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The child was found to carry a heterozygous missense mutation c.1939G>A (p.Ala647Thr) in exon 19 of the protein-O-mannosyltransferase 1 (POMT1) gene inherited from the mother and a heterozygous frameshift mutation c.2141delG (p.Trp714Ter) in exon 20 inherited from the father.
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These findings may expand phenotype and mutation spectrum of the POMT1 gene. Clinical diagnosis supplemented with molecular screening may result in more accurate diagnoses of, prognoses for, and improved genetic counselling for this disease
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O-mannosylation of cadherins and protocadherins does not require POMT1 and/or POMT2 in contrast to alpha-dystroglycan, and moreover, the O-Man glycans on cadherins are not elongated.
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results demonstrate functional and biochemical similarities between POMT1 and its orthologue from bakers' yeast Pmt4.
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Our results suggest that POMT activity is inversely proportional to clinical severity, and demonstrate that skin fibroblasts can be used for differential diagnosis of patients with alpha-dystroglycanopathies. We have provided clinical, histological, enzymatic and genetic evidence of POMT1 involvement in five unrelated Chinese patients.
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Inhibition of POMT1/2 in human mesencyhmal stem cells , resulted in complete abolishment of chondrogenesis and alterations of adipogenic and osteogenic potential together with a lethal effect during myogenic induction.
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report of 2 male siblings and an unrelated female with early onset muscular dystrophy and intellectual disability with minimal structural brain anomalies and no ocular abnormalities; a novel missense mutation (c.1958C>T; p.Pro653Leu) was identified
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Three patients with heterozygous POMT1 mutations showed left ventricular (LV) dilation and/or decrease in myocardial contractile force.
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the effects of replacing Arg(64), Glu(78) and Arg(138)residues in human POMT1 and POMT2 with Ala on complex formation and enzymatic activity were studied.
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the function of the gene products is only known for POMT1, POMT2, and POMGnT1, all responsible for the O-mannosylglycan biosynthesis
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the N-glycosylation of POMT1 and POMT2 is required for maintaining the conformation as well as the activity of the POMT1-POMT2 complex.
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Mutations in the O-mannosyltransferase gene POMT1 give rise to the severe neuronal migration disorder Walker-Warburg syndrome
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Extracellular matrix and nuclear abnormalities in skeletal muscle of a patient with Walker-Warburg syndrome caused by POMT1 mutation.
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active enzyme complex of POMT1 and POMT2 suggests that the regulation of protein O-mannosylation is complex and appears to be required for normal structure and function of alpha-dystroglycan in muscle and brain
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The authors report on a patient with Walker-Warburg syndrome and a novel POMT1 mutation. The patient expressed alpha-dystroglycan core protein, but fully glycosylated alpha-DG antibody epitopes were absent, associated with loss of laminin-binding activity
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Results indicate that mutations in the protein O-mannosyltransferase 1 gene result in a defect of protein O-mannosylation in Walker-Warburg syndrome patients.
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the phenotype of glycosylation disorders linked to POMT1 mutations. Furthermore, the A200P mutation is part of a conserved core haplotype, indicating an ancestral founder mutation.
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human protein O-mannosyltransferases 1 and 2 form heterocomplexes which possess protein O-mannosyltransferase activity
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Several mutations were found in the Protein O-Mannosyltransferase 1 and 2 (POMT1 and POMT2) genes, and one mutation was found in each of the fukutin and fukutin-related protein (FKRP) genes.
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An inverse Alu-repeated DNA element within exon 3 is associated with Walker Warburg syndrome in French Caucasian families.
