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15. Mutations of optineurin in amyotrophic lateral sclerosis

Author

Maruyama, Hirofumi, Morino, Hiroyuki, Ito, Hidefumi, Izumi, Yuishin, Kato, Hidemasa, Watanabe, Yasuhito, Kinoshita, Yoshimi, Kamada, Masaki, Nodera, Hiroyuki, Suzuki, Hidenori, Komure, Osamu, Matsuura, Shinya, Kobatake, Keitaro, Morimoto, Nobutoshi, Abe, Koji, Suzuki, Naoki, Aoki, Masashi, Kawata, Akihiro, Hirai, Takeshi, Kato, Takeo, Ogasawara, Kazumasa, Hirano, Asao, Takumi, Toru, Kusaka, Hirofumi, Hagiwara, Koichi, Kaji, Ryuji, and Kawakami, Hideshi

Subjects
Gene mutations -- Health aspects -- Research, Amyotrophic lateral sclerosis -- Genetic aspects -- Risk factors -- Research, Cellular proteins -- Physiological aspects -- Genetic aspects -- Research, Environmental issues, Science and technology, Zoology and wildlife conservation
Abstract

Amyotrophic lateral sclerosis (ALS) has its onset in middle age and is a progressive disorder characterized by degeneration of motor neurons of the primary motor cortex, brainstem and spinal cord (1). Most cases of ALS are sporadic, but about 10% are familial. Genes known to cause classic familial ALS (FALS) are superoxide dismutase 1 (SOD1) (2), ANG encoding angiogenin (3), TARDP encoding transactive response (TAR) DNA-binding protein TDP-43 (ref. 4) and fused in sarcoma/translated in liposarcoma (FUS, also known as TLS) (5,6). However, these genetic defects occur in only about 20-30% of cases of FALS, and most genes causing FALS are unknown. Here we show that there are mutations in the gene encoding optineurin (OPTN), earlier reported to be a causative gene of primary open-angle glaucoma (POAG) (7), in patients with ALS. We found three types of mutation of OPTN:ahomozygous deletion of exon 5, a homozygous Q398X nonsense mutation and a heterozygous E478G missense mutation within its ubiquitin-binding domain. Analysis of cell transfection showed that the nonsense and missense mutations of OPTN abolished the inhibition of activation of nuclear factor kappa B (NF-κB), and the E478G mutation revealed a cytoplasmic distribution different from that of the wild type or a POAG mutation. A case with the E478G mutation showed OPTN-immunoreactive cytoplasmic inclusions. Furthermore, TDP-43- or SOD1-positive inclusions of sporadic and SOD1 cases of ALS were also noticeably immunolabelled by anti-OPTN antibodies. Our findings strongly suggest that OPTN is involved in the pathogenesis of ALS. They also indicate that NF-κB inhibitors could be used to treat ALS and that transgenic mice bearing various mutations of OPTN will be relevant in developing new drugs for this disorder., We analysed six Japanese individuals from consanguineous marriages who had ALS; two of them were siblings, the others were from independent families. We used homozygosity mapping, which has been shown [...]

Published
2010
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23. BAC-DROP: Rapid Digestion of Proteome Fractionated via Dissolvable Polyacrylamide Gel Electrophoresis and Its Application to Bottom-Up Proteomics Workflow

Author

Takemori, Ayako, Ishizaki, Jun, Nakashima, Kenji, Shibata, Takeshi, Kato, Hidemasa, Kodera, Yoshio, Suzuki, Tetsuro, Hasegawa, Hitoshi, and Takemori, Nobuaki

Abstract

The GeLC–MS workflow, which combines low-cost, easy-to-use sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis (SDS-PAGE) with liquid chromatography–mass spectrometry (LC–MS), is very popular in current bottom-up proteomics. However, GeLC–MS requires that PAGE-separated proteins undergo overnight enzymatic digestion in a gel, resulting in more than 20 h of sample preparation for LC–MS. In this study, we overcame the limitations of GeLC–MS by developing a rapid digestion workflow for PAGE separation of proteins using N,N′-bis(acryloyl)cystamine (BAC) cross-linked gels that can be solubilized by reductive treatment. Making use of an established workflow called BAC-DROP (BAC-gel dissolution to digest PAGE-resolved objective proteins), crude proteome samples were fractionated based on molecular weight by BAC cross-linked PAGE. After fractionation, the gel fragments were reductively dissolved in under 5 min, and in-solution trypsin digestion of the protein released from the gel was completed in less than 1 h at 70 °C, equivalent to a 90–95% reduction in time compared to conventional in-gel trypsin digestion. The introduction of the BAC-DROP workflow to the MS assays for inflammatory biomarker CRP and viral marker HBsAg allowed for serum sample preparation to be completed in as little as 5 h, demonstrating successful marker quantification from a 0.5 μL sample of human serum.

Published
2021
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26. A Comprehensive Genomic Analysis Reveals the Genetic Landscape of Mitochondrial Respiratory Chain Complex Deficiencies

Author

50212220, 90396862, Kohda, Masakazu, Tokuzawa, Yoshimi, Kishita, Yoshihito, Nyuzuki, Hiromi, Moriyama, Yohsuke, Mizuno, Yosuke, Hirata, Tomoko, Yatsuka, Yukiko, Yamashita-Sugahara, Yzumi, Nakachi, Yutaka, Kato, Hidemasa, Okuda, Akihiko, Tamaru, Shunsuke, Borna, Nurun Nahar, Banshoya, Kengo, Aigaki, Toshiro, Sato-Miyata, Yukiko, Ohnuma, Kohei, Suzuki, Tsutomu, Nagao, Asuteka, Maehata, Hazuki, Matsuda, Fumihiko, Higasa, Koichiro, Nagasaki, Masao, Yasuda, Jun, Yamamoto, Masayuki, Fushimi, Takuya, Shimura, Masaru, Kaiho-Ichimoto, Keiko, Harashima, Hiroko, Yamazaki, Taro, Mori, Masato, Murayama, Kei, Ohtake, Akira, Okazaki, Yasushi, 50212220, 90396862, Kohda, Masakazu, Tokuzawa, Yoshimi, Kishita, Yoshihito, Nyuzuki, Hiromi, Moriyama, Yohsuke, Mizuno, Yosuke, Hirata, Tomoko, Yatsuka, Yukiko, Yamashita-Sugahara, Yzumi, Nakachi, Yutaka, Kato, Hidemasa, Okuda, Akihiko, Tamaru, Shunsuke, Borna, Nurun Nahar, Banshoya, Kengo, Aigaki, Toshiro, Sato-Miyata, Yukiko, Ohnuma, Kohei, Suzuki, Tsutomu, Nagao, Asuteka, Maehata, Hazuki, Matsuda, Fumihiko, Higasa, Koichiro, Nagasaki, Masao, Yasuda, Jun, Yamamoto, Masayuki, Fushimi, Takuya, Shimura, Masaru, Kaiho-Ichimoto, Keiko, Harashima, Hiroko, Yamazaki, Taro, Mori, Masato, Murayama, Kei, Ohtake, Akira, and Okazaki, Yasushi

Abstract

Mitochondrial disorders have the highest incidence among congenital metabolic disorders characterized by biochemical respiratory chain complex deficiencies. It occurs at a rate of 1 in 5, 000 births, and has phenotypic and genetic heterogeneity. Mutations in about 1, 500 nuclear encoded mitochondrial proteins may cause mitochondrial dysfunction of energy production and mitochondrial disorders. More than 250 genes that cause mitochondrial disorders have been reported to date. However exact genetic diagnosis for patients still remained largely unknown. To reveal this heterogeneity, we performed comprehensive genomic analyses for 142 patients with childhood-onset mitochondrial respiratory chain complex deficiencies. The approach includes whole mtDNA and exome analyses using high-throughput sequencing, and chromosomal aberration analyses using high-density oligonucleotide arrays. We identified 37 novel mutations in known mitochondrial disease genes and 3 mitochondria-related genes (MRPS23, QRSL1, and PNPLA4) as novel causative genes. We also identified 2 genes known to cause monogenic diseases (MECP2 and TNNI3) and 3 chromosomal aberrations (6q24.3-q25.1, 17p12, and 22q11.21) as causes in this cohort. Our approaches enhance the ability to identify pathogenic gene mutations in patients with biochemically defined mitochondrial respiratory chain complex deficiencies in clinical settings. They also underscore clinical and genetic heterogeneity and will improve patient care of this complex disorder.

Published
2016

27. A Comprehensive Genomic Analysis Reveals the Genetic Landscape of Mitochondrial Respiratory Chain Complex Deficiencies

Author

Kohda, Masakazu, primary, Tokuzawa, Yoshimi, additional, Kishita, Yoshihito, additional, Nyuzuki, Hiromi, additional, Moriyama, Yohsuke, additional, Mizuno, Yosuke, additional, Hirata, Tomoko, additional, Yatsuka, Yukiko, additional, Yamashita-Sugahara, Yzumi, additional, Nakachi, Yutaka, additional, Kato, Hidemasa, additional, Okuda, Akihiko, additional, Tamaru, Shunsuke, additional, Borna, Nurun Nahar, additional, Banshoya, Kengo, additional, Aigaki, Toshiro, additional, Sato-Miyata, Yukiko, additional, Ohnuma, Kohei, additional, Suzuki, Tsutomu, additional, Nagao, Asuteka, additional, Maehata, Hazuki, additional, Matsuda, Fumihiko, additional, Higasa, Koichiro, additional, Nagasaki, Masao, additional, Yasuda, Jun, additional, Yamamoto, Masayuki, additional, Fushimi, Takuya, additional, Shimura, Masaru, additional, Kaiho-Ichimoto, Keiko, additional, Harashima, Hiroko, additional, Yamazaki, Taro, additional, Mori, Masato, additional, Murayama, Kei, additional, Ohtake, Akira, additional, and Okazaki, Yasushi, additional

Published
2016
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29. Identification of Ccr4-Not Complex Components as Regulators of Transition from Partial to Genuine Induced Pluripotent Stem Cells

Author

Kamon, Masayoshi, primary, Katano, Miyuki, additional, Hiraki-Kamon, Keiko, additional, Hishida, Tomoaki, additional, Nakachi, Yutaka, additional, Mizuno, Yosuke, additional, Okazaki, Yasushi, additional, Suzuki, Ayumu, additional, Hirasaki, Masataka, additional, Ueda, Atsushi, additional, Nishimoto, Masazumi, additional, Kato, Hidemasa, additional, and Okuda, Akihiko, additional

Published
2014
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31. In Vivo Function and Evolution of the Eutherian-Specific Pluripotency Marker UTF1

Author

Nishimoto, Masazumi, primary, Katano, Miyuki, additional, Yamagishi, Toshiyuki, additional, Hishida, Tomoaki, additional, Kamon, Masayoshi, additional, Suzuki, Ayumu, additional, Hirasaki, Masataka, additional, Nabeshima, Yoko, additional, Nabeshima, Yo-ichi, additional, Katsura, Yukako, additional, Satta, Yoko, additional, Deakin, Janine E., additional, Graves, Jennifer A. Marshall, additional, Kuroki, Yoko, additional, Ono, Ryuichi, additional, Ishino, Fumitoshi, additional, Ema, Masatsugu, additional, Takahashi, Satoru, additional, Kato, Hidemasa, additional, and Okuda, Akihiko, additional

Published
2013
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46. In Vivo Function and Evolution of the Eutherian-Specific Pluripotency Marker UTF1.

Author

Nishimoto, Masazumi, Katano, Miyuki, Yamagishi, Toshiyuki, Hishida, Tomoaki, Kamon, Masayoshi, Suzuki, Ayumu, Hirasaki, Masataka, Nabeshima, Yoko, Nabeshima, Yo-ichi, Katsura, Yukako, Satta, Yoko, Deakin, Janine E., Graves, Jennifer A. Marshall, Kuroki, Yoko, Ono, Ryuichi, Ishino, Fumitoshi, Ema, Masatsugu, Takahashi, Satoru, Kato, Hidemasa, and Okuda, Akihiko

Subjects
BIOMARKERS, MAMMAL embryology, GENE expression in mammals, EMBRYONIC stem cells, GENETIC engineering, DEVELOPMENTAL biology, BIOLOGICAL evolution
Abstract

Embryogenesis in placental mammals is sustained by exquisite interplay between the embryo proper and placenta. UTF1 is a developmentally regulated gene expressed in both cell lineages. Here, we analyzed the consequence of loss of the UTF1 gene during mouse development. We found that homozygous UTF1 mutant newborn mice were significantly smaller than wild-type or heterozygous mutant mice, suggesting that placental insufficiency caused by the loss of UTF1 expression in extra-embryonic ectodermal cells at least in part contributed to this phenotype. We also found that the effects of loss of UTF1 expression in embryonic stem cells on their pluripotency were very subtle. Genome structure and sequence comparisons revealed that the UTF1 gene exists only in placental mammals. Our analyses of a family of genes with homology to UTF1 revealed a possible mechanism by which placental mammals have evolved the UTF1 genes. [ABSTRACT FROM AUTHOR]

Published
2013
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