Hydrocephalus and Hirschsprung's disease in a patient with a mutation of L1CAM.

Okamoto, Nobuhiko; Wada, Yoshinao; Goto, Mari

doi:10.1136/jmg.34.8.670

Cited by 65 publications

(38 citation statements)

References 13 publications

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“…We reported a patient with XLH due to a 2-bp deletion in exon 18 (2421delTG) who had cleft palate and HSCR (Okamoto et al 1997). Vits et al (1998) and Parisi et al (2002) reported similar conditions.…”

Section: Introductionmentioning

confidence: 90%

Hydrocephalus and Hirschsprung’s disease with a mutation of L1CAM

et al. 2004

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Abnormalities of the L1CAM gene, a member of the immunoglobulin gene superfamily of neural-cell adhesion molecules, are associated with X-linked hydrocephalus and some allelic disorders. Hirschsprung's disease (HSCR) is characterized by the absence of ganglion cells and the presence of hypertrophic nerve trunks in the distal bowel. There have been three reports of patients with X-linked hydrocephalus and HSCR with a mutation in the L1CAM gene. We report three more patients with similar conditions. We suspect that decreased L1CAM may be a modifying factor in the development of HSCR.

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Section: Introductionmentioning

confidence: 90%

Hydrocephalus and Hirschsprung’s disease with a mutation of L1CAM

et al. 2004

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“…Two other examples of phosphorylation of noncanonical sites by ERK have been reported (61,64). A possible explanation for this comes from structural analysis of ERK2, which reveals that it contains two regions for interacting with substrates: a proline specificity region as well as another region in the C-terminal domain of the kinase that forms a substrate-binding groove (65). Furthermore, MAPKs bind short proline-containing peptides relatively poorly, suggesting that a longer sequence with additional structural determinants is necessary for optimal binding and phosphorylation by the kinase (66,67).…”

Section: Erk2 and P90mentioning

confidence: 99%

Activation of the MAPK Signal Cascade by the Neural Cell Adhesion Molecule L1 Requires L1 Internalization

Schaefer¹,

Kamiguchi²,

Wong³

et al. 1999

Journal of Biological Chemistry

168

171

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“…60, 61, and Figure 2C). The importance of ENCDC cell-cell contact is suggested by human L1 cell adhesion molecule (L1CAM) mutations that increase risk of HSCR, hydrocephalus, and corpus callosum defects (62)(63)(64). L1cam mutations also increase the number of isolated ENCDCs and reduce bowel colonization in mice (62).…”

Section: Chain Migration and Cell Adhesionmentioning

confidence: 99%