Search

Your search keyword '"Iwahashi, Naoko"' showing total 18 results
Start Over Author "Iwahashi, Naoko"
18 results on '"Iwahashi, Naoko"'

15. A CASE OF PERFORATED DUODENAL DIVERTICULUM

Author

HASEGAWA, Takeshi, primary, KAMIYA, Yasuhiro, additional, IWAHASHI, Naoko, additional, KITAMURA, Souji, additional, MURAMOTO, Masayuki, additional, ASANO, Miki, additional, ISHII, Toshiharu, additional, SATAKE, Akira, additional, TAKEUCHI, Yasushi, additional, OKUBO, Takashi, additional, USAMI, Shizuo, additional, and KOTANI, Hikozou, additional

Published
1996
Full Text
View/download PDF

17. Different nuclear/cytoplasmic distributions of RET finger protein in different cell types.

Author

Takahashi, Masahide, Tezel, Gaye, Nagasaka, Tetsuro, Iwahashi, Naoko, Asai, Naoya, Iwashita, Toshihide, and Sakata, Keita

Subjects
ZINC proteins, IMMUNOHISTOCHEMISTRY, PLASMA cells, PLASMACYTOMA
Abstract

The RET finger protein (RFP), which belongs to the B box zinc finger protein family, has a tripartite motif consisting of a Ring finger, a B box finger and a coiled-coil domain. The RET finger protein becomes oncogenic when its tripartite motif is fused with the tyrosine kinase domain of the RET protein. This study examined the RFP expression in normal and tumor tissues by immunohistochemistry. RFP was detected in the nuclei of various cells, including peripheral and central neurones, hepatocytes, adrenal chromaffin cells and male germ cells. Among them, RFP was expressed at high levels in male germ cells such as primary spermatocytes and round spermatids, and formed a perinuclear cap structure in primary spermatocytes. On the other hand, high levels of cytoplasmic expression of RFP were observed in some plasma cells as well as solitary plasmacytoma and multiple myeloma. These results suggested that different nuclear/cytoplasmic distributions of RFP might play a role in the regulation of growth or differentiation of different cell types. [ABSTRACT FROM AUTHOR]

Published
1999
Full Text
View/download PDF

18. Molecular Cloning of Macrophin, a Human Homologue of DrosophilaKakapo with a Close Structural Similarity to Plectin and Dystrophin

Author

Okuda, Takahito, Matsuda, Satoru, Nakatsugawa, Shigekazu, Ichigotani, Yasukatu, Iwahashi, Naoko, Takahashi, Masahide, Ishigaki, Takeo, and Hamaguchi, Michinari

Abstract

We have determined the complete cDNA coding sequence of a novel cytoskeletal protein by the degenerative primer-mediated PCR strategy. This novel gene, named as macrophin (microfilament and actin filament cross-linker protein related to plectin and dystrophin, Accession No. AB029290), appears to be a human homologue of a Drosophilagene, kakapo,and shows close similarity to plectin and dystrophin on the search of BLAST homology-computed database. Comparison of the deduced protein sequences for macrophin and kakapo revealed that they were 66% similar, and both of them have an NH2-terminal actin-binding domain, a central rod region composed of spectrin-like repeats, and COOH-terminal Gas2-related region. The predicted sequences for macrophin are 5430 amino acids in length with a calculated molecular mass of 620 kDa, which is one of the largest size idenfied in human cytoskeletal proteins. High expression of macrophin was observed in brain, heart, lung, placenta, liver, kidney, and pancreas. In pancreas, we found that macrophin was specifically expressed in acinar cells than islet cells by in situhybridization. By using radiation hybrid panel, we have mapped the macrophingene to the chromosome 1p31-32.

Published
1999
Full Text
View/download PDF

Catalog

Books, media, physical & digital resources
See catalog results