epidermal-growth-factor and Tetralogy-of-Fallot

epidermal-growth-factor has been researched along with Tetralogy-of-Fallot* in 2 studies

Other Studies

2 other study(ies) available for epidermal-growth-factor and Tetralogy-of-Fallot

ArticleYear
4q25 microdeletion encompassing PITX2: A patient presenting with tetralogy of Fallot and dental anomalies without ocular features.
    European journal of medical genetics, 2018, Volume: 61, Issue:2

    Axenfeld-Rieger syndrome (ARS) is a heterogeneous clinical entity transmitted in an autosomal dominant manner. The main feature, Axenfeld-Rieger Anomaly (ARA), is a malformation of the anterior segment of the eye that can lead to glaucoma and impair vision. Extra-ocular defects have also been reported. Point mutations of FOXC1 and PITX2 are responsible for about 40% of the ARS cases. We describe the phenotype of a patient carrying a deletion encompassing the 4q25 locus containing PITX2 gene. This child presented with a congenital heart defect (Tetralogy of Fallot, TOF) and no signs of ARA. He is the first patient described with TOF and a complete deletion of PITX2 (arr[GRCh37]4q25(110843057-112077858)x1, involving PITX2, EGF, ELOVL6 and ENPEP) inherited from his ARS affected mother. In addition, to our knowledge, he is the first patient reported with no ocular phenotype associated with haploinsufficiency of PITX2. We compare the phenotype and genotype of this patient to those of five other patients carrying 4q25 deletions. Two of these patients were enrolled in the university hospital in Toulouse, while the other three were already documented in DECIPHER. This comparative study suggests both an incomplete penetrance of the ocular malformation pattern in patients carrying PITX2 deletions and a putative association between TOF and PITX2 haploinsufficiency.

    Topics: Acetyltransferases; Adult; Anterior Eye Segment; Child; Chromosome Deletion; Chromosomes, Human, Pair 4; Epidermal Growth Factor; Eye Abnormalities; Eye Diseases, Hereditary; Fatty Acid Elongases; Female; Glutamyl Aminopeptidase; Haploinsufficiency; Homeobox Protein PITX2; Homeodomain Proteins; Humans; Male; Pedigree; Phenotype; Tetralogy of Fallot; Tooth Abnormalities; Transcription Factors

2018
The tetralogy of Fallot-associated G274D mutation impairs folding of the second epidermal growth factor repeat in Jagged-1.
    The FEBS journal, 2009, Volume: 276, Issue:21

    Notch signaling controls spatial patterning and cell-fate decisions in all metazoans. Mutations in JAG1, one of the five Notch ligands in man, have been associated with Alagille syndrome and with a familial form of tetralogy of Fallot. A specific G274D mutation in the second epidermal growth factor repeat of the Jagged-1 was found to correlate with tetralogy of Fallot symptoms but not with usual Alagille syndrome phenotypes. To investigate the effects of this mutation, we studied the in vitro oxidative folding of the wild-type and mutant peptides encompassing the second epidermal growth factor. We found that the G274D mutation strongly impairs the correct folding of the epidermal growth factor module, and folding cannot be rescued by compensative mutations. The 274 position displays very low tolerance to substitution because neither the G274S nor the G274A mutants could be refolded in vitro. A sequence comparison of epidermal growth factor repeats found in human proteins revealed that the pattern displayed by the second epidermal growth factor is exclusively found in Notch ligands and that G274 is absolutely conserved within this group. We carried out a systematic and comprehensive analysis of mutations found in epidermal growth factor repeats and show that specific residue requirements for folding, structural integrity and correct post-translational processing may provide a rationale for most of the disease-associated mutations.

    Topics: Alagille Syndrome; Amino Acid Sequence; Animals; Calcium-Binding Proteins; Epidermal Growth Factor; Humans; Intercellular Signaling Peptides and Proteins; Jagged-1 Protein; Membrane Proteins; Mice; Molecular Sequence Data; Mutation; NIH 3T3 Cells; Protein Folding; Serrate-Jagged Proteins; Tandem Repeat Sequences; Tetralogy of Fallot

2009
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