ArticleMolecular vision2008
A novel PITX2 mutation in a Chinese family with Axenfeld-Rieger syndrome.
Article in Molecular vision, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 10 citations in OpenAlex.
- In Silico Characterization of Pathogenic Homeodomain Missense Mutations in the PITX2 Gene.Biochemical genetics · 2025Article
- Novel PITX2 Mutations including a Mutation Causing an Unusual Ophthalmic Phenotype of Axenfeld-Rieger Syndrome.Journal of ophthalmology · 2019Article
- Accurate prediction of functional, structural, and stability changes in PITX2 mutations using in silico bioinformatics algorithms.PloS one · 2018Article
- Identification of a novel frameshift mutation in PITX2 gene in a Chinese family with Axenfeld-Rieger syndrome.Journal of Zhejiang University. Science. B · 2014Article
- Magnetic resonance imaging findings in Axenfeld-Rieger syndrome.Clinical ophthalmology (Auckland, N.Z.) · 2013Article
- Structural and biophysical insights into the ligand-free Pitx2 homeodomain and a ring dermoid of the cornea inducing homeodomain mutant.Biochemistry · 2012Article
- The Pitx2c N-terminal domain is a critical interaction domain required for asymmetric morphogenesis.Developmental dynamics : an official publication of the American Association of Anatomists · 2009Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
purposeAxenfeld-Rieger syndrome (ARS) is an autosomal dominant disorder characterized by extraocular anomalies and developmental defects of the anterior segment. PITX2 (paired-like homeodomain transcription factor 2) is considered the major causative gene. In this study, we characterized the molecular defect in PITX2 in a Chinese family with ARS.
methodsTwo generations of the family with ARS were enrolled in the present study. In addition to ophthalmologic examinations, polymerase chain reaction (PCR) amplification and nucleotide sequencing of all coding exons of PITX2 were performed. Exon 5 (region 1) was also sequenced in 100 healthy controls unrelated to the family for comparison.
resultsA novel PITX2 mutation, c.840G>T, was identified in all affected members of the family with ARS that causes an amino acid substitution from tryptophan to cysteine at codon 86.
conclusionsWe found a novel p.W86C mutation in PITX2 in a Chinese family with ARS. The tryptophan residue at position 86 is strictly conserved in PITX2a proteins from several species and in homeodomain proteins. We suggest that this mutation in PITX2 is the cause of typical ARS in patients. Our results may be useful for better understanding of the spectrum of PITX2 mutations and the role of PITX2 in the development and progression of ARS.
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19052653PMC2592999W2137102304What OpenQuestion holds
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