Myotubularin loss-of-function mutations cause X-linked myotubular myopathy a severe congenital myoopathy with predominance and hypotrophy of type I (slow) muscle fibers
level of myotubes MTM1 mutations do not dramatically affect calcium homeostasis and calcium release mediated through the ryanodine receptor 1 though they do affect myotube size and nuclear content..mature muscles such as those obtained from patient muscle biopsies exhibit a significant decrease in expression of the ryanodine receptor 1 a decrease in muscle-specific microRNAs and a considerable up-regulation of HDAC4.
In platelets MTM1 is a highly active 3-phosphatase mainly associated to membranes and found on the dense granules and to a lesser extent on alpha-granules.
Results confirm that the severe neonatal onset of myopathy in male infants is sufficient to address the direct molecular testing toward the MTM1 gene and above all suggest that the number of undiagnosed symptomatic female carriers is probably underestimated
Analysis of human XLMTM patient myotubes showed that mutations that disrupt the interaction between myotubularin and MTMR12 proteins result in reduction of both myotubularin and MTMR12
The patients of Myopathy had a novel heterozygous splice site mutation in the myotubularin gene MTM1 (c.867+1G>T). Analysis of MTM1 cDNA revealed that the mutation resulted in aberrant splicing with variable exon skipping.
data explain the basis for phenotypic variability among human patients with MTM1 p.R69C mutations and establish the Mtm1 p.R69C mouse as a valuable model for the disease as its less severe phenotype will expand the scope of testable preclinical therapies
Sequence analysis of the entire coding region of the MTM1 gene identified a hemizygous deletion of the T nucleotide at position 431 in exon 6 (c.431delT [p.Leu144fs]
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