AI Article Synopsis

  • - X-linked hypophosphatemic rickets (XLH) is caused by mutations in the PHEX gene, leading to elevated levels of fibroblast growth factor 23 (FGF23) and impaired phosphate absorption, resulting in rickets and poor bone mineralization.
  • - Two specific pathogenic mutations, c.433 G > T (p.Glu145*) and c.2245 T > C (p.Trp749Arg), were identified in XLH patients, with studies showing these mutations reduce PHEX protein levels and intracellular enzyme activity compared to the wild-type PHEX.
  • - PHEX was found to be a direct transcriptional inhibitor of FGF23, with mutant PHEX enhancing F

Article Abstract

X-linked hypophosphatemic rickets (XLH) is characterized by increased circulating fibroblast growth factor 23 (FGF23) concentration caused by PHEX (NM_000444.5) mutations. Renal tubular resorption of phosphate is impaired, resulting in rickets and impaired bone mineralization. By phenotypic-genetic linkage analysis, two PHEX pathogenic mutations were found in two XLH families: c.433 G > T, p.Glu145* in exon 4 and c.2245 T > C, p.Trp749Arg in exon 22. Immunofluorescence showed that the localization of p.Glu145* and p.Trp749Arg mutant and secretory PHEX (secPHEX) changed, with decreased expression. In a HEK293T cell model co-transfected with PHEX, secPHEX, and FGF23, wild-type PHEX, secPHEX, and FGF23 proteins were distributed in the cell membrane or endoplasmic reticulum, while the mutant was located in the nuclear membrane and cytoplasm. qPCR of p.Glu145* revealed decreased PHEX and secPHEX mRNA expression in cells, with no difference in mRNA expression of p.Trp749Arg. Both mutations decreased intracellular PHEX endopeptidase activity. Western blot analysis showed decrease in mutant and secPHEX protein expression and no FGF23 protein expression in single-transfected PHEX and secPHEX cells. In cells co-transfected with FGF23, PHEX and secPHEX mutation promoted FGF23 expression. Dual-luciferase reporter gene was used to detect the effect of PHEX on FGF23 promoter. The dual-luciferase reporter gene showed that after PHEX overexpression, the activity of mutant firefly luciferase was significantly higher than that of wild type. The regulatory mechanism between PHEX and FGF23 is still unclear, but we found that PHEX is a direct transcriptional inhibitor of FGF23 and affects the expression of FGF23. This study verified the pathogenicity of the two variants and revealed the possible regulatory mechanism between PHEX and FGF23.

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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC9163062PMC
http://dx.doi.org/10.1038/s41419-022-04969-5DOI Listing

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Article Synopsis
  • - X-linked hypophosphatemic rickets (XLH) is caused by mutations in the PHEX gene, leading to elevated levels of fibroblast growth factor 23 (FGF23) and impaired phosphate absorption, resulting in rickets and poor bone mineralization.
  • - Two specific pathogenic mutations, c.433 G > T (p.Glu145*) and c.2245 T > C (p.Trp749Arg), were identified in XLH patients, with studies showing these mutations reduce PHEX protein levels and intracellular enzyme activity compared to the wild-type PHEX.
  • - PHEX was found to be a direct transcriptional inhibitor of FGF23, with mutant PHEX enhancing F
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Matrix Extracellular Phospho-glycoprotEin (MEPE) and proteases are elevated and PHEX is defective in HYP. PHEX prevents proteolysis of MEPE and release of a protease-resistant MEPE-ASARM peptide, an inhibitor of mineralization (minhibin). Thus, in HYP, mutated PHEX may contribute to increased ASARM peptide release.

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X-linked hypophosphatemia (XLH) and autosomal dominant hypophosphatemic rickets (ADHR) are characterized by renal phosphate wasting, rickets, and osteomalacia. ADHR is caused by gain of function mutations in the fibroblast growth factor 23 gene (FGF23). During secretion, FGF23 is processed at the C-terminus between amino acids 179 and 180.

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Mutations in the PHEX gene (phosphate-regulating gene with homologies to endopeptidases on the X chromosome) are responsible for X-linked hypophosphataemia, and studies in the Hyp mouse model of the human disease implicate the gene product in the regulation of renal phosphate (P(i)) reabsorption and bone mineralization. Although the mechanism for PHEX action is unknown, structural homologies with members of the M13 family of endopeptidases suggest a function for PHEX protein in the activation or degradation of peptide factors involved in the control of renal P(i) transport and matrix mineralization. To determine whether PHEX has endopeptidase activity, we generated a recombinant soluble, secreted form of human PHEX (secPHEX) and tested the activity of the purified protein with several peptide substrates, including a variety of bone-related peptides.

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