Papers - NISHIHARA, Hiroshi

Tumor angiogenesis and dynamic CT in lung adenocarcinoma: Radiologic-Pathologic correlation

Ukihide Tateishi, Hiroshi Nishihara, Satoshi Watanabe, Toshiaki Morikawa, Kazuhiro Abe, Kazuo Miyasaka

Journal of Computer Assisted Tomography 25 ( 1 ) 23 - 27 2001

Research paper (scientific journal), Joint Work, Accepted,  ISSN  0363-8715

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Purpose: The purpose of this work was to evaluate the correlation of tumor angiogenesis and dynamic CT in lung adenocarcinoma. Method: Thirty-five consecutive patients with lung adenocarcinoma underwent dynamic chest CT. Maximum attenuation of dynamic CT was compared with microvessel densities (MVDs) and vascular endothelial growth factor (VEGF) expression by immunohistochemistry. Results: The mean peak attenuation (APA) of lung adenocarcinoma correlated with MVD (r = 0.689, p &lt
0.0001). VEGF positiveness of lung adenocarcinoma was 63%. There was a significant difference in APA between VEGF-positive and -negative lung adenocarcinomas (39.9 ± 3.9 and 24.3 ± 2.3
p &lt
0.05). The mean MVDs of VEGF-positive adenocarcinomas were significantly higher than those of negative ones (82.5 ± 5.9 and 49.2 ± 7.1
p &lt
0.05). The mean APA of VEGF-positive lung adenocarcinomas correlated positively with MVD (r = 0.707, p &lt
0.0001). Conclusion: The APA value of dynamic CT reflects MVD in lung adenocarcinoma. The APA value of dynamic CT might be an index for VEGF-related tumor angiogenesis.

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High-resolution CT findings of macrophage activation syndrome: a case report.

Tateishi U, Nishihara H, Okano M, Kobayashi R, Kobayashi I, Fujita N

Pediatric radiology 30 ( 10 ) 699 - 701 2000.10

Accepted,  ISSN  0301-0449

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Non-adherent cell-specific expression of DOCK2, a member of the human CDM-family proteins

Hiroshi Nishihara, Shin Kobayashi, Yuko Hashimoto, Fumiyo Ohba, Naoki Mochizuki, Takeshi Kurata, Kazuo Nagashima, Michiyuki Matsuda

Biochimica et Biophysica Acta - Molecular Cell Research 1452 ( 2 ) 179 - 187 1999.11

Accepted,  ISSN  0167-4889

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Human DOCK180, which was originally identified as a major protein bound to the Crk oncogene product, is an archetype of the CDM family of proteins, including Ced-5 of Caenorhabditis elegans and Mbc of Drosophila melanogaster. After DOCK180, at least three putative human proteins that manifest high amino acid sequence similarity to DOCK180 have been registered in the GenBank/EMBL database. We have designated one of them, KIAA0209, as DOCK2 and characterize here. DOCK2 mRNA was expressed mostly in peripheral blood cells, followed by slight expression in the spleen and thymus, whereas DOCK180 was expressed in all tissues tested except in peripheral blood cells. Immunostaining of human cadaver tissues revealed that the expression of DOCK2 was limited to the lymphocytes and macrophages of various organs. DOCK2 bound to and activated Rac1, as did DOCK180
however, DOCK2 did not bind to CrkII, which transduces signals at focal adhesions. Thus, DOCK180 and DOCK2 are regulators of Rac and function in adherent and non-adherent cells, respectively.

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JCウイルスcapsid proteinの機能的領域に対する抗体を用いた免疫組織学的検索と感染抑制実験

西原 広史, 小林 希, 佐藤 真実, 宍戸 由紀子, 岡田 由紀, 田中 伸哉, 澤 洋文, 古林 与志安, 長嶋 和郎

日本病理学会会誌 ((一社)日本病理学会)  88 ( 1 ) 333 - 333 1999.03

Accepted,  ISSN  0300-9181

Constitutive association of EGF receptor with the CrkII-23 mutant that inhibits transformation of NRK cells by EGF and TGF-beta

S Ota, S Kizaka-Kondoh, Y Hashimoto, H Nishihara, K Nagashima, T Kurata, H Okayama, M Matsuda

CELLULAR SIGNALLING (ELSEVIER SCIENCE INC)  10 ( 4 ) 283 - 290 1998.04

Accepted,  ISSN  0898-6568

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Crk belongs to the adapter proteins that participate in many signalling pathways from cell surface receptors. We have characterised the CrkII-23 mutant that inhibits the transformation of NRK cells induced by epidermal growth factor (EGF) and transforming growth factor (TGF)-beta. To study the biochemical difference, cDNAs of the wild-type CrkII and the CrkII-23 mutant were introduced stably into NIH 3T3 cells expressing EGF receptor (EGFR). Both CrkII and CrkII-23 were phosphorylated on tyrosine upon EGF simulation with similar time course and dose dependency. Whereas the wild-type CrkII bound to EGFR only after EGF stimulation, CrkII-23 bound to EGFR from before stimulation. Mutation in the Src homology (SH) 2 or amino terminal SH3 domain did not abolish the binding of CrkII-23 to EGFR in the quiescent cells, suggesting that the binding is mediated by a novel mechanism. These CrkII-23-derived mutants, however, did not suppress transformation of NRK cells by EGF and TGF-beta. Hence, both the SH2 and amino-terminal SH3 domains are required to inhibit transformation of NRK cells. These results suggest that persistent signalling from CrkII-23 bound to EGFR suppresses transformation by EGF and TGF-beta in NRK23 cells. (C) 1998 Elsevier Science Inc.