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1. TRPC6 counteracts TRPC3-Nox2 protein complex leading to attenuation of hyperglycemia-induced heart failure in mice

Author

Sayaka Oda, Takuro Numaga-Tomita, Naoyuki Kitajima, Takashi Toyama, Eri Harada, Tsukasa Shimauchi, Akiyuki Nishimura, Tatsuya Ishikawa, Yoshito Kumagai, Lutz Birnbaumer, and Motohiro Nishida

Subjects
Medicine, Science
Abstract

Abstract Excess production of reactive oxygen species (ROS) caused by hyperglycemia is a major risk factor for heart failure. We previously reported that transient receptor potential canonical 3 (TRPC3) channel mediates pressure overload-induced maladaptive cardiac fibrosis by forming stably functional complex with NADPH oxidase 2 (Nox2). Although TRPC3 has been long suggested to form hetero-multimer channels with TRPC6 and function as diacylglycerol-activated cation channels coordinately, the role of TRPC6 in heart is still obscure. We here demonstrated that deletion of TRPC6 had no impact on pressure overload-induced heart failure despite inhibiting interstitial fibrosis in mice. TRPC6-deficient mouse hearts 1 week after transverse aortic constriction showed comparable increases in fibrotic gene expressions and ROS production but promoted inductions of inflammatory cytokines, compared to wild type hearts. Treatment of TRPC6-deficient mice with streptozotocin caused severe reduction of cardiac contractility with enhancing urinary and cardiac lipid peroxide levels, compared to wild type and TRPC3-deficient mice. Knockdown of TRPC6, but not TRPC3, enhanced basal expression levels of cytokines in rat cardiomyocytes. TRPC6 could interact with Nox2, but the abundance of TRPC6 was inversely correlated with that of Nox2. These results strongly suggest that Nox2 destabilization through disrupting TRPC3-Nox2 complex underlies attenuation of hyperglycemia-induced heart failure by TRPC6.

Published
2017
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2. TRPC6 counteracts TRPC3-Nox2 protein complex leading to attenuation of hyperglycemia-induced heart failure in mice

Author

Yoshito Kumagai, Tsukasa Shimauchi, Akiyuki Nishimura, Sayaka Oda, Naoyuki Kitajima, Eri Harada, Lutz Birnbaumer, Takuro Numaga-Tomita, Tatsuya Ishikawa, Motohiro Nishida, and Takashi Toyama

Subjects
0301 basic medicine, Cardiac fibrosis, TRPC6, purl.org/becyt/ford/1 [https], Mice, CORAZON, TRPC3, FIBROSIS, Myocytes, Cardiac, Mice, Knockout, Multidisciplinary, NADPH oxidase, biology, Lipid peroxide, 3. Good health, NADPH Oxidase 2, cardiovascular system, Medicine, CIENCIAS NATURALES Y EXACTAS, medicine.drug, Protein Binding, Signal Transduction, HIPERGLUCEMIA, medicine.medical_specialty, Lipid Peroxides, Science, Otras Ciencias Biológicas, Primary Cell Culture, Streptozocin, Article, Proinflammatory cytokine, Diabetes Mellitus, Experimental, Ciencias Biológicas, 03 medical and health sciences, Internal medicine, medicine, TRPC6 Cation Channel, Animals, purl.org/becyt/ford/1.6 [https], TRPC Cation Channels, Heart Failure, 030102 biochemistry & molecular biology, Myocardium, TRPC3-Nox2, medicine.disease, Streptozotocin, Myocardial Contraction, Rats, 030104 developmental biology, Endocrinology, Gene Expression Regulation, TRPC6 counteracts TRPC3-Nox2 protein complex leading to attenuation of hyperglycemia-induced heart failure in mice, 13. Climate action, Heart failure, Hyperglycemia, biology.protein, hyperglycemia, Reactive Oxygen Species
Abstract

Fil: Oda, Sayaka. National Institute for Physiological Sciences. Division of Cardiocirculatory Signaling; Japón Fil: Oda, Sayaka. The Graduate University for Advanced Studies. Department of Physiological Sciences; Japón Fil: Numaga-Tomita, Takuro. National Institute for Physiological Sciences. Division of Cardiocirculatory Signaling; Japón Fil: Numaga-Tomita, Takuro. The Graduate University for Advanced Studies. Department of Physiological Sciences; Japón Fil: Kitajima, Naoyuki. National Institute for Physiological Sciences. Division of Cardiocirculatory Signaling; Japón Fil: Kitajima, Naoyuki. Kyushu University. Graduate School of Pharmaceutical Sciences. Department of Translational Pharmaceutical Sciences; Japón Fil: Toyama, Takashi. National Institute for Physiological Sciences. Division of Cardiocirculatory Signaling; Japón Fil: Toyama, Takashi. Kyushu University. Graduate School of Pharmaceutical Sciences. Department of Translational Pharmaceutical Sciences; Japón Fil: Toyama, Takashi. University of Tsukuba. Faculty of Medicine and Graduate School of Comprehensive Human Sciences. Environmental Biology Laboratory; Japón Fil: Harada, Eri. Ajinomoto Company Incorporated; Japón Fil: Harada, Eri. EA Pharma Company; Japón Fil: Shimauchi, Tsukasa. National Institute for Physiological Sciences. Division of Cardiocirculatory Signaling; Japón Fil: Shimauchi, Tsukasa. Kyushu University. Graduate School of Pharmaceutical Sciences. Department of Translational Pharmaceutical Sciences; Japón Fil: Nishimura, Akiyuki. National Institute for Physiological Sciences. Division of Cardiocirculatory Signaling; Japón Fil: Nishimura, Akiyuki. The Graduate University for Advanced Studies. Department of Physiological Sciences; Japón Fil: Ishikawa, Tatsuya. National Institute for Physiological Sciences. Division of Cardiocirculatory Signaling; Japón Fil: Ishikawa, Tatsuya. Kyushu University. Graduate School of Pharmaceutical Sciences. Department of Translational Pharmaceutical Sciences; Japón Fil: Ishikawa, Tatsuya. EA Pharma Company; Japón Fil: Kumagai, Yoshito. University of Tsukuba. Faculty of Medicine and Graduate School of Comprehensive Human Sciences. Environmental Biology Laboratory; Japón Fil: Birnbaumer, Lutz. National Institute of Environmental Health Sciences. Laboratory of Neuroscience; Estados Unidos Fil: Birnbaumer, Lutz. Pontificia Universidad Católica Argentina. Facultad de Ciencias Médicas. Instituto de Investigaciones Biomédicas; Argentina Fil: Nishida, Motohiro. National Institute for Physiological Sciences. Division of Cardiocirculatory Signaling; Japón Fil: Nishida, Motohiro. The Graduate University for Advanced Studies. Department of Physiological Sciences; Japón Fil: Kyushu University. Graduate School of Pharmaceutical Sciences. Department of Translational Pharmaceutical Sciences; Japón Abstract: Excess production of reactive oxygen species (ROS) caused by hyperglycemia is a major risk factor for heart failure. We previously reported that transient receptor potential canonical 3 (TRPC3) channel mediates pressure overload-induced maladaptive cardiac fibrosis by forming stably functional complex with NADPH oxidase 2 (Nox2). Although TRPC3 has been long suggested to form hetero-multimer channels with TRPC6 and function as diacylglycerol-activated cation channels coordinately, the role of TRPC6 in heart is still obscure. We here demonstrated that deletion of TRPC6 had no impact on pressure overload-induced heart failure despite inhibiting interstitial fibrosis in mice. TRPC6-deficient mouse hearts 1 week after transverse aortic constriction showed comparable increases in fibrotic gene expressions and ROS production but promoted inductions of inflammatory cytokines, compared to wild type hearts. Treatment of TRPC6-deficient mice with streptozotocin caused severe reduction of cardiac contractility with enhancing urinary and cardiac lipid peroxide levels, compared to wild type and TRPC3-deficient mice. Knockdown of TRPC6, but not TRPC3, enhanced basal expression levels of cytokines in rat cardiomyocytes. TRPC6 could interact with Nox2, but the abundance of TRPC6 was inversely correlated with that of Nox2. These results strongly suggest that Nox2 destabilization through disrupting TRPC3-Nox2 complex underlies attenuation of hyperglycemia-induced heart failure by TRPC6.

Published
2017

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