGF family and offers a structural basis for its unusual receptor affinity. Biochemistry 2004; 43(3):629-640
138. Wu X, Ge H, Lemon B et al. FGF19 induced hepatocyte proliferation is mediated through FGFR4 activation. J Biol Chem 2009
139. Zhu H, Ramnarayan K, Anchin J et al. Glu-96 of basic fibroblast growth factor is essential for high affinity receptor binding. Identification by structure-based site-directed mutagenesis. J Biol Chem 1995; 270(37):21869-21874
140. Burmeister WP, Cottaz S, Rollin P et al. High resolution X-ray crystallography shows that ascorbate is a cofactor for myrosinase and substitutes for the function of the catalytic base. J Biol Chem 2000; 275(50):39385-39393