Knock-In Mouse Model of Dilated Cardiomyopathy Caused by Troponin Mutation
- C. Du, S. Morimoto, T. Sasaguri
- BiologyCirculation Research
- 20 July 2007
The hypothesis that Ca2+ desensitization of cardiac myofilament is the absolute cause of the pathogenesis of dilated cardiomyopathy associated with this mutation is verified and it is strongly suggested thatCa2+ sensitizers are beneficial for the treatment of Dilated carduomyopathy patients affected by sarcomeric regulatory protein mutations.
Functional consequences of the mutations in human cardiac troponin I gene found in familial hypertrophic cardiomyopathy.
- F. Takahashi‐Yanaga, S. Morimoto, I. Ohtsuki
- BiologyJournal of Molecular and Cellular Cardiology
- 1 December 2001
It is demonstrated that most of the HCM-linked cTnI mutations did affect the regulatory processes involving the cTNI molecule, and that at least five mutations increased the Ca(2+) sensitivity of cardiac muscle contraction.
Identification of an internal cis-element essential for the human L1 transcription and a nuclear factor(s) binding to the element.
- R. Minakami, K. Kurose, K. Etoh, Y. Furuhata, M. Hattori, Y. Sakaki
- BiologyNucleic Acids Research
- 25 June 1992
Results indicate that an internal short element located at the very 5' terminal of L1 sequence and the nuclear factor binding to the element play a crucial role in the transcription of human L1.
Phosphorylation and Calmodulin Binding of the Metabotropic Glutamate Receptor Subtype 5 (mGluR5) Are Antagonistic in Vitro *
- R. Minakami, N. Jinnai, H. Sugiyama
- Biology, ChemistryJournal of Biological Chemistry
- 8 August 1997
It is reported that calmodulin interacts with the metabotropic glutamate receptor subtype 5 (mGluR5) in a Ca2+-dependent manner in vitro and antagonisms of the CaM binding and phosphorylation suggest the possibility that they regulate the receptor responses in vivo.
Ca2+-desensitizing effect of a deletion mutation ΔK210 in cardiac troponin T that causes familial dilated cardiomyopathy
- S. Morimoto, Q. Lu, I. Ohtsuki
- BiologyProceedings of the National Academy of Sciences…
- 2 January 2002
The present study strongly suggests that Ca2+ desensitization of force generation in sarcomere is a primary mechanism for the pathogenesis of DCM associated with the deletion mutation ΔK210 in cTnT.
Targeted disruption of the cardiac troponin T gene causes sarcomere disassembly and defects in heartbeat within the early mouse embryo.
- K. Nishii, S. Morimoto, Y. Shibata
- BiologyDevelopmental Biology
- 1 October 2008
Phagocytosis-Coupled Activation of the Superoxide-Producing Phagocyte Oxidase, a Member of the NADPH Oxidase (Nox) Family
- R. Minakami, H. Sumimoto
- Biology, ChemistryInternational journal of hematology
- 1 October 2006
A current molecular model for phagocytosis-coupled activation of the NADPH oxidase is described, which involves the integrated function of cytoplasmic proteins that translocate to the phagosomal membrane to interact with cytochrome b558, leading to superoxide production.
The insert region of the Rac GTPases is dispensable for activation of superoxide-producing NADPH oxidases.
- K. Miyano, H. Koga, R. Minakami, H. Sumimoto
- BiologyBiochemical Journal
- 1 September 2009
It is shown that removal of the insert region from Rac1 neither affects activation of gp91phox/Nox2, which is reconstituted under cell-free and whole-cell conditions, nor blocks its localization to phagosomes during ingestion of IgG-coated beads by macrophage-like RAW264.7 cells.
Visualization of phagosomal hydrogen peroxide production by a novel fluorescent probe that is localized via SNAP-tag labeling.
- M. Abo, R. Minakami, H. Sumimoto
- Biology, ChemistryAnalytical Chemistry
- 6 June 2014
NBzF-BG, combined with the SNAP-tag technology, should be useful as a tool to measure local production of H2O2 in living cells.
Full‐length p40phox structure suggests a basis for regulation mechanism of its membrane binding
- K. Honbou, R. Minakami, F. Inagaki
- BiologyEMBO Journal
- 21 February 2007
It is shown that the PtdIns(3)P‐binding activity of p40phox is normally inhibited by the PB1 domain both in vivo and in vitro, and the crystal structure of the full‐length p 40phox reveals that the inhibition is mediated via intramolecular interaction between thePB1 and PX domains.
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