Kyushu University · Biochemistry, Genetics and Molecular Biology
Professor Motohiro Nishida's research lab focuses on cardiovascular pathophysiology, particularly the molecular mechanisms underlying cardiac remodeling, mitochondrial dynamics, and vascular dysfunction in heart disease and hypertension. The lab investigates key signaling pathways involving G protein-coupled receptors (e.g., AT1R and P2Y6R), ion channels (e.g., TRPC3), and cytoskeletal proteins (e.g., filamin A) in regulating cellular stress responses, senescence, and oxidative damage in cardiomyocytes and vascular cells. A central theme is the crosstalk between cellular structures like mitochondria and the cytoskeleton, and how their dysregulation contributes to heart failure and vascular disease. The lab also explores therapeutic targets to prevent chemotherapy-induced cardiotoxicity and hypertension-related organ damage.
Figures are computed from collected data and may differ slightly.
Defective mitochondrial dynamics through aberrant interactions between mitochondria and actin cytoskeleton is increasingly recognized as a key determinant of cardiac fragility after myocardial infarction (MI). Dynamin-related protein 1 (Drp1), a mitochondrial fission-accelerating factor, is activated locally at the fission site through interactions with actin. Here, we report that the actin-binding protein filamin A acted as a guanine nucleotide exchange factor for Drp1 and mediated mitochondria
The angiotensin (Ang) type 1 receptor (AT1R) promotes functional and structural integrity of the arterial wall to contribute to vascular homeostasis, but this receptor also promotes hypertension. In our investigation of how Ang II signals are converted by the AT1R from physiological to pathological outputs, we found that the purinergic P2Y6 receptor (P2Y6R), an inflammation-inducible G protein (heterotrimeric guanine nucleotide-binding protein)-coupled receptor (GPCR), promoted Ang II-induced hy
Myocardial atrophy is a wasting of cardiac muscle due to hemodynamic unloading. Doxorubicin is a highly effective anticancer agent but also induces myocardial atrophy through a largely unknown mechanism. Here, we demonstrate that inhibiting transient receptor potential canonical 3 (TRPC3) channels abolishes doxorubicin-induced myocardial atrophy in mice. Doxorubicin increased production of ROS in rodent cardiomyocytes through hypoxic stress-mediated upregulation of NADPH oxidase 2 (Nox2), which
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