Titin isoforms are increasingly protected against oxidative modifications in developing rat cardiomyocytes

Beáta Bódi, Enikő Pásztorné Tóth, Laszlo Nagy, Attila Tóth, Lilla Mártha, Árpád Kovács, György Balla, Tamás Kovács, Zoltán Papp

Research output: Contribution to journalArticle

Abstract

During the perinatal adaptation process N2BA titin isoforms are switched for N2B titin isoforms leading to an increase in cardiomyocyte passive tension (Fpassive). Here we attempted to reveal how titin isoform composition and oxidative insults (i.e. sulfhydryl (SH)-group oxidation or carbonylation) influence Fpassive of left ventricular (LV) cardiomyocytes during rat heart development. Moreover, we also examined a hypothetical protective role for titin associated small heat shock proteins (sHSPs), Hsp27 and αB-crystallin in the above processes. Single, permeabilized LV cardiomyocytes of the rat (at various ages following birth) were exposed either to 2,2′-dithiodipyridine (DTDP) to provoke SH-oxidation or Fenton reaction reagents (iron(II), hydrogen peroxide (H2O2), ascorbic acid) to induce protein carbonylation of cardiomyocytes in vitro. Thereafter, cardiomyocyte force measurements for Fpassive determinations and Western immunoblot assays were carried out for the semiquantitative determination of oxidized SH-groups or carbonyl-groups of titin isoforms and to monitor sHSPs’ expressions. DTDP or Fenton reagents increased Fpassive in 0- and 7-day-old rats to relatively higher extents than in 21-day-old and adult animals. The degrees of SH-group oxidation or carbonylation declined with cardiomyocyte age to similar extents for both titin isoforms. Moreover, the above characteristics were mirrored by increasing levels of HSP27 and αB-crystallin expressions during cardiomyocyte development. Our data implicate a gradual build-up of a protective mechanism against titin oxidation through the upregulation of HSP27 and αB-crystallin expressions during postnatal cardiomyocyte development.

Original languageEnglish (US)
Pages (from-to)224-235
Number of pages12
JournalFree Radical Biology and Medicine
Volume113
DOIs
StatePublished - Dec 1 2017
Externally publishedYes

Fingerprint

Connectin
Cardiac Myocytes
Rats
Protein Isoforms
Carbonylation
Crystallins
Small Heat-Shock Proteins
Oxidation
Protein Carbonylation
Force measurement
Hydrogen Peroxide
Ascorbic Acid
Assays
Animals
Iron
Up-Regulation
Western Blotting
Parturition
Chemical analysis

Keywords

  • Carbonylation
  • Heat shock protein
  • Isolated cardiomyocytes
  • Modifications
  • Oxidation
  • Passive tension
  • Titin isoform

ASJC Scopus subject areas

  • Biochemistry
  • Physiology (medical)

Cite this

Titin isoforms are increasingly protected against oxidative modifications in developing rat cardiomyocytes. / Bódi, Beáta; Tóth, Enikő Pásztorné; Nagy, Laszlo; Tóth, Attila; Mártha, Lilla; Kovács, Árpád; Balla, György; Kovács, Tamás; Papp, Zoltán.

In: Free Radical Biology and Medicine, Vol. 113, 01.12.2017, p. 224-235.

Research output: Contribution to journalArticle

Bódi, Beáta ; Tóth, Enikő Pásztorné ; Nagy, Laszlo ; Tóth, Attila ; Mártha, Lilla ; Kovács, Árpád ; Balla, György ; Kovács, Tamás ; Papp, Zoltán. / Titin isoforms are increasingly protected against oxidative modifications in developing rat cardiomyocytes. In: Free Radical Biology and Medicine. 2017 ; Vol. 113. pp. 224-235.
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AU - Mártha, Lilla

AU - Kovács, Árpád

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AU - Papp, Zoltán

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