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Cardiac troponin T N-domain variant destabilizes the actin interface resulting in disturbed myofilament function.
Landim-Vieira, Maicon; Ma, Weikang; Song, Taejeong; Rastegarpouyani, Hosna; Gong, Henry; Coscarella, Isabella Leite; Bogaards, Sylvia J P; Conijn, Stefan P; Ottenheijm, Coen A C; Hwang, Hyun S; Papadaki, Maria; Knollmann, Bjorn C; Sadayappan, Sakthivel; Irving, Thomas C; Galkin, Vitold E; Chase, P Bryant; Pinto, Jose Renato.
Afiliação
  • Landim-Vieira M; Department of Biomedical Sciences, Florida State University College of Medicine, Tallahassee, FL 32306.
  • Ma W; Department of Biology, Illinois Institute of Technology, Chicago, IL 60616.
  • Song T; Division of Cardiovascular Health and Disease, Department of Internal Medicine, University of Cincinnati College of Medicine, Cincinnati, OH 45267.
  • Rastegarpouyani H; Department of Biological Science, Florida State University, Tallahassee, FL 32306.
  • Gong H; Institude of Molecular Biophysics, Florida State University, Tallahassee, FL 32306.
  • Coscarella IL; Department of Biology, Illinois Institute of Technology, Chicago, IL 60616.
  • Bogaards SJP; Department of Biomedical Sciences, Florida State University College of Medicine, Tallahassee, FL 32306.
  • Conijn SP; Department of Physiology, Amsterdam University Medical Center, Amsterdam, De Boelelaan 1108, 1081 HZ Amsterdam, The Netherlands.
  • Ottenheijm CAC; Department of Physiology, Amsterdam University Medical Center, Amsterdam, De Boelelaan 1108, 1081 HZ Amsterdam, The Netherlands.
  • Hwang HS; Department of Physiology, Amsterdam University Medical Center, Amsterdam, De Boelelaan 1108, 1081 HZ Amsterdam, The Netherlands.
  • Papadaki M; Department of Nutrition and Integrative Physiology, Florida State University, Tallahassee, FL 32306.
  • Knollmann BC; Department of Cell and Molecular Physiology, Loyola University Chicago Stritch School of Medicine, Chicago, IL 60153.
  • Sadayappan S; Department of Medicine, Vanderbilt University Medical Center, Nashville, TN 37232.
  • Irving TC; Division of Cardiovascular Health and Disease, Department of Internal Medicine, University of Cincinnati College of Medicine, Cincinnati, OH 45267.
  • Galkin VE; Department of Biology, Illinois Institute of Technology, Chicago, IL 60616.
  • Chase PB; Department of Physiological Sciences, Eastern Virginia Medical School, Norfolk, VA 23507.
  • Pinto JR; Department of Biological Science, Florida State University, Tallahassee, FL 32306.
Proc Natl Acad Sci U S A ; 120(23): e2221244120, 2023 06 06.
Article em En | MEDLINE | ID: mdl-37252999
Missense variant Ile79Asn in human cardiac troponin T (cTnT-I79N) has been associated with hypertrophic cardiomyopathy and sudden cardiac arrest in juveniles. cTnT-I79N is located in the cTnT N-terminal (TnT1) loop region and is known for its pathological and prognostic relevance. A recent structural study revealed that I79 is part of a hydrophobic interface between the TnT1 loop and actin, which stabilizes the relaxed (OFF) state of the cardiac thin filament. Given the importance of understanding the role of TnT1 loop region in Ca2+ regulation of the cardiac thin filament along with the underlying mechanisms of cTnT-I79N-linked pathogenesis, we investigated the effects of cTnT-I79N on cardiac myofilament function. Transgenic I79N (Tg-I79N) muscle bundles displayed increased myofilament Ca2+ sensitivity, smaller myofilament lattice spacing, and slower crossbridge kinetics. These findings can be attributed to destabilization of the cardiac thin filament's relaxed state resulting in an increased number of crossbridges during Ca2+ activation. Additionally, in the low Ca2+-relaxed state (pCa8), we showed that more myosin heads are in the disordered-relaxed state (DRX) that are more likely to interact with actin in cTnT-I79N muscle bundles. Dysregulation of the myosin super-relaxed state (SRX) and the SRX/DRX equilibrium in cTnT-I79N muscle bundles likely result in increased mobility of myosin heads at pCa8, enhanced actomyosin interactions as evidenced by increased active force at low Ca2+, and increased sinusoidal stiffness. These findings point to a mechanism whereby cTnT-I79N weakens the interaction of the TnT1 loop with the actin filament, which in turn destabilizes the relaxed state of the cardiac thin filament.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Troponina T / Miofibrilas Tipo de estudo: Prognostic_studies Limite: Humans Idioma: En Revista: Proc Natl Acad Sci U S A Ano de publicação: 2023 Tipo de documento: Article País de publicação: Estados Unidos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Troponina T / Miofibrilas Tipo de estudo: Prognostic_studies Limite: Humans Idioma: En Revista: Proc Natl Acad Sci U S A Ano de publicação: 2023 Tipo de documento: Article País de publicação: Estados Unidos