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Your search keyword '"Takahashi, Masahide"' showing total 22 results
Start Over Author "Takahashi, Masahide" Journal pathology international
22 results on '"Takahashi, Masahide"'

1. Matrix remodeling‐associated protein 8 is a marker of a subset of cancer‐associated fibroblasts in pancreatic cancer

Author

Ichihara, Ryosuke, primary, Shiraki, Yukihiro, additional, Mizutani, Yasuyuki, additional, Iida, Tadashi, additional, Miyai, Yuki, additional, Esaki, Nobutoshi, additional, Kato, Akira, additional, Mii, Shinji, additional, Ando, Ryota, additional, Hayashi, Masamichi, additional, Takami, Hideki, additional, Fujii, Tsutomu, additional, Takahashi, Masahide, additional, and Enomoto, Atsushi, additional

Published
2022
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5. Development of a method to preliminarily embed tissue samples using low melting temperature fish gelatin before sectioning: A technical note

Author

Ushida, Kaori, Asai, Naoya, Uchiyama, Kozo, Enomoto, Atsushi, and Takahashi, Masahide

Subjects
tissue sample preparation, paraffin embedding, preliminary embedding, low melting temperature gelatin
Abstract

Embedding of tissue samples that maintains a desired orientation is critical for preparing sections suitable for diagnosis and study objectives. Methods to prepare tissue sections include: (i) paraffin embedding or snap‐freezing followed by microtome or cryostat sectioning; and (ii) agarose embedding followed by cutting on a vibrating microslicer. Although these methods are useful for routine laboratory work, preparation of small and fragile tissues such as mouse organs, small human biopsy samples, and cultured floating spheres is difficult and requires special skills. In particular, tissue specimen orientation can be lost during embedding in molds and subsequent sectioning. Here, we developed a method using low melting temperature (LM) gelatin either alone or mixed with agarose to preliminarily embed collected tissues that are either prefixed or unfixed, followed by conventional fixation, paraffin embedding, freezing, and sectioning. The advantage of the method is that the LM gelatin and its mixture with agarose can be handled at room temperature but quickly hardens at 4°C, which allows embedding, trimming, and arranging of small and fragile tissues in a desired orientation and are compatible with traditional stainings. Thus, this method can have various laboratory applications and can be modified according to the needs of each laboratory., ファイル公開：2019-04-02

Published
2018

8. CD109 expression in basal-like breast carcinoma

Author

Hasegawa, Masaki, Moritani, Suzuko, Murakumo, Yoshiki, Sato, Tomoko, Hagiwara, Sumitaka, Suzuki, Chikage, Mii, Shinji, Jijiwa, Mayumi, Enomoto, Atsushi, Asai, Naoya, Ichihara, Shu, and Takahashi, Masahide

Published
2008

18. Well-differentiated neuroendocrine tumor of the breast with extensive lymphatic and vascular infiltration

Author

Nakai, Tokiko, primary, Kawasaki, Tomonori, additional, Tada, Takashi, additional, Ishida, Motoo, additional, Iwakoshi, Akari, additional, Enomoto, Atsushi, additional, Okuda, Satoshi, additional, Takahashi, Masahide, additional, Ambo, Jun-ichi, additional, Sugai, Tamotsu, additional, Ohbayashi, Chiho, additional, and Ichihara, Shu, additional

Published
2016
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21. 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
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