Updated on 2025/08/22

写真a

 
KAI Masahiro
 
Organization
School of Medicine Department of Molecular Biology Lecturer
Title
Lecturer
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Degree

  • Ph.D.

Research Interests

  • 生化学

Research Areas

  • Life Science / Molecular biology

Education

  • Tokyo Institute of Technology

    - 1993

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    Country: Japan

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  • Tokyo Institute of Technology

    - 1993

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Professional Memberships

Papers

  • Screening for long noncoding RNAs associated with oral squamous cell carcinoma reveals the potentially oncogenic actions of DLEU1. Reviewed International journal

    Koyo Nishiyama, Reo Maruyama, Takeshi Niinuma, Masahiro Kai, Hiroshi Kitajima, Mutsumi Toyota, Yui Hatanaka, Tomohiro Igarashi, Jun-Ichi Kobayashi, Kazuhiro Ogi, Hironari Dehari, Akihiro Miyazaki, Akira Yorozu, Eiichiro Yamamoto, Masashi Idogawa, Yasushi Sasaki, Tamotsu Sugai, Takashi Tokino, Hiroyoshi Hiratsuka, Hiromu Suzuki

    Cell death & disease   9 ( 8 )   826 - 826   2018.8

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    Recent studies have shown that long noncoding RNAs (lncRNAs) have pivotal roles in human malignancies, although their significance in oral squamous cell carcinoma (OSCC) is not fully understood. In the present study, we identified lncRNAs functionally associated with OSCC. By analyzing RNA-seq datasets obtained from primary head and neck squamous cell carcinoma (HNSCC), we identified 15 lncRNAs aberrantly expressed in cancer tissues. We then validated their expression in 18 OSCC cell lines using qRT-PCR and identified 6 lncRNAs frequently overexpressed in OSCC. Among those, we found that knocking down DLEU1 (deleted in lymphocytic leukemia 1) strongly suppressed OSCC cell proliferation. DLEU1 knockdown also suppressed migration, invasion, and xenograft formation by OSCC cells, which is suggestive of its oncogenic functionality. Microarray analysis revealed that DLEU1 knockdown significantly affects expression of a number of cancer-related genes in OSCC cells, including HAS3, CD44, and TP63, suggesting that DLEU1 regulates HA-CD44 signaling. Expression of DLEU1 was elevated in 71% of primary OSCC tissues, and high DLEU1 expression was associated with shorter overall survival of HNSCC patients. These data suggest that elevated DLEU1 expression contributes to OSCC development, and that DLEU1 may be a useful therapeutic target in OSCC.

    DOI: 10.1038/s41419-018-0893-2

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  • A Screen for Epigenetically Silenced microRNA Genes in Gastrointestinal Stromal Tumors. Reviewed International journal

    Mai Isosaka, Takeshi Niinuma, Masanori Nojima, Masahiro Kai, Eiichiro Yamamoto, Reo Maruyama, Takayuki Nobuoka, Toshirou Nishida, Tatsuo Kanda, Takahiro Taguchi, Tadashi Hasegawa, Takashi Tokino, Koichi Hirata, Hiromu Suzuki, Yasuhisa Shinomura

    PloS one   10 ( 7 )   e0133754   2015

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    BACKGROUND: Dysregulation of microRNA (miRNA) has been implicated in gastrointestinal stromal tumors (GISTs) but the mechanism is not fully understood. In this study, we aimed to explore the involvement of epigenetic alteration of miRNA genes in GISTs. METHODS: GIST-T1 cells were treated with 5-aza-2'-deoxycytidine (5-aza-dC) and 4-phenylbutyric acid (PBA), after which miRNA expression profiles were analyzed using TaqMan miRNA arrays. DNA methylation was then analyzed using bisulfite pyrosequencing. The functions of miRNAs were examined using MTT assays, wound-healing assays, Boyden chamber assays and Matrigel invasion assays. Gene expression microarrays were analyzed to assess effect of ectopic miRNA expression in GIST-T1 cells. RESULTS: Of the 754 miRNAs analyzed, 61 were significantly upregulated in GIST-T1 cells treated with 5-aza-dC plus PBA. Among those, 21 miRNA genes were associated with an upstream CpG island (CGI), and the CGIs of miR-34a and miR-335 were frequently methylated in GIST-T1 cells and primary GIST specimens. Transfection of miR-34a or miR-335 mimic molecules into GIST-T1 cells suppressed cell proliferation, and miR-34a also inhibited migration and invasion by GIST-T1 cells. Moreover, miR-34a downregulated a number of predicted target genes, including PDGFRA. RNA interference-mediated knockdown of PDGFRA in GIST-T1 cells suppressed cell proliferation, suggesting the tumor suppressive effect of miR-34a is mediated, at least in part, through targeting PDGFRA. CONCLUSIONS: Our results suggest that miR-34a and miR-335 are candidate tumor suppressive miRNAs in GISTs, and that they are frequent targets of epigenetic silencing in GISTs.

    DOI: 10.1371/journal.pone.0133754

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  • IGFBP7 is a p53-responsive gene specifically silenced in colorectal cancer with CpG island methylator phenotype. Reviewed International journal

    Hiromu Suzuki, Shinichi Igarashi, Masanori Nojima, Reo Maruyama, Eiichiro Yamamoto, Masahiro Kai, Hirofumi Akashi, Yoshiyuki Watanabe, Hiroyuki Yamamoto, Yasushi Sasaki, Fumio Itoh, Kohzoh Imai, Tamotsu Sugai, Lanlan Shen, Jean-Pierre J Issa, Yasuhisa Shinomura, Takashi Tokino, Minoru Toyota

    Carcinogenesis   31 ( 3 )   342 - 9   2010.3

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    A subset of colorectal cancers (CRCs) show simultaneous methylation of multiple genes; these tumors have the CpG island methylator phenotype (CIMP). CRCs with CIMP show a specific pattern of genetic alterations, including a high frequency of BRAF mutations and a low frequency of p53 mutations. We therefore hypothesized that genes inactivated by DNA methylation are involved in the BRAF- and p53-signaling pathways. Among those, we examined the epigenetic inactivation of insulin-like growth factor-binding protein 7 (IGFBP7) expression in CRCs. We found that in CRC cell lines, the silencing of IGFBP7 expression was correlated with high levels of DNA methylation and low levels of histone H3K4 methylation. Luciferase and chromatin immunoprecipitation assays in unmethylated cells revealed that p53 induces expression of IGFBP7 upon binding to a p53 response element within intron 1 of the gene. Treating methylated CRC cell lines with 5-aza-2'-deoxycytidine restored p53-induced IGFBP7 expression. Levels of IGFBP7 methylation were also significantly higher in primary CRC specimens than in normal colonic tissue (P < 0.001). Methylation of IGFBP7 was correlated with BRAF mutations, an absence of p53 mutations and the presence of CIMP. Thus, epigenetic inactivation of IGFBP7 appears to play a key role in tumorigenesis of CRCs with CIMP by enabling escape from p53-induced senescence.

    DOI: 10.1093/carcin/bgp179

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  • Diacylglycerol kinase η augments C-raf activity and B-Raf/C-Raf heterodimerization Reviewed

    Satoshi Yasuda, Masahiro Kai, Shin Ichi Imai, Kazuki Takeishi, Akinobu Taketomi, Minoru Toyota, Hideo Kanoh, Fumio Sakane

    Journal of Biological Chemistry   284 ( 43 )   29559 - 29570   2009.10

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    DOI: 10.1074/jbc.M109.043604

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  • Diacylglycerol kinase α enhances protein kinase Cζ-dependent phosphorylation at Ser311 of p65/RelA subunit of nuclear factor-κB Reviewed

    Masahiro Kai, Satoshi Yasuda, Shin ichi Imai, Minoru Toyota, Hideo Kanoh, Fumio Sakane

    FEBS Letters   583 ( 19 )   3265 - 3268   2009.10

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    DOI: 10.1016/j.febslet.2009.09.017

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  • Diacylglycerol kinase delta associates with receptor for activated C kinase 1, RACK1 Reviewed

    Shin-ichi Imai, Satoshi Yasuda, Masahiro Kai, Hideo Kanoh, Fumio Sakane

    BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR AND CELL BIOLOGY OF LIPIDS   1791 ( 4 )   246 - 253   2009.4

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    DOI: 10.1016/j.bbalip.2009.01.024

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  • Phorbol ester and hydrogen peroxide synergistically induce the interaction of diacylglycerol kinase γ with the Src homology 2 and C1 domains of β2-chimaerin Reviewed

    Satoshi Yasuda, Masahiro Kai, Shin Ichi Imai, Hideo Kanoh, Fumio Sakane

    Biochemical Journal   409 ( 1 )   95 - 106   2008.1

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    DOI: 10.1042/BJ20070848

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  • Rab7 regulates maturation of melanosomal matrix protein gp100/Pmel17/Silv Reviewed

    Akinori Kawakami, Fumio Sakane, Shin-Ichi Imai, Satoshi Yasuda, Masahiro Kai, Hideo Kanoh, Hai-Ying Jin, Kuninori Hirosaki, Toshiharu Yamashita, David E. Fisher, Kowichi Jimbow

    JOURNAL OF INVESTIGATIVE DERMATOLOGY   128 ( 1 )   143 - 150   2008.1

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    DOI: 10.1038/sj.jid.5700964

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  • Tyrosine phosphorylation of beta2-chimaerin by Src-family kinase negatively regulates its Rac-specific GAP activity. Reviewed International journal

    Masahiro Kai, Satoshi Yasuda, Shin-Ichi Imai, Hideo Kanoh, Fumio Sakane

    Biochimica et biophysica acta   1773 ( 9 )   1407 - 15   2007.9

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    beta2-Chimaerin, an intracellular receptor for the second messenger diacylglycerol and phorbol esters, is a GTPase-activating protein (GAP) specific for Rac. beta2-Chimaerin negatively controls many Rac-dependent pathophysiological events including tumor development. However, the regulatory mechanism of beta2-chimaerin remains largely unknown. Here we report that beta2-chimaerin is tyrosine-phosphorylated by Src-family kinases (SFKs) upon cell stimulation with epidermal growth factor (EGF). Mutational analysis identified Tyr-21 in the N-terminal regulatory region as a major phosphorylation site. Intriguingly, the addition of SFK inhibitor and the replacement of Tyr-21 with Phe (Y21F) markedly enhanced Rac-GAP activity of beta2-chimaerin in EGF-treated cells. Moreover, the Y21F mutant inhibited integrin-dependent cell spreading, in which Rac1 plays a critical role, more strongly than wild-type beta2-chimaerin. These results suggest Tyr-21 phosphorylation as a novel, SFK-dependent mechanism that negatively regulates beta2-chimaerin Rac-GAP activity.

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  • Tyrosine phosphorylation of beta 2-chimaerin by Src-family kinase negatively regulates its Rac-specific GAP activity Reviewed

    Masahiro Kai, Satoshi Yasuda, Shin-ichi Imai, Hideo Kanoh, Fumio Sakane

    BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH   1773 ( 9 )   1407 - 1415   2007.9

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    DOI: 10.1016/j.bbamcr.2007.05.004

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  • Diacylglycerol kinases: why so many of them? Reviewed International journal

    Fumio Sakane, Shin-Ichi Imai, Masahiro Kai, Satoshi Yasuda, Hideo Kanoh

    Biochimica et biophysica acta   1771 ( 7 )   793 - 806   2007.7

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    Diacylglycerol (DAG) kinase (DGK) modulates the balance between the two signaling lipids, DAG and phosphatidic acid (PA), by phosphorylating DAG to yield PA. To date, ten mammalian DGK isozymes have been identified. In addition to the C1 domains (protein kinase C-like zinc finger structures) conserved commonly in all DGKs, these isoforms possess a variety of regulatory domains of known and/or predicted functions, such as a pair of EF-hand motifs, a pleckstrin homology domain, a sterile alpha motif domain and ankyrin repeats. Beyond our expectations, recent studies have revealed that DGK isozymes play pivotal roles in a wide variety of signal transduction pathways conducting development, neural and immune responses, cytoskeleton reorganization and carcinogenesis. Moreover, there has been rapidly growing evidence indicating that individual DGK isoforms exert their specific roles through interactions with unique partner proteins such as protein kinase Cs, Ras guanyl nucleotide-releasing protein, chimaerins and phosphatidylinositol-4-phosphate 5-kinase. Therefore, an emerging paradigm for DGK is that the individual DGK isoforms assembled in their own signaling complexes should carry out spatio-temporally segregated tasks for a wide range of biological processes via regulating local, but not global, concentrations of DAG and/or PA.

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  • Diacylglycerol kinase alpha suppresses tumor necrosis factor-alpha-induced apoptosis of human melanoma cells through NF-kappaB activation. Reviewed International journal

    Kenji Yanagisawa, Satoshi Yasuda, Masahiro Kai, Shin-ichi Imai, Keiko Yamada, Toshiharu Yamashita, Kowichi Jimbow, Hideo Kanoh, Fumio Sakane

    Biochimica et biophysica acta   1771 ( 4 )   462 - 74   2007.4

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    We investigated the implication of diacylglycerol kinase (DGK) alpha (type I isoform) in melanoma cells because we found that this DGK isoform was expressed in several human melanoma cell lines but not in noncancerous melanocytes. Intriguingly, the overexpression of wild-type (WT) DGKalpha, but not of its kinase-dead (KD) mutant, markedly suppressed tumor necrosis factor (TNF)-alpha-induced apoptosis of AKI human melanoma cells. In the reverse experiment, siRNA-mediated knockdown of DGKalpha significantly enhanced the apoptosis. The overexpression of other type I isoforms (DGKbeta and DGKgamma) had, on the other hand, no detectable effects on the apoptosis. These results indicate that DGKalpha specifically suppresses the TNF-alpha-induced apoptosis through its catalytic action. We found that the overexpression of DGKalpha-WT, but not of DGKalpha-KD, further enhanced the TNF-alpha-stimulated transcriptional activity of an anti-apoptotic factor, NF-kappaB. Conversely, DGKalpha-knockdown considerably inhibited the NF-kappaB activity. Moreover, an NF-kappaB inhibitor blunted the anti-apoptotic effect of DGKalpha overexpression. Together, these results strongly suggest that DGKalpha is a novel positive regulator of NF-kappaB, which suppresses TNF-alpha-induced melanoma cell apoptosis.

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  • Diacylglycerol kinase alpha suppresses tumor necrosis factor-alpha- -induced apoptosis of human melanoma cells through NF-kappa B activation Reviewed

    Kenji Yanagisawa, Satoshi Yasuda, Masahiro Kai, Shin-ichi Imai, Keiko Yamada, Toshiharu Yamashita, Kowichi Jimbow, Hideo Kanoh, Fumio Sakane

    BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR AND CELL BIOLOGY OF LIPIDS   1771 ( 4 )   462 - 474   2007.4

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    DOI: 10.1016/j.bbalip.2006.12.008

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  • Diacylglycerol kinase γ interacts with and activates β2-chimaerin, a Rac-specific GAP, in response to epidermal growth factor Reviewed

    Satoshi Yasuda, Masahiro Kai, Shin ichi Imai, Hideo Kanoh, Fumio Sakane

    FEBS Letters   581 ( 3 )   551 - 557   2007.2

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    DOI: 10.1016/j.febslet.2007.01.022

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  • Lipid phosphate phosphatases 1 and 3 are localized in distinct lipid rafts Reviewed

    Masahiro Kai, Fumio Sakane, Yan-Jun Jia, Shin-ichi Imai, Satoshi Yasuda, Hideo Kanoh

    JOURNAL OF BIOCHEMISTRY   140 ( 5 )   677 - 686   2006.11

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    DOI: 10.1093/jb/mvj195

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  • Nuclear transportation of diacylglycerol kinase gamma and its possible function in the nucleus. Reviewed International journal

    Takehiro Matsubara, Yasuhito Shirai, Kei Miyasaka, Takuya Murakami, Yasuto Yamaguchi, Takehiko Ueyama, Masahiro Kai, Fumio Sakane, Hideo Kanoh, Toshiaki Hashimoto, Shinji Kamada, Ushio Kikkawa, Naoaki Saito

    The Journal of biological chemistry   281 ( 10 )   6152 - 64   2006.3

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    Diacylglycerol kinases (DGKs) convert diacylglycerol (DG) to phosphatidic acid, and both lipids are known to play important roles in lipid signal transduction. Thereby, DGKs are considered to be a one of the key players in lipid signaling, but its physiological function remains to be solved. In an effort to investigate one of nine subtypes, we found that DGKgamma came to be localized in the nucleus with time in all cell lines tested while seen only in the cytoplasm at the early stage of culture, indicating that DGKgamma is transported from the cytoplasm to the nucleus. The nuclear transportation of DGKgamma didn't necessarily need DGK activity, but its C1 domain was indispensable, suggesting that the C1 domain of DGKgamma acts as a nuclear transport signal. Furthermore, to address the function of DGKgamma in the nucleus, we produced stable cell lines of wild-type DGKgamma and mutants, including kinase negative, and investigated their cell size, growth rate, and cell cycle. The cells expressing the kinase-negative mutant of DGKgamma were larger in size and showed slower growth rate, and the S phase of the cells was extended. These findings implicate that nuclear DGKgamma regulates cell cycle.

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  • Identification and characterization of a novel human type II diacylglycerol kinase, DGK kappa Reviewed

    S Imai, M Kai, S Yasuda, H Kanoh, F Sakane

    JOURNAL OF BIOLOGICAL CHEMISTRY   280 ( 48 )   39870 - 39881   2005.12

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    DOI: 10.1074/jbc.M500669200

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MISC

  • 大腸がんにおけるdiacylglycerol kinase zeta遺伝子バリアントのエピジェネティックな制御

    甲斐 正広, 新沼 猛, 北嶋 洋志, 丸山 玲緒, 山本 英一郎, 鈴木 拓

    日本癌学会総会記事   75回   P - 1061   2016.10

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    Ichushi

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  • 大腸がんのDNAメチル化異常におけるTET1関与の可能性(Possible role of TET1 dysregulation to induce aberrant DNA methylation in colorectal cancer)

    鈴木 拓, 丸山 玲緒, 津矢田 明泰, 新沼 猛, 山本 英一郎, 伊早坂 舞, 甲斐 正広, 篠村 恭久, 今井 浩三

    日本癌学会総会記事   73回   P - 1122   2014.9

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  • DGKGは大腸がん細胞の増殖・浸潤・遊走をその酵素活性によらず抑制する(DGKG attenuates proliferation, invasion and migration of colorectal cancer cells independently of its enzymic activity)

    甲斐 正広, 山本 英一郎, 丸山 玲緒, 佐藤 亜紀子, 新沼 猛, 津矢田 明泰, 鈴木 拓

    日本癌学会総会記事   72回   341 - 341   2013.10

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  • 悪性黒色腫の細胞浸潤におけるDGK-γの関与(DGK-gamma is involved in suppression of malignant melanoma cell invasion)

    佐藤 亜紀子, 甲斐 正広, 鈴木 拓, 山本 英一郎, 丸山 玲緒, 西坂 尚大, 山下 利春

    日本癌学会総会記事   71回   359 - 359   2012.8

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    Ichushi

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  • Diacylglycerol kinases as emerging potential drug targets for a variety of diseases

    Fumio Sakane, Shin-ichi Imai, Masahiro Kai, Satoshi Yasuda, Hideo Kanoh

    CURRENT DRUG TARGETS   9 ( 8 )   626 - 640   2008.8

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  • Diacylglycerol kinases: Why so many of them?

    Fumio Sakane, Shin-ichi Imai, Masahiro Kai, Satoshi Yasuda, Hideo Kanoh

    BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR AND CELL BIOLOGY OF LIPIDS   1771 ( 7 )   793 - 806   2007.7

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    DOI: 10.1016/j.bbalip.2007.04.006

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  • ジアシルグリセロールキナーゼγは細胞刺激に応答し β2-chimaerin (Rac特異的GAP)を活性化する

    安田 智, 甲斐 正広, 今井 伸一, 坂根 郁夫, 加納 英雄

    脂質生化学研究   49   302 - 304   2007.6

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  • β2-chimaerin のチロシンリン酸化によるRac特異的GAP活性の抑制

    甲斐 正広, 安田 智, 今井 伸一, 坂根 郁夫, 加納 英雄

    脂質生化学研究   49   312 - 315   2007.6

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  • The plasma membrane translocation of diacylglycerol kinase delta 1 is negatively regulated by conventional protein kinase C-dependent phosphorylation at Ser-22 and Ser-26 within the pleckstrin homology domain

    S Imai, M Kai, K Yamada, H Kanoh, F Sakane

    BIOCHEMICAL JOURNAL   382 ( 3 )   957 - 966   2004.9

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  • Heparin-binding EGF-like growth factor is a promising target for ovarian cancer therapy

    S Miyamoto, M Hirata, A Yamazaki, T Kageyama, H Hasuwa, H Mizushima, Y Tanaka, H Yagi, K Sonoda, M Kai, H Kanoh, H Nakano, E Mekada

    CANCER RESEARCH   64 ( 16 )   5720 - 5727   2004.8

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  • Diacylglycerol kinase gamma serves as an upstream suppressor of Rac1 and lamellipodium formation

    S Tsushima, M Kai, K Yamada, S Imai, K Houkin, H Kanoh, F Sakane

    JOURNAL OF BIOLOGICAL CHEMISTRY   279 ( 27 )   28603 - 28613   2004.7

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  • Differential localization of lipid phosphate phosphatases 1 and 3 to cell surface subdomains in polarized MDCK cells

    YJ Jia, M Kai, Wada, I, F Sakane, H Kanoh

    FEBS LETTERS   552 ( 2-3 )   240 - 246   2003.9

  • Cell surface activities of the human type 2b phosphatidic acid phosphatase

    T Ishikawa, M Kai, Wada, I, H Kanoh

    JOURNAL OF BIOCHEMISTRY   127 ( 4 )   645 - 651   2000.4

  • Molecular characterization of the type 2 phosphatidic acid phosphatase

    H Kanoh, M Kai, Wada, I

    CHEMISTRY AND PHYSICS OF LIPIDS   98 ( 1-2 )   119 - 126   1999.4

  • ホスファチジン酸ホスファターゼ

    蛋白質・核酸・酵素   44   983 - 8   1999

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  • [Phosphatidic acid phosphatase]

    Tanpakushitsu Kakusan Koso.   44   983 - 8   1999

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  • Phosphatidic acid phosphatase (type 2), haloperoxidase family and germ cell migration

    Wada, I, M Kai, H Kanoh

    SEIKAGAKU   70 ( 9 )   1183 - 1188   1998.9

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  • ホスファチジン酸ホスファターゼ2型とハロペルオキシダーゼファミリーと生殖細胞ガイダンス.

    生化学   70   1185 - 8   1998

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  • Cloning and characterization of two human isozymes of Mg2+-independent phosphatidic acid phosphatase

    M Kai, Wada, I, S Imai, F Sakane, H Kanoh

    JOURNAL OF BIOLOGICAL CHEMISTRY   272 ( 39 )   24572 - 24578   1997.9

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  • Promotion of transferrin folding by cyclic interactions with calnexin and calreticulin

    Wada, I, M Kai, S Imai, F Sakane, H Kanoh

    EMBO JOURNAL   16 ( 17 )   5420 - 5432   1997.9

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  • Phosphatidic acid phosphatase from mammalian tissues: discovery of channel-like proteins with unexpected functions

    H Kanoh, M Kai, Wada, I

    BIOCHIMICA ET BIOPHYSICA ACTA-LIPIDS AND LIPID METABOLISM   1348 ( 1-2 )   56 - 62   1997.9

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  • Translocation of diacylglycerol kinase alpha to the nuclear matrix of rat thymocytes and peripheral T-lymphocytes

    Wada, I, M Kai, S Imai, F Sakane, H Kanoh

    FEBS LETTERS   393 ( 1 )   48 - 52   1996.9

  • Molecular properties of enzymes involved in diacylglycerol and phosphatidate metabolism

    H Kanoh, M Kai, Wada, I

    JOURNAL OF LIPID MEDIATORS AND CELL SIGNALLING   14 ( 1-3 )   245 - 250   1996.9

  • Identification and cDNA cloning of 35-kDa phosphatidic acid phosphatase (Type 2) bound to plasma membranes - Polymerase chain reaction amplification of mouse H2O2-inducible hic53 clone yielded the cDNA encoding phosphatidic acid phosphatase

    M Kai, Wada, I, S Imai, F Sakane, H Kanoh

    JOURNAL OF BIOLOGICAL CHEMISTRY   271 ( 31 )   18931 - 18938   1996.8

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  • Molecular cloning of a novel diacylglycerol kinase isozyme with a pleckstrin homology domain and a C-terminal tail similar to those the EPH family of protein-tyrosine kinases

    F Sakane, S Imai, M Kai, Wada, I, H Kanoh

    JOURNAL OF BIOLOGICAL CHEMISTRY   271 ( 14 )   8394 - 8401   1996.4

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  • The C-terminal part of diacylglycerol kinase alpha lacking zinc fingers serves as a catalytic domain.

    Biochem J   318   583 - 90   1996

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  • LOCALIZATION OF THE GENE ENCODING DIACYLGLYCEROL-KINASE-3 (DAGK3) TO HUMAN-CHROMOSOME 3Q27-28 AND MOUSE CHROMOSOME-16

    J FITZGIBBON, D WELLS, A PILZ, J DELHANTY, M KAI, H KANOH, D HUNT

    CURRENT EYE RESEARCH   14 ( 11 )   1041 - 1043   1995.11

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  • CHAPERONE FUNCTION OF CALRETICULIN WHEN EXPRESSED IN THE ENDOPLASMIC-RETICULUM AS THE MEMBRANE-ANCHORED AND SOLUBLE FORMS

    WADA, I, S IMAI, M KAI, F SAKANE, H KANOH

    JOURNAL OF BIOLOGICAL CHEMISTRY   270 ( 35 )   20298 - 20304   1995.9

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  • MOLECULAR-CLONING OF A DIACYLGLYCEROL KINASE ISOZYME PREDOMINANTLY EXPRESSED IN HUMAN RETINA WITH A TRUNCATED AND INACTIVE ENZYME EXPRESSION IN MOST OTHER HUMAN-CELLS

    M KAI, F SAKANE, S IMAI, WADA, I, H KANOH

    JOURNAL OF BIOLOGICAL CHEMISTRY   269 ( 28 )   18492 - 18498   1994.7

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Research Projects

  • リン脂質代謝酵素の機能解析

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    Grant type:Competitive

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