Abstract We evaluated the changes in sarcoplasmic reticulum (SR) function and the parallel hemodynamic and morphological modifications in a heart subjected to volume overload. We also determined the levels of acylphosphatase, a cytosolic enzyme, that could play a regulatory effect on SR Ca(2+) pump by hydrolyzing the phosphorylated intermediate of this transport system. For this, swine hearts were subjected to volume overload by aorta-cava shunt for 1, 2, or 3 months. Changes in heart contractility reflected modifications of SR function, whose reduction after 1 month of overload was followed by a gradual recovery. A decrease in SERCA2a protein and mRNA content was shown from 1 month and remained for the following 2 months. Phospholamban content and its phosphorylation status were not modified. Acylphosphatase was unchanged at 1 month, but at 2 months this enzyme exhibited an increased activity, protein and mRNA expression. Morphological alterations consisting of the cytoskeletal architectures, intermyofibrillar oedema, swollen mitochondria and abnormality of the membrane system (T-tubule and SR cisternae) were particularly evident after 1 month but almost disappeared after 3 months. These results suggest that our overloaded hearts underwent a substantial recovery of their structural and biochemical properties at 3 months after surgery. A possible involvement of acylphosphatase in the modification of SR function is discussed.

Biochemical changes and their relationship with morphological and functional finding in pig heart subjected to lasting volume-overload: a possible role of Acylphosphatase in the regulation of sarcoplasmic reticulum calcium pump / C. Nediani; L. Formigli; A.M. Perna; A. Pacini; V. Ponziani; P.A. Modesti; L. Ibba; S. Zecchi; C. Fiorillo; C. Cecchi; P. Liguori; G. Fratini; S. Vanni; P. Nassi.. - In: BASIC RESEARCH IN CARDIOLOGY. - ISSN 0300-8428. - STAMPA. - 97:(2002), pp. 469-478. [10.1007/s00395-002-0367-6]

Biochemical changes and their relationship with morphological and functional finding in pig heart subjected to lasting volume-overload: a possible role of Acylphosphatase in the regulation of sarcoplasmic reticulum calcium pump.

NEDIANI, CHIARA;FORMIGLI, LUCIA;PACINI, ALESSANDRA;MODESTI, PIETRO AMEDEO;IBBA, LIDIA;ZECCHI, SANDRA;FIORILLO, CLAUDIA;CECCHI, CRISTINA;S. Vanni;NASSI, PAOLO ANTONIO
2002

Abstract

Abstract We evaluated the changes in sarcoplasmic reticulum (SR) function and the parallel hemodynamic and morphological modifications in a heart subjected to volume overload. We also determined the levels of acylphosphatase, a cytosolic enzyme, that could play a regulatory effect on SR Ca(2+) pump by hydrolyzing the phosphorylated intermediate of this transport system. For this, swine hearts were subjected to volume overload by aorta-cava shunt for 1, 2, or 3 months. Changes in heart contractility reflected modifications of SR function, whose reduction after 1 month of overload was followed by a gradual recovery. A decrease in SERCA2a protein and mRNA content was shown from 1 month and remained for the following 2 months. Phospholamban content and its phosphorylation status were not modified. Acylphosphatase was unchanged at 1 month, but at 2 months this enzyme exhibited an increased activity, protein and mRNA expression. Morphological alterations consisting of the cytoskeletal architectures, intermyofibrillar oedema, swollen mitochondria and abnormality of the membrane system (T-tubule and SR cisternae) were particularly evident after 1 month but almost disappeared after 3 months. These results suggest that our overloaded hearts underwent a substantial recovery of their structural and biochemical properties at 3 months after surgery. A possible involvement of acylphosphatase in the modification of SR function is discussed.
2002
97
469
478
C. Nediani; L. Formigli; A.M. Perna; A. Pacini; V. Ponziani; P.A. Modesti; L. Ibba; S. Zecchi; C. Fiorillo; C. Cecchi; P. Liguori; G. Fratini; S. Vann...espandi
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Utilizza questo identificatore per citare o creare un link a questa risorsa: https://hdl.handle.net/2158/312446
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