IBA57 mutations abrogate iron-sulfur cluster assembly leading to cavitating leukoencephalopathy

University of Yamanashi (山梨大学)博士(医学)医工博4甲第255号 Neurol Genet.2017 Sep 8;3(5):e184. に掲載、https://doi.org/10.1212/NXG.0000000000000184doctoral thesi

Failures as sons : a study of Saul Bellow

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Negative feedback by IRE1β optimizes mucin production in goblet cells

In mammals, the prototypical endoplasmic reticulum (ER) stress sensor inositol-requiring enzyme 1 (IRE1) has diverged into two paralogs. IRE1α is broadly expressed and mediates the unconventional splicing of X-box binding protein 1 (XBP1) mRNA during ER stress. By contrast, IRE1β is expressed selectively in the digestive tract, and its function remains unclear. Here, we report that IRE1β plays a distinctive role in mucin-secreting goblet cells. In IRE1β-/- mice, aberrant mucin 2 (MUC2) accumulated in the ER of goblet cells, accompanied by ER distension and elevated ER stress signaling such as increased XBP1 mRNA splicing. In contrast, conditional IRE1α-/- mice showed no such ER distension but a marked decrease in spliced XBP1 mRNA. mRNA stability assay revealed that MUC2 mRNA was greatly stabilized in IRE1β-/- mice. These findings suggest that in goblet cells, IRE1β, but not IRE1α, promotes efficient protein folding and secretion in the ER by optimizing the level of mRNA encoding their major secretory product, MUC2.journal articl

Observation of b→dγ and Determination of |Vtd/Vts|

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A Study of Buddhapālita's Mūlamadhyamakavṛtti (1)

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Additional file 1 of USP13 drives lung squamous cell carcinoma by switching lung club cell lineage plasticity

Additional file 1: Table S1

(A) Testicular cells, and sperm from cauda epididymis and vas deferens were ( ) or were not (-) treated with biotin or trypsin and then subjected to western blot analysis

ADAM2, known to be located at the sperm surface, was included as a control. TC, testicular (spermatogenic) cells; S, mature sperm from the epididymis and vas deferens. ADAM, a disintegrin and metalloprotease. (B) Sperm from the epididymis and vas deferens were fractionated into heads and tails. These fractions were subjected to western blot analysis. ADAM2 localized on sperm head and α-tubulin composing the axoneme in the sperm flagellum were used as control proteins.<p><b>Copyright information:</b></p><p>Taken from "Characterization of eight novel proteins with male germ cell-specific expression in mouse"</p><p>http://www.rbej.com/content/6/1/32</p><p>Reproductive biology and endocrinology : RB&E 2008;6():32-32.</p><p>Published online 24 Jul 2008</p><p>PMCID:PMC2500023.</p><p></p

(A) Acrosome reaction of sperm from the epididymis and vas deferens was induced by calcium ionophore A23187

Acrosome-intact and -reacted sperm were subjected to western blot anaylsis with the anti-Shsp1/Mm.87328 antibody. AI, acrosome-intact sperm; AR, acrosome-reacted sperm. (B) Sperm from the epididymis and vas deferens were treated with 1% Triton X-100 and urea with different concentrations (2, 3, 4 and 6 M). Soluble and insoluble fractions after centrifugation of the treated sperm were subjected to western blot anaylsis with the anti-Sfap1/Mm.386907 and anti-Sfap2/Mm.157049 antibodies. Sup, supernatant after centrifugation; Pt, pellet after centrifugation.<p><b>Copyright information:</b></p><p>Taken from "Characterization of eight novel proteins with male germ cell-specific expression in mouse"</p><p>http://www.rbej.com/content/6/1/32</p><p>Reproductive biology and endocrinology : RB&E 2008;6():32-32.</p><p>Published online 24 Jul 2008</p><p>PMCID:PMC2500023.</p><p></p

(A) Testicular germ cells were isolated from testis, boiled in 3% SDS with 5% β-mercaptoethanol, subjected to SDS-PAGE and blotted with antibodies

Two antibodies were used for the test of antibody specificity to each protein. The first one is a control antibody affinity-purified against GST (G) protein from each serum. The second one is a test antibody affinity-purified against each GST fusion protein (G-F) used for immunization and serum production. ADAM2, known to exhibit spermatogenic cell-specific expression, was included as a control. (B) GST or GST fusion (GST-F) proteins were added to a buffer containing the first antibodies during the incubation of immune blot analysis.<p><b>Copyright information:</b></p><p>Taken from "Characterization of eight novel proteins with male germ cell-specific expression in mouse"</p><p>http://www.rbej.com/content/6/1/32</p><p>Reproductive biology and endocrinology : RB&E 2008;6():32-32.</p><p>Published online 24 Jul 2008</p><p>PMCID:PMC2500023.</p><p></p

A de novo nonsense variant in the DMD gene associated with X‐linked dystrophin‐deficient muscular dystrophy in a cat

Abstract Background X‐linked dystrophin‐deficient muscular dystrophy (MD) is a form of MD caused by variants in the DMD gene. It is a fatal disease characterized by progressive weakness and degeneration of skeletal muscles. Hypothesis/Objectives Identify deleterious genetic variants in DMD by whole‐genome sequencing (WGS) using a next‐generation sequencer. Animals One MD‐affected cat, its parents, and 354 cats from a breeding colony. Methods We compared the WGS data of the affected cat with data available in the National Center for Biotechnology Information database and searched for candidate high‐impact variants by in silico analyses. Next, we confirmed the candidate variants by Sanger sequencing using samples from the parents and cats from the breeding colony. We used 2 genome assemblies, the standard felCat9 (from an Abyssinian cat) and the novel AnAms1.0 (from an American Shorthair cat), to evaluate genome assembly differences. Results We found 2 novel high‐impact variants: a 1‐bp deletion in felCat9 and an identical nonsense variant in felCat9 and AnAms1.0. Whole genome and Sanger sequencing validation showed that the deletion in felCat9 was a false positive because of misassembly. Among the 357 cats, the nonsense variant was only found in the affected cat, which indicated it was a de novo variant. Conclusion and Clinical Importance We identified a de novo variant in the affected cat and next‐generation sequencing‐based genotyping of the whole DMD gene was determined to be necessary for affected cats because the parents of the affected cat did not have the risk variant