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Modulation of titin-based stiffness by disulfide bonding in the cardiac titin N2-B unique sequence.

Abstract：

:The giant protein titin is responsible for the elasticity of nonactivated muscle sarcomeres. Titin-based passive stiffness in myocardium is modulated by titin-isoform switching and protein-kinase (PK)A- or PKG-dependent titin phosphorylation. Additional modulatory effects on titin stiffness may arise from disulfide bonding under oxidant stress, as many immunoglobulin-like (Ig-)domains in titin's spring region have a potential for S-S formation. Using single-molecule atomic force microscopy (AFM) force-extension measurements on recombinant Ig-domain polyprotein constructs, we show that titin Ig-modules contain no stabilizing disulfide bridge, contrary to previous belief. However, we demonstrate that the human N2-B-unique sequence (N2-B(us)), a cardiac-specific, physiologically extensible titin segment comprising 572 amino-acid residues, contains up to three disulfide bridges under oxidizing conditions. AFM force spectroscopy on recombinant N2-B(us) molecules demonstrated a much shorter contour length in the absence of a reducing agent than in its presence, consistent with intramolecular S-S bonding. In stretch experiments on isolated human heart myofibrils, the reducing agent thioredoxin lowered titin-based stiffness to a degree that could be explained (using entropic elasticity theory) by altered extensibility solely of the N2-B(us). We conclude that increased oxidant stress can elevate titin-based stiffness of cardiomyocytes, which may contribute to the global myocardial stiffening frequently seen in the aging or failing heart.

journal_name

Biophys J

journal_title

Biophysical journal

authors

Grützner A,Garcia-Manyes S,Kötter S,Badilla CL,Fernandez JM,Linke WA

doi

10.1016/j.bpj.2009.05.037

subject

Has Abstract

pub_date

2009-08-05 00:00:00

pages

825-34

issue

3

eissn

0006-3495

issn

1542-0086

pii

S0006-3495(09)01046-7

journal_volume

97

pub_type

杂志文章

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