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Tatsuomi Matsuoka - One of the best experts on this subject based on the ideXlab platform.
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resting cyst formation of Unicellular Organism colpoda and phosphorylation analyses by phos tag
Seibutsu Butsuri Kagaku, 2012Co-Authors: Tatsuomi Matsuoka, Yoichiro SogameAbstract:In the Unicellular eukaryote Colpoda cucullus, resting cyst formation (encystment), which is a cellular morphogenetic process, is mediated by intracellular signaling pathways, which are triggered by an inflow of Ca2+ due to cell-to-cell mechanical contact. The enhanced chemiluminescence detection (ECL) for phosphorylated proteins using biotinylated Phos-tag showed that the phosphorylation level in several proteins was enhanced in Ca2+-dependent manner prior to the beginning of the cyst formation (within 1 h after the onset of encystment induction). The cAMP enzyme immunoassay (EIA) showed that the intracellular cAMP concentration was elevated in encystment-induced cells. The encystment induction and the phosphorylation of some proteins are slightly promoted by the addition of membrane-permeable derivatives of cAMP or non-selective phosphodiesterase inhibitor, while they tend to be suppressed by the addition of an inhibitor of cAMP-dependent kinase (PKA). These results suggest that a Ca2+-activated signaling pathway involving cAMP/PKA-dependent protein phosphorylation may be responsible for the encystment induction of C. cucullus. Encystment-specific phosphorylated proteins were isolated by phosphate-affinity chromatography using Phos-tag agarose beads, and some of them were tentatively identified by mass spectrometry analysis.
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Immunochemical analysis of a photoreceptor protein using anti-IP3 receptor antibody in the Unicellular Organism, Blepharisma
Journal of Photochemistry and Photobiology B-biology, 2000Co-Authors: Tatsuomi Matsuoka, Naoko Moriyama, Akemi Kida, Tomohiko Suzuki, Kazuo Okuda, Hiyoshizo KotsukiAbstract:Abstract The blepharismin–200 kD protein complex of the ciliated protozoan Blepharisma is a novel type of photosensor responsible for the step-up photophobic response of the cell. In immunoblotting assays, the 200 kD protein is weakly cross-reacted with anti-inositol triphosphate receptor antibody (anti-IP 3 R antibody). Indirect immunofluorescence assays show that the pigment granules in which the blepharismin–200 kD protein complex is localized are labelled by anti-IP 3 R antibody. When the anti-IP 3 R antibody or antisense oligonucleotide for IP 3 receptor is introduced into the living cells of Blepharisma , both the photosensitivity of the cells and content of blepharismin–200 kD protein are reduced. The results suggest that the photoreceptor 200 kD protein is possibly an IP 3 receptor-like protein.
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photoreceptor pigment mediating swimming acceleration of blepharisma a Unicellular Organism
Microbios, 1999Co-Authors: Tatsuomi Matsuoka, M Sato, S MatsuokaAbstract:The ciliated protozoan Blepharisma japonicum which has a pink-coloured pigment called blepharismin shows a step-up photophobic response (ciliary reversal induced by a sudden increase in light intensity), followed by swimming acceleration (photokinetic response), dependent upon an absolute light intensity which is responsible for photodispersal. Pigmentless cells obtained by inhibiting pigment synthesis did not show swimming acceleration in response to continuous light stimulation. The action spectrum of swimming acceleration response of the pink-coloured (normal) cells resembled absorption spectra of blue-coloured pigments derived from pink-coloured blepharismin. The result suggests that blepharismin pigment is involved in the swimming acceleration response.
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blepharismin 1 5 novel photoreceptor from the Unicellular Organism blepharisma japonicum
ChemInform, 1998Co-Authors: Mitsuru Maeda, Hiyoshizo Kotsuki, Tatsuomi Matsuoka, Yoji Kato, Hideo Naoki, Kozo Utsumi, Takaharu TanakaAbstract:Abstract The structures of new photoreceptor molecules mediating the photobehavior of the Unicellular Organism, Blepharisma japonicum , were determined spectroscopically. These molecules had a 4-hydroxyphenyl-11H-dibenzo[a,o]cyclohepta[pqr]perylene moiety as a common chromophore structure.
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localization of blepharismin photosensors and identification of a photoreceptor complex mediating the step up photophobic response of the Unicellular Organism blepharisma
Photochemistry and Photobiology, 1997Co-Authors: Tatsuomi Matsuoka, Mitsuru Maeda, Hideo Naoki, Takaharu Tanaka, M Sato, Hiyoshizo KotsukiAbstract:Abstract— Photosensitivity for the step-up photophobic response of Blepharisma is localized in the anterior 1/5 of the cell body. Blepharismin pigment, which is believed to be a photoreceptor pigment mediating the step-up photophobic response of the cells, was separated into five types of blepharismin (BL-1, -2, -3, -4 and -5). Blepharismin-1, -3, -4 and -5 were localized in the posterior 4/5, while BL-2 was located over the entire cell body; the anterior end, which is the photosensitive region, contained only BL-2. The results indicate that a functional photoreceptor pigment mediating the step-up photophobic response is BL-2. Hydroxylapatite chromatography revealed that BL-2 was bound to a 200 kDa membrane protein. We concluded that a photoreceptor mediating the step-up photophobic response was a BL-2/200 kDa protein complex.
Hiyoshizo Kotsuki - One of the best experts on this subject based on the ideXlab platform.
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Immunochemical analysis of a photoreceptor protein using anti-IP3 receptor antibody in the Unicellular Organism, Blepharisma
Journal of Photochemistry and Photobiology B-biology, 2000Co-Authors: Tatsuomi Matsuoka, Naoko Moriyama, Akemi Kida, Tomohiko Suzuki, Kazuo Okuda, Hiyoshizo KotsukiAbstract:Abstract The blepharismin–200 kD protein complex of the ciliated protozoan Blepharisma is a novel type of photosensor responsible for the step-up photophobic response of the cell. In immunoblotting assays, the 200 kD protein is weakly cross-reacted with anti-inositol triphosphate receptor antibody (anti-IP 3 R antibody). Indirect immunofluorescence assays show that the pigment granules in which the blepharismin–200 kD protein complex is localized are labelled by anti-IP 3 R antibody. When the anti-IP 3 R antibody or antisense oligonucleotide for IP 3 receptor is introduced into the living cells of Blepharisma , both the photosensitivity of the cells and content of blepharismin–200 kD protein are reduced. The results suggest that the photoreceptor 200 kD protein is possibly an IP 3 receptor-like protein.
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blepharismin 1 5 novel photoreceptor from the Unicellular Organism blepharisma japonicum
ChemInform, 1998Co-Authors: Mitsuru Maeda, Hiyoshizo Kotsuki, Tatsuomi Matsuoka, Yoji Kato, Hideo Naoki, Kozo Utsumi, Takaharu TanakaAbstract:Abstract The structures of new photoreceptor molecules mediating the photobehavior of the Unicellular Organism, Blepharisma japonicum , were determined spectroscopically. These molecules had a 4-hydroxyphenyl-11H-dibenzo[a,o]cyclohepta[pqr]perylene moiety as a common chromophore structure.
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localization of blepharismin photosensors and identification of a photoreceptor complex mediating the step up photophobic response of the Unicellular Organism blepharisma
Photochemistry and Photobiology, 1997Co-Authors: Tatsuomi Matsuoka, Mitsuru Maeda, Hideo Naoki, Takaharu Tanaka, M Sato, Hiyoshizo KotsukiAbstract:Abstract— Photosensitivity for the step-up photophobic response of Blepharisma is localized in the anterior 1/5 of the cell body. Blepharismin pigment, which is believed to be a photoreceptor pigment mediating the step-up photophobic response of the cells, was separated into five types of blepharismin (BL-1, -2, -3, -4 and -5). Blepharismin-1, -3, -4 and -5 were localized in the posterior 4/5, while BL-2 was located over the entire cell body; the anterior end, which is the photosensitive region, contained only BL-2. The results indicate that a functional photoreceptor pigment mediating the step-up photophobic response is BL-2. Hydroxylapatite chromatography revealed that BL-2 was bound to a 200 kDa membrane protein. We concluded that a photoreceptor mediating the step-up photophobic response was a BL-2/200 kDa protein complex.
Yoji Kato - One of the best experts on this subject based on the ideXlab platform.
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blepharismin 1 5 novel photoreceptor from the Unicellular Organism blepharisma japonicum
ChemInform, 1998Co-Authors: Mitsuru Maeda, Hiyoshizo Kotsuki, Tatsuomi Matsuoka, Yoji Kato, Hideo Naoki, Kozo Utsumi, Takaharu TanakaAbstract:Abstract The structures of new photoreceptor molecules mediating the photobehavior of the Unicellular Organism, Blepharisma japonicum , were determined spectroscopically. These molecules had a 4-hydroxyphenyl-11H-dibenzo[a,o]cyclohepta[pqr]perylene moiety as a common chromophore structure.
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the photoreceptor pigment of the Unicellular Organism blepharisma generates hydroxyl radicals
Journal of Photochemistry and Photobiology B-biology, 1996Co-Authors: Yoji Kato, Yasunori Murakami, Yoshiya Watanabe, Yasuhiro Sagara, Masanori Sugiyama, Tatsuomi MatsuokaAbstract:Abstract The quinone pigment blepharismin isolated from Blepharisma, which is believed to be a photoreceptor pigment mediating photobehaviour (P. Scevoli, F. Bisi, G. Colombetti, F. Ghetti, F. Lenci and V. Passarelli, Photomotile responses of Blepharisma japonicum. I. Action spectra determination and time-resolved fluorescence of photoreceptor pigments, J. Photochem. Photobiol. B: Biol., 1 (1987) 75–84; T. Matsuoka, S. Matsuoka, Y. Yamaoka, T. Kuriu, Y. Watanabe, M. Takayanagi, Y. Kato and K. Taneda, Action spectra for step-up photophobic response in Blepharisma, J. Protozool., 39 (1992) 498–502), killed mammalian cells (L cells) when activated by light. Electron spin resonance (ESR) spectroscopy demonstrated that light-activated blepharismin generated hydroxyl radicals (.OH). Light-activated blepharismin pigment promoted lipid peroxidation of L cells, which was partially suppressed in the presence of the singlet oxygen quencher sodium azide (NaN3). The results suggest that the photodynamic action of blepharismin is correlated with lipid peroxidation which may be caused by hydroxyl radicals and/or singlet oxygen (1O2) produced via reactions sensitized by the pigment.
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additional evidence for blepharismin photoreceptor pigment mediating step up photophobic response of Unicellular Organism blepharisma
Photochemistry and Photobiology, 1995Co-Authors: Tatsuomi Matsuoka, Yoshiya Watanabe, Yasuhiro Sagara, Miyuki Takayanagi, Yoji KatoAbstract:In the ciliated protozoan, Blepharisma japonicum, the pink-colored pigment (blepharismin) contained in the pigment granules is believed to be the photoreceptor pigment responsible for the step-up photophobic response. When the cells partially bleached by extrusion of the pigment granules caused by cold shock were subsequently cultured under illuminated conditions, the pigment-less granules regenerated and the cells were further bleached (pigment content below 0.5%). The photosensitivity of such colorless cells disappeared completely. In contrast, the blepharismin pigment regenerated gradually when such colorless cells were transferred to darkness. The photosensitivity of the cells also recovered with regeneration of the pigment. We found that blepharismin pigment was not photobleached in the absence of O2. The step-up photophobic response was also completely repressed in the absence of O2. These results strongly confirm that blepharismin is a photoreceptor pigment mediating photobehavior of Blepharisma and that O2 is required for the early step in the phototransduction of the light-excited pigment.
Yoshihisa Nakano - One of the best experts on this subject based on the ideXlab platform.
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oscillation of adp ribosyl cyclase activity during the cell cycle and function of cyclic adp ribose in a Unicellular Organism euglena gracilis
FEBS Letters, 1997Co-Authors: Wataru Masuda, Shigeo Takenaka, Shingo Tsuyama, Kazutaka Miyatake, Hiroshi Nishina, Kiyoshi Inageda, Katsunobu Takahashi, Toshiaki Katada, Hiroshi Inui, Yoshihisa NakanoAbstract:Abstract In Euglena gracilis , the activity of ADP-ribosyl cyclase, which produces cyclic ADP-ribose, oscillated during the cell cycle in a synchronous culture induced by a light-dark cycle, and a marked increase in the activity was observed in the G2 phase. Similarly, the ADP-ribosyl cyclase activity rose extremely immediately before cell division started, when synchronous cell division was induced by adding cobalamin (which is an essential growth factor and participates in DNA synthesis in this Organism) to its deficient culture. Further, cADPR in these cells showed a maximum level immediately before cell division started. A dose-dependent Ca 2+ release was observed when microsomes were incubated with cADPR. © 1997 Federation of European Biochemical Societies.
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Cell cycle dependent ADP-ribosylation of a Unicellular Organism, Euglena gracilis Z
Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology, 1995Co-Authors: Shigeo Takenaka, Junko Inagaki, Shingo Tsuyama, Kazutaka Miyatake, Yoshihisa NakanoAbstract:Abstract Poly and mono ADP-ribosylation activities occur in Euglena gracilis Z. The ADP-ribosylation activity changes depending on the stage of cell cycle in cells synchronized by a light—dark cycle and shows two different peaks: the first in the S phase and the other in the G2-M transition. The latter has about two times greater activity compared to the former. Poly ADP-ribosylation occurred only in the S phase. Mono ADP-ribosylation occurred in the S phase and the G2-M transition. ADP-ribosylation activity was found in the cytosol, mitochondria and chloroplasts and also showed a change in activity dependent upon cell division.
Daohong Jiang - One of the best experts on this subject based on the ideXlab platform.
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proto oncogenes in a eukaryotic Unicellular Organism play essential roles in plasmodial growth in host cells
BMC Genomics, 2018Co-Authors: Tao Chen, Zhixiao Gao, Ying Zhao, Jiasen Cheng, Jiatao Xie, Daohong JiangAbstract:The eukaryotic Unicellular protist Plasmodiophora brassicae is an endocellular parasite of cruciferous plants. In host cortical cells, this protist develops a Unicellular structure that is termed the plasmodium. The plasmodium is actually a multinucleated cell, which subsequently splits and forms resting spores. The mechanism for the growth of this endocellular parasite in host cell is unclear. Here, combining de novo genome sequence and transcriptome analysis of strain ZJ-1, we identified top five significant enriched KEGG pathways of differentially expressed genes (DEGs), namely translation, cell growth and death, cell communication, cell motility and cancers. We detected 171 proto-oncogenes from the genome of P. brassicae that were implicated in cancer-related pathways, of which 46 were differential expression genes. Three predicted proto-oncogenes (Pb-Raf1, Pb-Raf2, and Pb-MYB), which showed homology to the human proto-oncogenes Raf and MYB, were specifically activated during the plasmodial growth in host cortical cells, demonstrating their involvement in the multinucleate development stage of the Unicellular protist Organism. Gene networks involved in the tumorigenic-related signaling transduction pathways and the activation of 12 core genes were identified. Inhibition of phosphoinositol-3-kinase relieved the clubroot symptom and significantly suppressed the development process of plasmodia. Proto-oncogene-related regulatory mechanisms play an important role in the plasmodial growth of P. brassicae.
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Proto-oncogenes in a eukaryotic Unicellular Organism play essential roles in plasmodial growth in host cells
BMC, 2018Co-Authors: Tao Chen, Zhixiao Gao, Ying Zhao, Jiasen Cheng, Jiatao Xie, Daohong JiangAbstract:Abstract Background The eukaryotic Unicellular protist Plasmodiophora brassicae is an endocellular parasite of cruciferous plants. In host cortical cells, this protist develops a Unicellular structure that is termed the plasmodium. The plasmodium is actually a multinucleated cell, which subsequently splits and forms resting spores. The mechanism for the growth of this endocellular parasite in host cell is unclear. Results Here, combining de novo genome sequence and transcriptome analysis of strain ZJ-1, we identified top five significant enriched KEGG pathways of differentially expressed genes (DEGs), namely translation, cell growth and death, cell communication, cell motility and cancers. We detected 171 proto-oncogenes from the genome of P. brassicae that were implicated in cancer-related pathways, of which 46 were differential expression genes. Three predicted proto-oncogenes (Pb-Raf1, Pb-Raf2, and Pb-MYB), which showed homology to the human proto-oncogenes Raf and MYB, were specifically activated during the plasmodial growth in host cortical cells, demonstrating their involvement in the multinucleate development stage of the Unicellular protist Organism. Gene networks involved in the tumorigenic-related signaling transduction pathways and the activation of 12 core genes were identified. Inhibition of phosphoinositol-3-kinase relieved the clubroot symptom and significantly suppressed the development process of plasmodia. Conclusions Proto-oncogene-related regulatory mechanisms play an important role in the plasmodial growth of P. brassicae
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Additional file 1: of Proto-oncogenes in a eukaryotic Unicellular Organism play essential roles in plasmodial growth in host cells
2018Co-Authors: Tao Chen, Zhixiao Gao, Ying Zhao, Jiasen Cheng, Jiatao Xie, Daohong JiangAbstract:Figure S1. Heatmap of DEGs of P. brassicae at three stages. IN, multinucleate secondary plasmodia stage in plant cortical cells; GS, germinating resting spores stage when the resting spores germinating and releasing primary zoospores; and RS, resting spores stage. (TIF 1974 kb
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Additional file 7: of Proto-oncogenes in a eukaryotic Unicellular Organism play essential roles in plasmodial growth in host cells
2018Co-Authors: Tao Chen, Zhixiao Gao, Ying Zhao, Jiasen Cheng, Jiatao Xie, Daohong JiangAbstract:Figure S3. Effect of PI3K inhibitor treatment on the growth, development of oilseed rape plants, resting spores germination rate and root hair infection rate of P. brassicae. a Growth and development status of oilseed rape plants treated with PI3K inhibitor (right). MOCK (DMSO) treatment served as control (left). The pictures of plants were taken at 28 day after treatment. Bar = 1.5 cm. b At 28 day after treatment, the roots of MOCK treated plants and inhibitor treated plants were harvested. The expression level of Cyclin gene (XM_013809141.1, downstream gene of PI3K signaling pathway) in B. napus with MOCK and inhibitor treatment was quantified by qPCR. The actin gene of B. napus was used as control to normalize the expression level. Data represent the means and standard deviations. The expression level of MOCK treated group was set as 1.0. Statistically significant difference of data between MOCK and inhibitor treated groups was compared, same letter in the graph indicates no significant differences at the level of P = 0.05. c-d Resting spores germination rate and root hair infection rate of P. brassicae were compared between H2O, MOCK and PI3K-Inhibitor treated groups. At 6 day, the treated spores were stained with orcein (Sigma-Aldrich Canada). The germination rate of spores was counted under microscope. At 7 dpi, the roots of oilseed rape plants were stained with Trypan Blue, then the root hair infection rate was counted with microscopic examination. The graphic data represent the means and standard deviations from three biological replicates. At the level of P = 0.05, statistically significant differences of data between H2O, MOCK and inhibitor treated groups were compared, same letters in the graph indicate no significant differences. (TIF 642 kb
