Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 2005 May;37(5):520-5.
doi: 10.1038/ng1549. Epub 2005 Apr 17.

Identification of a new gene mutated in Fraser syndrome and mouse myelencephalic blebs

Shalini Jadeja  1 , Ian Smyth, Jolanta E Pitera, Martin S Taylor, Mieke van Haelst, Elizabeth Bentley, Lesley McGregor, Jason Hopkins, Georges Chalepakis, Nicole Philip, Antonio Perez Aytes, Fiona M Watt, Susan M Darling, Ian Jackson, Adrian S Woolf, Peter J Scambler
Affiliations

Identification of a new gene mutated in Fraser syndrome and mouse myelencephalic blebs

Shalini Jadeja et al. Nat Genet. 2005 May.

Abstract

Fraser syndrome is a recessive, multisystem disorder presenting with cryptophthalmos, syndactyly and renal defects and associated with loss-of-function mutations of the extracellular matrix protein FRAS1. Fras1 mutant mice have a blebbed phenotype characterized by intrauterine epithelial fragility generating serous and, later, hemorrhagic blisters. The myelencephalic blebs (my) strain has a similar phenotype. We mapped my to Frem2, a gene related to Fras1 and Frem1, and showed that a Frem2 gene-trap mutation was allelic to my. Expression of Frem2 in adult kidneys correlated with cyst formation in my homozygotes, indicating that the gene is required for maintaining the differentiated state of renal epithelia. Two individuals with Fraser syndrome were homozygous with respect to the same missense mutation of FREM2, confirming genetic heterogeneity. This is the only missense mutation reported in any blebbing mutant or individual with Fraser syndrome, suggesting that calcium binding in the CALXbeta-cadherin motif is important for normal functioning of FREM2.

PubMed Disclaimer

Similar articles

See all similar articles

Cited by

See all "Cited by" articles

Publication types

Substances

Associated data