Christiane Messaed

TL;DR: It is reported that protein aggregation in a cell model of OPMD directly impaires the function of the ubiquitin-proteasome pathway (UPP) as well as molecular chaperone functions and that molecular regulators of polyalanine protein solubility and degradation may provide insights into new mechanisms in O PMD pathogenesis.

TL;DR: It is proposed that the impaired cytokine trafficking and secretion caused by NLRP7 defects makes the patients tolerant to the growth of these earlier arrested conceptions with no fetal vessels and that the retention of these conceptions until the end of the first trimester contribute to the molar phenotype.

TL;DR: The results indicate that expanded PABPN1, presumably via the toxic effects of its polyalanine tract, can lead to inclusion formation and neurodegeneration in both the mouse and the human.

TL;DR: The hnRNP proteins are involved in mRNA processing and mRNA nucleocytoplasmic export, sequestering of hnRNPs in OPMD intranuclear aggregates supports the view that O PMD intanuclear inclusions are “poly(A) RNA traps”, which would interfere with RNA export, and cause muscle cell death.

TL;DR: This is the first report directly indicating that nuclear aggregation in OPMD may reflect an active process by which cells sequester and inactivate the soluble toxic form of expPABPN1.