FIGURE 1.

Representative 15% SDS-PAGE of cross-linked troponin subunits. BP-MAL, benzenophenone-4-malemide cross-linker; min, minutes exposed to 365 nm UV light; T, troponin T; I, troponin I; C, troponin C; I-T, troponin I cross-linked to troponin T; I-C₁*, slower migrating troponin I cross-linked to troponin C; I-C₂*, faster migrating troponin I cross-linked to troponin C; I-I* intramolecular cross-link of troponin I; I-T*, troponin I cross-linked to troponin T; I-C, troponin I and troponin C complex; T-I-C, whole troponin complex; + Ca, cross-linked in the presence of Ca²⁺; -Ca, cross-linked in the absence of Ca²⁺. A, the S5C mutant troponin I was used on all lanes of the gel. B, the I19C mutant troponin I was used in all lanes of the gel. Note: the protein loads were equalized on each gel, but gels were not equalized to each other.

Sites of Intra- and Intermolecular Cross-linking of the N-terminal Extension of Troponin I in Human Cardiac Whole Troponin Complex

J Biol Chem. 2009 May 22;284(21):14258-14266.
FIGURE 4.

MALDI-TOF spectra of cross-linked peptide complex purified as in Fig. 3 (B–E). BP-MAL, cross-linker mass 277.1 with hydrolyzed maleimide ring 18 = 295.1 (30). Complexes are broken up into major fragments as indicated in the spectrum. The unidentified peaks are non-cross-linked peptides. A, intramolecular cross-link of troponin I at position 5 to troponin I amino acids 149–162. B, intermolecular cross-link of troponin I at position 5 to troponin C amino acids 47–59. C, intermolecular cross-link of troponin I at position 5 to troponin C amino acids 77–83. D, intramolecular cross-link of troponin I at position 19 to troponin I amino acids 149–162. E, intermolecular cross-link of troponin I at position 19 to troponin C amino acids 47–59. F, intermolecular cross-link of troponin I at position 19 to troponin C amino acids 77–83.

Sites of Intra- and Intermolecular Cross-linking of the N-terminal Extension of Troponin I in Human Cardiac Whole Troponin Complex

J Biol Chem. 2009 May 22;284(21):14258-14266.
FIGURE 3.

HPLC of peptides and whole proteins. The bar indicates either cross-linked proteins or peptides depending on the run. Signal evaluated at 280 nm for A and 260 nm for B–E. Fractions were collected manually, and each fraction from B–E was analyzed by MALDI-TOF to determine which fractions were cross-linked. A, representative separation of cross-linked and non-cross-linked whole troponin subunits. The dark line represents whole troponin complex cross-linked for 30 min and separated by C4 (4.6 × 150 mm) reversed-phase HPLC, and the light line is non-cross-linked negative control. I, troponin I; T, troponin T; C, troponin C; I+I, intramolecular cross-link of troponin I; I+T, intermolecular cross-link of troponin I and T; I+C, intermolecular cross-link of troponin I and C. B, the dark line intramolecular cross-link of the troponin I mutant S5C digested with Arg-C and separated by C18 (0.3 × 150 mm) reversed-phase capillary HPLC, and the light line is non-cross-linked negative control. C, the dark line intermolecular cross-link of the troponin I mutant S5C to troponin C digested sequentially with trypsin and Glu-C and separated by C18 (0.3 × 150 mm) reversed-phase capillary HPLC, and the light line is the enzymes-only control. D, the dark line intramolecular cross-link of the troponin I mutant I19C digested with Arg-C and separated by C18 (0.3 × 150 mm) reversed-phase capillary HPLC, and the light line is non-cross-linked negative control. E, dark line intermolecular cross-links of the troponin I mutant I19C to troponin C digested sequentially with trypsin and Glu-C and separated by C18 (0.3 × 150 mm) reversed-phase capillary HPLC, and the light line is the enzymes-only control.

Sites of Intra- and Intermolecular Cross-linking of the N-terminal Extension of Troponin I in Human Cardiac Whole Troponin Complex

J Biol Chem. 2009 May 22;284(21):14258-14266.
Figure 1

Age-dependent stoichiometric replacement in cardiac troponin I A164H transgenic mice. (A) Sequence alignment showing location of the single histidine substitution originally studied in the slow skeletal isoform of troponin I and subsequently introduced into cardiac troponin I (cTnI A164HFLAG). Expression cassette of cDNA-encoding cardiac troponin I A164H with an SV40 polyadenylation (pA) signal was driven by the 5.5 kb Myh6 promoter. A C-terminal flag epitope was used to aid detection of cardiac troponin I A164H. (B) Immunoblot and bar graph showing expression of native cardiac troponin I (filled square) in non-transgenic mice as well as stoichiometric incorporation of cardiac troponin I A164HFLAG (open square) relative to endogenous cardiac troponin I (filled square) in transgenic mice at 6 months (n = 12) and 2 years (n = 6). Values are expressed as mean ± SEM. *P < 0.05 for 6 month vs. 2 year replacement.

Single histidine-substituted cardiac troponin I confers protection from age-related systolic and diastolic dysfunction

Cardiovasc Res. 2008 November 1;80(2):209-218.

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