ALFA ACTININA PDF

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Potencial Conflito de Interesses. Fontes de Financiamento. Cardiac titin: structure, functions and role in disease. Clin Chim Acta. Granzier HL, Labeit S. The giant protein titin: a major player in myocardial mechanics, signaling, and disease.

Circ Res. Tskhovrebova L, Trinick J. Properties of titin immunoglobulin and fibronectin-3 domains. J Biol Chem. Titin: properties and family relationships.

Nat Rev Mol Cell Biol. Maruyama K. Faseb J. Granzier H, Labeit S. Cardiac titin: an adjustable multi-functional spring. J Physiol. Series of exon-skipping events in the elastic spring region of titin as the structural basis for myofibrillar elastic diversity. I-band titin in cardiac muscle is a three-element molecular spring and is critical for maintaining thin filament structure.

J Cell Biol. Titin develops restoring force in rat cardiac myocytes. Altered titin expression, myocardial stiffness, and left ventricular function in patients with dilated cardiomyopathy. Differential expression of cardiac titin isoforms and modulation of cellular stiffness. Leite-Moreira AF. Current perspectives in diastolic dysfunction and diastolic heart failure. Titin: an endosarcomeric protein that modulates myocardial stiffness in DCM. J Card Fail. Passive tension in cardiac muscle: contribution of collagen, titin, microtubules, and intermediate filaments.

Biophys J. Myocardial structure and function differ in systolic and diastolic heart failure. Titin determines the Frank-Starling relation in early diastole. J Gen Physiol.

Fukuda N, Granzier HL. J Muscle Res Motil. Katz AM. Ernest Henry Starling, his predecessors, and the "Law of the Heart". Influence of calcium concentrations on these relations. Titin-based modulation of calcium sensitivity of active tension in mouse skinned cardiac myocytes. Titin isoform variance and length dependence of activation in skinned bovine cardiac muscle.

Length dependence of tension generation in rat skinned cardiac muscle: role of titin in the Frank-Starling mechanism of the heart. The sensitive giant: the role of titin-based stretch sensing complexes in the heart. Trends Cell Biol. Linke WA. Sense and stretchability: the role of titin and titin-associated proteins in myocardial stress-sensing and mechanical dysfunction. Cardiovasc Res. Muscle assembly: a titanic achievement?

Curr Opin Cell Biol. Disuse-induced preferential loss of the giant protein titin depresses muscle performance via abnormal sarcomeric organization. The giant muscle protein titin is an adjustable molecular spring. Exerc Sport Sci Rev. Protein kinase A phosphorylates titin's cardiac-specific N2B domain and reduces passive tension in rat cardiac myocytes. Kruger M, Linke WA. Protein kinase-A phosphorylates titin in human heart muscle and reduces myofibrillar passive tension.

J Muscle Res Cell Motil. Cardiomyocyte stiffness in diastolic heart failure. Phosphorylation of titin modulates passive stiffness of cardiac muscle in a titin isoform-dependent manner.

Modulation of cardiac function: titin springs into action. J Am Coll Cardiol. A : A. Bers DM. Cardiac excitation-contraction coupling. Protein kinase G modulates human myocardial passive stiffness by phosphorylation of the titin springs.

Hypophosphorylation of the stiff N2B titin isoform raises cardiomyocyte resting tension in failing human myocardium. Prog Biophys Mol Biol. Titin isoform expression in aortic stenosis. Clin Sci Lond. Transcriptional and posttranslational modifications of titin: implications for diastole. Titin, myosin light chains and C-protein in the developing and failing human heart.

J Mol Cell Cardiol. Passive stiffness changes caused by upregulation of compliant titin isoforms in human dilated cardiomyopathy hearts. Titin isoform switch in ischemic human heart disease. Titin isoform expression in normal and hypertensive myocardium. All the contents of this journal, except where otherwise noted, is licensed under a Creative Commons Attribution License. Services on Demand Journal. How to cite this article.

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2006, Número S4

ISSN SUMMARY: The cytoskeleton of muscle cell is a complex network of proteins which expression pattern is related with the differentiation process. The a -actinin, a protein which plays an important role in the muscular contraction, is essential to the sarcomeres conformation, serving as an anchoring point or center of organization for the preformation of actin filaments. The modulation of the a -actinin expression during the muscular cell maturation, has an important morphofuntional implications to the myocardiocytes. Immunofluorescence studies on cryotome sectins of chick embryo hearts and myocardiocyte cultures showed that a-actinin expression was weak in early stages Hamburger Hamilton stage 18 , staining the cellular membrane of myocardiocytes.

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α-actinina

Yang F, Condeelis J: Actin and associated proteins. Guidebook to the cytoskeletal and motor proteins. Kreis T, Vale R, Ed. A Sambrook and tooze publication at oxford university press, , p. Ayscough KR: In vivo functions of actin-binding-proteins.. Curr Opin Cell Biol ;

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