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. 2016 Feb 17;24(4):259–267. doi: 10.1007/s12471-016-0812-z

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© The Author(s) 2016

Open Access This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.

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Fig. 4 — The effects of oxidative stress on titin and cardiomyocyte-based stiffness. a Oxidative stress induces post-translational modifications of titin, such as oxidation of cysteines in N2B-unique sequence of titin (N2-Bus) causing disulphide bonding (far left), S-glutathionylation of cysteines in unfolded Ig domains inhibiting domain refolding (left-middle), and reduced cGMP-dependent protein kinase-G (PKG)–dependent N2-Bus phosphorylation, because of oxidation of the haeme moiety in soluble guanylyl cyclase (sGC) and the ensuing blockade of cGMP production (right). Graphs in B to D show oxidative stress–related effects on titin-based passive tension caused by S–S bonding within N2-Bus (b), S-glutathionylation of unfolded titin-Ig domains (c), or depressed cGMP-PKG pathway activation (d). 5′GMP guanosine-5′-monophosphate, cGMP cyclic guanosine monophosphate, G glutathione, GSSG, glutathione-disulphide, NO, nitric oxide, P, titin phosphorylation, PDE5, phosphodiesterase-5, pGC, particulate guanylyl cyclase, PKG, cGMP-dependent protein kinase-G, and sGC, soluble guanylyl cyclase. (Used with permission from [62])