Distribution of mutations in the PEX gene in families with X-linked hypophosphataemic rickets (HYP)

生物 遗传学 外显子 无义突变 错义突变 基因 苯丙氨酸 突变 终止密码子 分子生物学 基因突变 佝偻病 维生素D与神经学 内分泌学
作者
Peter Rowe,C Oudet,Fiona Francis,Christiane Sinding,Solange Pannetier,Mike J. Econs,Tim M. Strom,Thomas Meitinger,Michèle Garabédian,Albert David,Marie Alice Macher,E. Questiaux,Ewa Popowska,Ewa Pronicka,Andrew Read,Agnes Mokrzycki,Francis H. Glorieux,Marc K. Drezner,André Hanauer,Hans Lehrach
出处
期刊:Human Molecular Genetics [Oxford University Press]
卷期号:6 (4): 539-549 被引量:199
标识
DOI:10.1093/hmg/6.4.539
摘要

Mutations in the PEXgene at Xp22.1 (phosphate-regulating gene with homologies to endopeptidases, on the X-chromosome), are responsible for X-linked hypo-phosphataemic rickets (HYP). Homology of PEX to the M13 family of Zn2+ metallopeptidases which include neprilysin (NEP) as prototype, has raised important questions regarding PEX function at the molecular level. The aim of this study was to analyse 99 HYP families for PEX gene mutations, and to correlate predicted changes in the protein structure with Zn2+ metallo-peptidase gene function. Primers flanking 22 characterised exons were used to amplify DNA by PCR, and SSCP was then used to screen for mutations. Deletions, insertions, nonsense mutations, stop codons and splice mutations occurred in 83% of families screened for in all 22 exons, and 51% of a separate set of families screened in 17 PEX gene exons. Missense mutations in four regions of the gene were informative regarding function, with one mutation in the Zn2+-bind-ing site predicted to alter substrate-enzyme interaction and catalysis. Computer analysis of the remaining mutations predicted changes in secondary structure, N-glycosylation, protein phosphorylation and catalytic site molecular structure. The wide range of mutations that align with regions required for protease activity in NEP suggests that PEX also functions as a protease, and may act by processing factor(s) involved in bone mineral metabolism.
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