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463 results on '"Saheki T"'

1. Citrin deficiency

Author

Saheki, T., Kobayashi, K., Iijima, M., Mil, M. A., Begum, L., Li, M. X., Nishi, I., Yasuda, T., Yamaguchi, N., Gao, H. Z., Lu, Y. B., Horiuchi, M., Jones, E. Anthony, editor, Meijer, Alfred J., editor, and Chamuleau, Robert A. F. M., editor

Published
2003
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22. Pathophysiology of citrin deficiency

Author

Saheki, T., primary, Kobayashi, K., additional, Iijima, M., additional, Li, M. X., additional, Horiuchi, M., additional, Tabata, A., additional, Lu, Y. B., additional, Ushikai, M., additional, Terashi, M., additional, and Moriyama, M., additional

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25. Mutations in argininosuccinate synthetase mRNA of Japanese patients, causing classical citrullinemia

Author

Kobayashi, K, Shaheen, N, Terazono, H, and Saheki, T

Subjects
Adult, DNA, Complementary, Base Sequence, Molecular Sequence Data, Infant, Newborn, Correction, Infant, Argininosuccinate Synthase, Mutagenesis, Insertional, Japan, Mutation, Citrulline, Humans, Female, Amino Acid Sequence, RNA, Messenger, Amino Acid Metabolism, Inborn Errors, Research Article
Abstract

Citrullinemia is an autosomal recessive disease caused by a genetic deficiency of argininosuccinate synthetase. In order to characterize mutations in Japanese patients with classical citrullinemia, RNA isolated from 10 unrelated patients was reverse-transcribed, and cDNA amplified by PCR was cloned and sequenced. The 10 mutations identified included 6 missense mutations (A118T, A192V, R272C, G280R, R304W, and R363L), 2 mutations associated with an absence of an exon 7 or exon 13, 1 mutation with a deletion of the first 7 bp in exon 16 (which might be caused by abnormal splicing), and 1 mutation with an insertion of 37 bp within exons 15 and 16 in cDNA. The insertion mutation and the five missense mutations (R304W being excluded) are new mutations described in the present paper. These are in addition to 14 mutations (9 missense mutations, 4 mutations associated with an absence of an exon in mRNA, and 1 splicing mutation) that we identified previously in mainly American patients with neonatal citrullinemia. Two of these 20 mutations, a deletion of exon 13 sequence and a 7-bp deletion in exon 16, were common to Japanese and American populations from different ethnic backgrounds; however, other mutations were unique to each population. Furthermore, the presence of a frequent mutation--the exon 7 deletion mutation in mRNA, which accounts for 10 of 23 affected alleles--was demonstrated in Japanese citrullinemia. This differs from the situation in the United States, where there was far greater heterogeneity of mutations.

Published
1994

45. Citrin and aralar1 are Ca2+-stimulated aspartate/glutamate transporters in mitochondria.

Author

Palmieri, L., Pardo, B., Lasorsa, F. M., del Arco, A., Kobayashi, K., Iijima, M., Runswick, M. J., Walker, J. E., Saheki, T., Satrüstegui, J., and Palmieri, F.

Subjects
ASPARTATE aminotransferase, GLUTAMINE synthetase, MITOCHONDRIA, CELLS, PROTEINS, ASPARTIC acid
Abstract

The mitochondrial aspartate/glutamate carrier catalyzes an important step in both the urea cycle and the aspartate/malate NADH shuttle. Citrin and aralar1 are homologous proteins belonging to the mitochondrial carrier family with EF-hand Ca2+-binding motifs in their N-terminal domains. Both proteins and their C-terminal domains were overexpressed in Escherichia coli, reconstituted into liposomes and shown to catalyze the electrogenic exchange of aspartate for glutamate and a H+. Overexpression of the carriers in transfected human cells increased the activity of the malate/aspartate NADH shuttle. These results demonstrate that citrin and aralar1 are isoforms of the hitherto unidentified aspartate/glutamate carrier and explain why mutations in citrin cause type II citrullinemia in humans. The activity of citrin and aralar1 as aspartate/glutamate exchangers was stimulated by Ca2+ on the external side of the inner mitochondrial membrane, where the Ca2+-binding domains of these proteins are localized. These results show that the aspartate/glutamate carrier is regulated by Ca2+ through a mechanism independent of Ca2+ entry into mitochondria, and suggest a novel mechanism of Ca2+ regulation of the aspartate/malate shuttle. [ABSTRACT FROM AUTHOR]

Published
2001
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