Phosphate-Sensing.


Journal

Advances in experimental medicine and biology
ISSN: 0065-2598
Titre abrégé: Adv Exp Med Biol
Pays: United States
ID NLM: 0121103

Informations de publication

Date de publication:
2022
Historique:
entrez: 15 3 2022
pubmed: 16 3 2022
medline: 17 3 2022
Statut: ppublish

Résumé

The blood level of phosphate is tightly regulated in a narrow range. Hyperphosphatemia and hypophosphatemia both lead to the development of diseases, such as hyperphosphatemic tumoral calcinosis and rickets/osteomalacia, respectively. Although several humoral factors have been known to affect blood phosphate levels, fibroblast growth factor 23 (FGF23) is the principal hormone involved in the regulation of blood phosphate. This hormone is produced by bone, particularly by osteocytes and osteoblasts, and has the effect of lowering the blood level of phosphate in the renal proximal tubules. Therefore, some phosphate-sensing mechanism should exist, at least in the bone. However, the mechanisms through which bone senses changes in the blood level of phosphate, and through which the bone regulates FGF23 production remain to be fully elucidated. Our recent findings demonstrate that high extracellular phosphate phosphorylates FGF receptor 1c (FGFR1c). Its downstream extracellular signal-regulated kinase (ERK) kinase (MEK)/ERK signaling pathway regulates the expression of several transcription factors and the GALNT3 gene, which encodes GalNAc-T3, which plays a role in the regulation of posttranslational modification of FGF23 protein, which in turn enhances FGF23 production. The FGFR1c-GALNT3 gene axis is considered to be the most important mechanism for regulating the production of FGF23 in bone in the response to a high phosphate diet. Thus-in the regulation of FGF23 production and blood phosphate levels-FGFR1c may be considered to function as a phosphate-sensing molecule. A feedback mechanism, in which FGFR1c and FGF23 are involved, is present in blood phosphate regulation. In addition, other reports indicate that PiT1 and PiT2 (type III sodium-phosphate cotransporters), and calcium-sensing receptor are also involved in the phosphate-sensing mechanism. In the present chapter, we summarize new insights on phosphate-sensing mechanisms.

Identifiants

pubmed: 35288870
doi: 10.1007/978-3-030-91623-7_4
doi:

Substances chimiques

Phosphates 0
Fibroblast Growth Factors 62031-54-3

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

27-35

Informations de copyright

© 2022. Springer Nature Switzerland AG.

Références

Abe Y, Nagano M, Tada A et al (2017) Deep phosphotyrosine proteomics by optimization of phosphotyrosine enrichment and MS/MS parameters. J Proteome Res 16:1077–1086
pubmed: 28152594
Almaden Y, Canalejo A, Hernandez A et al (1996) Direct effect of phosphorus on PTH secretion from whole rat parathyroid glands in vitro. J Bone Miner Res 11:970–976
pubmed: 8797118
Beck GR Jr, Knecht N (2003) Osteopontin regulation by inorganic phosphate is ERK1/2-, protein kinase C-, and proteasome-dependent. J Biol Chem 278:41921–41929
pubmed: 12920127
Beck GR Jr, Zerler B, Moran E (2000) Phosphate is a specific signal for induction of osteopontin gene expression. Proc Natl Acad Sci U S A 97:8352–8357
pubmed: 10890885 pmcid: 26951
Bennett EP, Mandel U, Clausen H et al (2012) Control of mucin-type O-glycosylation: a classification of the polypeptide GalNAc-transferase gene family. Glycobiology 22:736–756
pubmed: 22183981
Biber J, Hernando N, Forster I (2013) Phosphate transporters and their function. Annu Rev Physiol 75:535–550
pubmed: 23398154
Bon N, Couasnay G, Bourgine A et al (2018a) Phosphate (Pi)-regulated heterodimerization of the high-affinity sodium-dependent Pi transporters PiT1/Slc20a1 and PiT2/Slc20a2 underlies extracellular Pi sensing independently of Pi uptake. J Biol Chem 293:2102–2114
pubmed: 29233890
Bon N, Frangi G, Sourice S et al (2018b) Phosphate-dependent FGF23 secretion is modulated by PiT2/Slc20a2. Mol Metab 11:197–204
pubmed: 29551636 pmcid: 6001877
Brown EM, Macleod RJ (2001) Extracellular calcium sensing and extracellular calcium signaling. Physiol Rev 81:239–297
pubmed: 11152759
Brown EM, Gamba G, Riccardi D et al (1993) Cloning and characterization of an extracellular ca(2+)-sensing receptor from bovine parathyroid. Nature 366:575–580
pubmed: 8255296
Centeno PP, Herberger A, Mun HC et al (2019) Phosphate acts directly on the calcium-sensing receptor to stimulate parathyroid hormone secretion. Nat Commun 10:4693
pubmed: 31619668 pmcid: 6795806
Comps-Agrar L, Dunshee DR, Eaton DL et al (2015) Unliganded fibroblast growth factor receptor 1 forms density-independent dimers. J Biol Chem 290:24166–24177
pubmed: 26272615 pmcid: 4591805
Drüeke TB (2004) Modulation and action of the calcium-sensing receptor. Nephrol Dial Transplant 19(Suppl 5):V20–V26
pubmed: 15284356
Feng JQ, Ward LM, Liu S et al (2006) Loss of DMP1 causes rickets and osteomalacia and identifies a role for osteocytes in mineral metabolism. Nat Genet 38:1310–1315
pubmed: 17033621 pmcid: 1839871
Ferrari SL, Bonjour JP, Rizzoli R (2005) Fibroblast growth factor-23 relationship to dietary phosphate and renal phosphate handling in healthy young men. J Clin Endocrinol Metab 90:1519–1524
pubmed: 15613425
Florenzano P, Cipriani C, Roszko KL et al (2020) Approach to patients with hypophosphataemia. Lancet Diabetes Endocrinol 8:163–174
pubmed: 31924563
Frishberg Y, Ito N, Rinat C et al (2007) Hyperostosis-hyperphosphatemia syndrome: a congenital disorder of O-glycosylation associated with augmented processing of fibroblast growth factor 23. J Bone Miner Res 22:235–242
pubmed: 17129170
Fukumoto S, Yamashita T (2007) FGF23 is a hormone-regulating phosphate metabolism--unique biological characteristics of FGF23. Bone 40:1190–1195
pubmed: 17276744
Furdui CM, Lew ED, Schlessinger J et al (2006) Autophosphorylation of FGFR1 kinase is mediated by a sequential and precisely ordered reaction. Mol Cell 21:711–717
pubmed: 16507368
Goetz R, Mohammadi M (2013) Exploring mechanisms of FGF signalling through the lens of structural biology. Nat Rev Mol Cell Biol 14:166–180
pubmed: 23403721 pmcid: 3695728
Gotoh N (2008) Regulation of growth factor signaling by FRS2 family docking/scaffold adaptor proteins. Cancer Sci 99:1319–1325
pubmed: 18452557
Guagnano V, Furet P, Spanka C et al (2011) Discovery of 3-(2,6-dichloro-3,5-dimethoxy-phenyl)-1-{6-[4-(4-ethyl-piperazin-1-yl)-phenylamin o]-pyrimidin-4-yl}-1-methyl-urea (NVP-BGJ398), a potent and selective inhibitor of the fibroblast growth factor receptor family of receptor tyrosine kinase. J Med Chem 54:7066–7083
pubmed: 21936542
Jono S, Mckee MD, Murry CE et al (2000) Phosphate regulation of vascular smooth muscle cell calcification. Circ Res 87:E10–E17
pubmed: 11009570
Khoshniat S, Bourgine A, Julien M et al (2011) The emergence of phosphate as a specific signaling molecule in bone and other cell types in mammals. Cell Mol Life Sci 68:205–218
pubmed: 20848155
Kimata M, Michigami T, Tachikawa K et al (2010) Signaling of extracellular inorganic phosphate up-regulates cyclin D1 expression in proliferating chondrocytes via the Na+/Pi cotransporter Pit-1 and Raf/MEK/ERK pathway. Bone 47:938–947
pubmed: 20709201
Kinoshita Y, Fukumoto S (2018) X-linked hypophosphatemia and FGF23-related Hypophosphatemic diseases: prospect for new treatment. Endocr Rev 39:274–291
pubmed: 29381780
Kuro-O M, Matsumura Y, Aizawa H et al (1997) Mutation of the mouse klotho gene leads to a syndrome resembling ageing. Nature 390:45–51
pubmed: 9363890
Kurosu H, Ogawa Y, Miyoshi M et al (2006) Regulation of fibroblast growth factor-23 signaling by klotho. J Biol Chem 281:6120–6123
Lew ED, Furdui CM, Anderson KS et al (2009) The precise sequence of FGF receptor autophosphorylation is kinetically driven and is disrupted by oncogenic mutations. Sci Signal 2:ra6
pubmed: 19224897 pmcid: 2755185
Lin CC, Melo FA, Ghosh R et al (2012) Inhibition of basal FGF receptor signaling by dimeric Grb2. Cell 149:1514–1524
pubmed: 22726438
Liu S, Zhou J, Tang W et al (2006) Pathogenic role of Fgf23 in Hyp mice. Am J Physiol Endocrinol Metab 291:E38–E49
pubmed: 16449303
Mckay MM, Morrison DK (2007) Integrating signals from RTKs to ERK/MAPK. Oncogene 26:3113–3121
pubmed: 17496910
Michigami T, Kawai M, Yamazaki M et al (2018) Phosphate as a signaling molecule and its sensing mechanism. Physiol Rev 98:2317–2348
pubmed: 30109818
Nielsen PK, Feldt-Rasmussen U, Olgaard K (1996) A direct effect in vitro of phosphate on PTH release from bovine parathyroid tissue slices but not from dispersed parathyroid cells. Nephrol Dial Transplant 11:1762–1768
pubmed: 8918619
Nishino J, Yamazaki M, Kawai M et al (2017) Extracellular phosphate induces the expression of dentin matrix protein 1 through the FGF receptor in osteoblasts. J Cell Biochem 118:1151–1163
pubmed: 27639037
Ornitz DM, Itoh N (2015) The fibroblast growth factor signaling pathway. Wiley Interdiscip Rev Dev Biol 4:215–266
pubmed: 25772309 pmcid: 4393358
Perwad F, Azam N, Zhang MY et al (2005) Dietary and serum phosphorus regulate fibroblast growth factor 23 expression and 1,25-dihydroxyvitamin D metabolism in mice. Endocrinology 146:5358–5364
pubmed: 16123154
Saito H, Maeda A, Ohtomo S et al (2005) Circulating FGF-23 is regulated by 1alpha,25-dihydroxyvitamin D3 and phosphorus in vivo. J Biol Chem 280:2543–2549
pubmed: 15531762
Sarabipour S, Hristova K (2016) Mechanism of FGF receptor dimerization and activation. Nat Commun 7:10262
pubmed: 26725515 pmcid: 4725768
Shimada T, Mizutani S, Muto T et al (2001) Cloning and characterization of FGF23 as a causative factor of tumor-induced osteomalacia. Proc Natl Acad Sci U S A 98:6500–6505
pubmed: 11344269 pmcid: 33497
Shimada T, Muto T, Urakawa I et al (2002) Mutant FGF-23 responsible for autosomal dominant hypophosphatemic rickets is resistant to proteolytic cleavage and causes hypophosphatemia in vivo. Endocrinology 143:3179–3182
pubmed: 12130585
Shimada T, Hasegawa H, Yamazaki Y et al (2004) FGF-23 is a potent regulator of vitamin D metabolism and phosphate homeostasis. J Bone Miner Res 19:429–435
pubmed: 15040831 pmcid: 15040831
Slatopolsky E, Finch J, Denda M et al (1996) Phosphorus restriction prevents parathyroid gland growth. High phosphorus directly stimulates PTH secretion in vitro. J Clin Invest 97:2534–2540
pubmed: 8647946 pmcid: 507339
Tagliabracci VS, Engel JL, Wiley SE et al (2014) Dynamic regulation of FGF23 by Fam20C phosphorylation, GalNAc-T3 glycosylation, and furin proteolysis. Proc Natl Acad Sci U S A 111:5520–5525
pubmed: 24706917 pmcid: 3992636
Takashi Y, Fukumoto S (2018) FGF23 beyond Phosphotropic hormone. Trends Endocrinol Metab 29:755–767
pubmed: 30217676
Takashi Y, Kosako H, Sawatsubashi S et al (2019) Activation of unliganded FGF receptor by extracellular phosphate potentiates proteolytic protection of FGF23 by its O-glycosylation. Proc Natl Acad Sci U S A 116:11418–11427
pubmed: 31097591 pmcid: 6561303
Thomas L, Bettoni C, Knöpfel T et al (2017) Acute adaption to Oral or intravenous phosphate requires parathyroid hormone. J Am Soc Nephrol 28:903–914
pubmed: 28246304
Topaz O, Shurman DL, Bergman R et al (2004) Mutations in GALNT3, encoding a protein involved in O-linked glycosylation, cause familial tumoral calcinosis. Nat Genet 36:579–581
pubmed: 15133511
Trokovic R, Trokovic N, Hernesniemi S et al (2003) FGFR1 is independently required in both developing mid- and hindbrain for sustained response to isthmic signals. EMBO J 22:1811–1823
pubmed: 12682014 pmcid: 154461
Urakawa I, Yamazaki Y, Shimada T et al (2006) Klotho converts canonical FGF receptor into a specific receptor for FGF23. Nature 444:770–774
pubmed: 17086194
Virkki LV, Biber J, Murer H et al (2007) Phosphate transporters: a tale of two solute carrier families. Am J Physiol Renal Physiol 293:F643–F654
pubmed: 17581921
White KE, Cabral JM, Davis SI et al (2005) Mutations that cause osteoglophonic dysplasia define novel roles for FGFR1 in bone elongation. Am J Hum Genet 76:361–367
pubmed: 15625620
Yamazaki Y, Tamada T, Kasai N et al (2008) Anti-FGF23 neutralizing antibodies show the physiological role and structural features of FGF23. J Bone Miner Res 23:1509–1518
pubmed: 18442315
Yamazaki M, Ozono K, Okada T et al (2010) Both FGF23 and extracellular phosphate activate Raf/MEK/ERK pathway via FGF receptors in HEK293 cells. J Cell Biochem 111:1210–1221
pubmed: 20717920
Zhang M, Xuan S, Bouxsein ML et al (2002) Osteoblast-specific knockout of the insulin-like growth factor (IGF) receptor gene reveals an essential role of IGF signaling in bone matrix mineralization. J Biol Chem 277:44005–44012
pubmed: 12215457

Auteurs

Yuichi Takashi (Y)

Department of Endocrinology and Diabetes Mellitus, Fukuoka University School of Medicine, Fukuoka, Japan.

Seiji Fukumoto (S)

Department of Molecular Endocrinology, Fujii Memorial Institute of Medical Sciences, Institute of Advanced Medical Sciences, Tokushima University, Tokushima, Japan. fukumoto-tky@umin.ac.jp.

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