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  1. Article ; Online: Characterization and localization of tropomyosin proteins in Xenopus embryos with specific antibodies.

    Tanaka, Tetsuya S / Tatsuta, Takashi / Ikenishi, Kohji

    Development, growth & differentiation

    2023  Volume 37, Issue 1, Page(s) 111–122

    Abstract: In the process of monoclonal antibody (mAb) production against the 38kDa protein which is lacking in the gastrula arrested mutant embryos in Xenopus we incidentally obtained two kinds of mAb (designated as B11 and 2D10 antibodies, respectively) ... ...

    Abstract In the process of monoclonal antibody (mAb) production against the 38kDa protein which is lacking in the gastrula arrested mutant embryos in Xenopus we incidentally obtained two kinds of mAb (designated as B11 and 2D10 antibodies, respectively) recognizing tropomyosin (TM) proteins in Xenopus embryos. The characterization of the corresponding antigens to those mAb was performed by immunoblotting and silver staining for two-dimensional (2-D) gels in the present study. The localization of the antigens in Xenopus embryos was also investigated by fluorescent microscopy. By 2-D immunoblots with those mAb, three distinct protein spots or TM isoforms were recognized in Xenopus embryos; a 38 kDa spot with a pl of approximately 4.8 reacted with both antibodies in embryos at stages later than the mid-tailbud (stage 28) and two 30 kDa spots, which are probably isomers, with a pl of approximately 4.8 were detected with 2D10 antibody in embryos at stages extending from the fertilized to the mid-neurula (stage 20). By immunofluorescent microscopy, B11 antibody was shown to react mainly with muscle cells and their precursor cells. In contrast, 2D10 antibody stained the cytoplasm of almost all cells in embryos at stages from the fertilized to the tadpole. Judging from the results obtained with immunoblotting and fluorescent microscopy, it is likely that the 38 kDa spot is a skeletal muscle TM isoform and the two 30 kDa spots are non-muscle TM isoforms.
    Language English
    Publishing date 2023-06-06
    Publishing country Japan
    Document type Journal Article
    ZDB-ID 280433-5
    ISSN 1440-169X ; 0012-1592
    ISSN (online) 1440-169X
    ISSN 0012-1592
    DOI 10.1046/j.1440-169X.1995.00013.x
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Quantitative Analysis of Glycerophospholipids in Mitochondria by Mass Spectrometry.

    Tatsuta, Takashi

    Methods in molecular biology (Clifton, N.J.)

    2017  Volume 1567, Page(s) 79–103

    Abstract: Lipids draw increasing attention of cell biologists because of the wide variety of functions beyond their role as building blocks of cellular membranes. Mitochondrial membranes possess characteristic lipid compositions that are intimately associated with ...

    Abstract Lipids draw increasing attention of cell biologists because of the wide variety of functions beyond their role as building blocks of cellular membranes. Mitochondrial membranes possess characteristic lipid compositions that are intimately associated with mitochondrial architecture and activities. Therefore, quantitative assessment of lipids in isolated mitochondria is of importance for mitochondrial research. Here, I describe our workflow for quantitative analysis of glycerophospholipids in mitochondria with a focus on purification of pure mitochondrial fractions from yeast and cultured mammalian cells as well as improved settings for the analysis of cardiolipin by nano-electrospray ionization mass spectrometry.
    Language English
    Publishing date 2017
    Publishing country United States
    Document type Journal Article
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-4939-6824-4_7
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Cervical Skeletal Muscle Metastasis of Colorectal Cancer.

    Tatsuta, Kyota / Harada, Takashi / Nishiwaki, Yoshiro

    Internal medicine (Tokyo, Japan)

    2021  Volume 61, Issue 2, Page(s) 263–264

    MeSH term(s) Carcinoma ; Colorectal Neoplasms ; Female ; Humans ; Muscle, Skeletal ; Uterine Cervical Neoplasms
    Language English
    Publishing date 2021-06-26
    Publishing country Japan
    Document type Journal Article
    ZDB-ID 32371-8
    ISSN 1349-7235 ; 0021-5120 ; 0918-2918
    ISSN (online) 1349-7235
    ISSN 0021-5120 ; 0918-2918
    DOI 10.2169/internalmedicine.7817-21
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: An intermolecular hydrogen bonded network in the PRELID-TRIAP protein family plays a role in lipid sensing.

    Miliara, Xeni / Tatsuta, Takashi / Eiyama, Akinori / Langer, Thomas / Rouse, Sarah L / Matthews, Steve

    Biochimica et biophysica acta. Proteins and proteomics

    2022  Volume 1871, Issue 1, Page(s) 140867

    Abstract: The PRELID-TRIAP1 family of proteins is responsible for lipid transfer in mitochondria. Multiple structures have been resolved of apo and lipid substrate bound forms, allowing us to begin to piece together the molecular level details of the full lipid ... ...

    Abstract The PRELID-TRIAP1 family of proteins is responsible for lipid transfer in mitochondria. Multiple structures have been resolved of apo and lipid substrate bound forms, allowing us to begin to piece together the molecular level details of the full lipid transfer cycle. Here, we used molecular dynamics simulations to demonstrate that the lipid binding is mediated by an extended, water-mediated hydrogen bonding network. A key mutation, R53E, was found to disrupt this network, causing lipid to be released from the complex. The X-ray crystal structure of R53E was captured in a fully closed and apo state. Lipid transfer assays and molecular simulations allow us to interpret the observed conformation in the context of the biological role. Together, our work provides further understanding of the mechanistic control of lipid transport by PRELID-TRIAP1 in mitochondria.
    MeSH term(s) Hydrogen ; Hydrogen Bonding ; Molecular Dynamics Simulation ; Lipids
    Chemical Substances Malononitrile dimer (OC6G895YHN) ; Hydrogen (7YNJ3PO35Z) ; Lipids
    Language English
    Publishing date 2022-10-26
    Publishing country Netherlands
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2918798-9
    ISSN 1878-1454 ; 1570-9639
    ISSN (online) 1878-1454
    ISSN 1570-9639
    DOI 10.1016/j.bbapap.2022.140867
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Prohibitins.

    Tatsuta, Takashi / Langer, Thomas

    Current biology : CB

    2017  Volume 27, Issue 13, Page(s) R629–R631

    Abstract: Tatsuta and Langer introduce prohibitins, membrane scaffolding proteins found predominantly ...

    Abstract Tatsuta and Langer introduce prohibitins, membrane scaffolding proteins found predominantly in mitochondria.
    MeSH term(s) Eukaryota/metabolism ; Membrane Proteins/metabolism ; Mitochondrial Proteins/metabolism ; Repressor Proteins/metabolism
    Chemical Substances Membrane Proteins ; Mitochondrial Proteins ; Repressor Proteins ; prohibitin
    Language English
    Publishing date 2017-07-10
    Publishing country England
    Document type Journal Article
    ZDB-ID 1071731-6
    ISSN 1879-0445 ; 0960-9822
    ISSN (online) 1879-0445
    ISSN 0960-9822
    DOI 10.1016/j.cub.2017.04.030
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: Defining the treatment strategy for uncomplicated appendicitis based on patient satisfaction feedback: A cross-sectional study.

    Tatsuta, Kyota / Miyazaki, Shinichiro / Ogiku, Masahito / Harada, Takashi / Yoshiro, Nishiwaki

    Asian journal of surgery

    2021  Volume 45, Issue 1, Page(s) 167–171

    Abstract: Background: Two surgical strategies are available for appendicitis: emergency laparoscopic appendectomy and interval laparoscopic appendectomy. However, timing of surgical intervention remains debatable. This study aimed to compare the surgical outcomes ...

    Abstract Background: Two surgical strategies are available for appendicitis: emergency laparoscopic appendectomy and interval laparoscopic appendectomy. However, timing of surgical intervention remains debatable. This study aimed to compare the surgical outcomes of emergency laparoscopic appendectomy and interval laparoscopic appendectomy and conduct a questionnaire survey to investigate the use of emergency laparoscopic appendectomy and patient satisfaction with regard to treatment.
    Methods: We included 162 patients who underwent laparoscopic appendectomy at our hospital. Outcomes were assessed by operation time, blood loss, postoperative fasting time, length of hospital stay, and complication rate. Patient satisfaction was measured by questionnaire addressing degree of satisfaction, presurgery anxiety, and length of hospital stay.
    Results: Of 162 patients, 74 (46%) and 88 (54%) received emergency and interval laparoscopic appendectomy, respectively. No significant difference was observed in the operation time, blood loss, length of hospital stay, or complication rate. Among 66 patients who responded to the questionnaire (28 emergency, 38 interval), a significant difference was observed only in the degree of satisfaction regarding the timing of the surgical intervention (p = 0.04).
    Conclusion: Surgical outcomes of emergency and interval appendectomy were equivalent; however, patient satisfaction favored emergency appendectomy, suggesting it is a preferable approach for the treatment of uncomplicated appendicitis.
    MeSH term(s) Appendectomy ; Appendicitis/surgery ; Cross-Sectional Studies ; Feedback ; Humans ; Laparoscopy ; Length of Stay ; Patient Satisfaction ; Postoperative Complications ; Retrospective Studies
    Language English
    Publishing date 2021-05-07
    Publishing country China
    Document type Journal Article
    ZDB-ID 1068461-x
    ISSN 0219-3108 ; 1015-9584
    ISSN (online) 0219-3108
    ISSN 1015-9584
    DOI 10.1016/j.asjsur.2021.04.021
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article ; Online: Mitochondria regulate intracellular coenzyme Q transport and ferroptotic resistance via STARD7.

    Deshwal, Soni / Onishi, Mashun / Tatsuta, Takashi / Bartsch, Tim / Cors, Eileen / Ried, Katharina / Lemke, Kathrin / Nolte, Hendrik / Giavalisco, Patrick / Langer, Thomas

    Nature cell biology

    2023  Volume 25, Issue 2, Page(s) 246–257

    Abstract: Coenzyme Q (or ubiquinone) is a redox-active lipid that serves as universal electron carrier in the mitochondrial respiratory chain and antioxidant in the plasma membrane limiting lipid peroxidation and ferroptosis. Mechanisms allowing cellular coenzyme ... ...

    Abstract Coenzyme Q (or ubiquinone) is a redox-active lipid that serves as universal electron carrier in the mitochondrial respiratory chain and antioxidant in the plasma membrane limiting lipid peroxidation and ferroptosis. Mechanisms allowing cellular coenzyme Q distribution after synthesis within mitochondria are not understood. Here we identify the cytosolic lipid transfer protein STARD7 as a critical factor of intracellular coenzyme Q transport and suppressor of ferroptosis. Dual localization of STARD7 to the intermembrane space of mitochondria and the cytosol upon cleavage by the rhomboid protease PARL ensures the synthesis of coenzyme Q in mitochondria and its transport to the plasma membrane. While mitochondrial STARD7 preserves coenzyme Q synthesis, oxidative phosphorylation function and cristae morphogenesis, cytosolic STARD7 is required for the transport of coenzyme Q to the plasma membrane and protects against ferroptosis. A coenzyme Q variant competes with phosphatidylcholine for binding to purified STARD7 in vitro. Overexpression of cytosolic STARD7 increases ferroptotic resistance of the cells, but limits coenzyme Q abundance in mitochondria and respiratory cell growth. Our findings thus demonstrate the need to coordinate coenzyme Q synthesis and cellular distribution by PARL-mediated STARD7 processing and identify PARL and STARD7 as promising targets to interfere with ferroptosis.
    MeSH term(s) Biological Transport ; Electron Transport ; Mitochondria/metabolism ; Mitochondrial Membranes/metabolism ; Oxidation-Reduction ; Ubiquinone/pharmacology ; Ubiquinone/metabolism ; Carrier Proteins/metabolism
    Chemical Substances Ubiquinone (1339-63-5) ; Carrier Proteins
    Language English
    Publishing date 2023-01-19
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1474722-4
    ISSN 1476-4679 ; 1465-7392
    ISSN (online) 1476-4679
    ISSN 1465-7392
    DOI 10.1038/s41556-022-01071-y
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article ; Online: Long-term prognosis after stapled and hand-sewn ileal pouch-anal anastomoses for familial adenomatous polyposis: a multicenter retrospective study.

    Tatsuta, Kyota / Sakata, Mayu / Iwaizumi, Moriya / Okamoto, Kazuya / Yoshii, Shigeto / Mori, Masashi / Asaba, Yutaro / Harada, Takashi / Shimizu, Mikihiro / Kurachi, Kiyotaka / Takeuchi, Hiroya

    International journal of colorectal disease

    2024  Volume 39, Issue 1, Page(s) 32

    Abstract: Purpose: The long-term prognosis of stapled and hand-sewn ileal pouch-anal anastomoses in familial adenomatous polyposis patients in Japan remains unknown. This study aimed to compare the overall survival in familial adenomatous polyposis patients who ... ...

    Abstract Purpose: The long-term prognosis of stapled and hand-sewn ileal pouch-anal anastomoses in familial adenomatous polyposis patients in Japan remains unknown. This study aimed to compare the overall survival in familial adenomatous polyposis patients who underwent stapled or hand-sewn ileal pouch-anal anastomosis.
    Methods: This multicenter retrospective study was conducted at 12 institutions in Shizuoka Prefecture, Japan. The clinical outcomes of 53 eligible familial adenomatous polyposis patients who underwent stapled (n = 24) and hand-sewn (n = 29) ileal pouch-anal anastomosis were compared.
    Results: The median follow-up duration was 171.5 months. The incidence of adenoma in the remnant rectum or anal transitional zone and metachronous rectal cancer was significantly more common in stapled ileal pouch-anal anastomosis (adenoma: stapled, 45.8%, vs. hand-sewn, 10.3%, p = 0.005; metachronous rectal cancer: 29.2%, vs. none, p = 0.002). The number of deaths was remarkably higher in stapled ileal pouch-anal anastomosis (p = 0.002). Metachronous rectal cancer was the most common cause of death. Overall survival was worse in stapled ileal pouch-anal anastomosis than in hand-sewn ileal pouch-anal anastomosis (120 months, 90.7% vs. 96.6%; 240 months, 63.7% vs. 96.6%; p = 0.044). Cox regression analysis revealed the independent effects of preoperative advanced colorectal cancer and stapled ileal pouch-anal anastomosis on overall survival.
    Conclusion: Stapled ileal pouch-anal anastomosis negatively affected the overall survival of familial adenomatous polyposis patients. Therefore, hand-sewn ileal pouch-anal anastomosis is recommended for better prognosis in these patients.
    MeSH term(s) Humans ; Retrospective Studies ; Anastomosis, Surgical/adverse effects ; Proctocolectomy, Restorative/adverse effects ; Adenomatous Polyposis Coli/surgery ; Prognosis ; Adenoma ; Rectal Neoplasms/surgery ; Colonic Pouches/adverse effects ; Treatment Outcome
    Language English
    Publishing date 2024-03-02
    Publishing country Germany
    Document type Multicenter Study ; Journal Article
    ZDB-ID 84975-3
    ISSN 1432-1262 ; 0179-1958
    ISSN (online) 1432-1262
    ISSN 0179-1958
    DOI 10.1007/s00384-024-04608-9
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: Protein quality control in mitochondria.

    Tatsuta, Takashi

    Journal of biochemistry

    2009  Volume 146, Issue 4, Page(s) 455–461

    Abstract: Mitochondria are crucial for both life and death of eukaryotic cells. Compromised mitochondrial integrity has severe cellular consequences and is linked to senescence and neurodegenerative disorders in humans. To maintain the functionality of proteins in ...

    Abstract Mitochondria are crucial for both life and death of eukaryotic cells. Compromised mitochondrial integrity has severe cellular consequences and is linked to senescence and neurodegenerative disorders in humans. To maintain the functionality of proteins in mitochondria, quality-control mechanisms including signal transduction pathways counteracting mitochondrial stress have evolved. A network of molecular chaperones and proteases monitors protein integrity and prevents accumulation of damaged proteins. In this review, the current knowledge of elaborate defence strategies within mitochondria is summarized.
    MeSH term(s) Humans ; Mitochondria/chemistry ; Mitochondria/metabolism ; Mitochondrial Proteins/chemistry ; Mitochondrial Proteins/metabolism ; Molecular Chaperones/chemistry ; Molecular Chaperones/metabolism ; Peptide Hydrolases/chemistry ; Peptide Hydrolases/metabolism ; Signal Transduction
    Chemical Substances Mitochondrial Proteins ; Molecular Chaperones ; Peptide Hydrolases (EC 3.4.-)
    Language English
    Publishing date 2009-10
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 218073-x
    ISSN 1756-2651 ; 0021-924X
    ISSN (online) 1756-2651
    ISSN 0021-924X
    DOI 10.1093/jb/mvp122
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article: Intramitochondrial phospholipid trafficking

    Tatsuta, Takashi / Thomas Langer

    Biochimica et biophysica acta. 2017 Jan., v. 1862, no. 1

    2017  

    Abstract: Mitochondrial functions and architecture rely on a defined lipid composition of their outer and inner membranes, which are characterized by a high content of non-bilayer phospholipids such as cardiolipin (CL) and phosphatidylethanolamine (PE). ... ...

    Abstract Mitochondrial functions and architecture rely on a defined lipid composition of their outer and inner membranes, which are characterized by a high content of non-bilayer phospholipids such as cardiolipin (CL) and phosphatidylethanolamine (PE). Mitochondrial membrane lipids are synthesized in the endoplasmic reticulum (ER) or within mitochondria from ER-derived precursor lipids, are asymmetrically distributed within mitochondria and can relocate in response to cellular stress. Maintenance of lipid homeostasis thus requires multiple lipid transport processes to be orchestrated within mitochondria. Recent findings identified members of the Ups/PRELI family as specific lipid transfer proteins in mitochondria that shuttle phospholipids between mitochondrial membranes. They cooperate with membrane organizing proteins that preserve the spatial organization of mitochondrial membranes and the formation of membrane contact sites, unravelling an intimate crosstalk of membrane lipid transport and homeostasis with the structural organization of mitochondria.This article is part of a Special Issue entitled: Lipids of Mitochondria edited by Guenther Daum.
    Keywords cardiolipins ; endoplasmic reticulum ; homeostasis ; lipid transfer proteins ; mitochondria ; mitochondrial membrane ; phosphatidylethanolamines
    Language English
    Dates of publication 2017-01
    Size p. 81-89.
    Publishing place Elsevier B.V.
    Document type Article
    ISSN 1388-1981
    DOI 10.1016/j.bbalip.2016.08.006
    Database NAL-Catalogue (AGRICOLA)

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