Skeletal troponin I

Li, Z., Gergely, J., and Tao, T. (2001). Proximity relationships between residue 117 of rabbit skeletal troponin-I and residues in troponin-C and actin. Biophys. J. 81, 321-333. 

Talbot, J. A., and Hodges, R. S. (1981). Synthetic studies on the inhibitory region of rabbit skeletal troponin I. Relationship of amino acid sequence to biological activity. / Biol. Chem. 256, 2798-2802. 

Fig. 4. Schematic representation of the amino acid sequence of rabbit skeletal troponin I. The primary sequence of troponin I (residues 1-178) is shown as an open bar. The posidons of main residues as well as approximate interacting regions are indicated at the upper part of the sequence. Tick marks below indicate the position of lysine residues reactive to acetylation tick marks with open circles indicate residues whose reactivity is affected by troponin T (residues 40, 65, 70, 78, 90) (Hitchcock-de Gregori, 1982). The position of fragments CN5, CF2, and CN4 is shown under the sequence (Syska etai, 1976).

The sequences of the main portions of rabbit cardiac and skeletal troponin I are nearly identical, but cardiac troponin I has about 20 additional residues at the N-terminal end (Wilkinson and Grand, 1978). It was found that Ser-20 of rabbit cardiac troponin I is very susceptible... 

Troponin components of bovine cardiac muscle were separated by essentially the same procedure as for skeletal troponin components (Tsukui and Ebashi, 1973). Studies on the Ca + sensitivity of superprecipitation with various combinations of troponin components from rabbit skeletal and bovine cardiac muscles showed that most hybrid troponins gave the lower Ca sensitivity of superprecipitation (Ebashi, 1974a,b) (Table III). The lowest value was obtained with the combination of skeletal troponin C-T and cardiac troponin I. However, when cardiac troponin T was combined with skeletal troponin I—C, the calcium sensitivity was exceptionally high and exceeded those obtained by the native... 

The contraction of ascidian smooth muscle was found to be regulated through the troponin-tropomyosin system. But the action of troponin components was different from that of troponin of vertebrate striated muscles (Endo and Obinata, 1981). In this system, the inhibitory action of troponin I (MW 24,000) is less remarkable compared with vertebrate skeletal troponin I, and troponin C (MW 18,000) does not neutralize the inhibition by troponin I. But upon further addition of troponin T (MW 33,000) in the concomitant presence of all three components and tropomyosin, the contractile interaction of myosin and actin is activated. In this case, the action of troponin T has some similarity with that of the above-mentioned cardiac troponin T hybridized with skeletal troponin C-I. Since actomyosin, without these regulatory proteins, is inhibited regardless of Ca concentration, Ca " and troponin-tropomyosin are activators for contraction of actomyosin in ascidian smooth muscle. In this respect, the type of Ca + regulation of ascidian smooth muscle is the same as that for vertebrate smooth muscles which do not contain troponin (Ebashi, 1980). 

Kiely, P. D. W, F. E. Bruckner, J. A. Nisbet, and A. Daghir. 2000. Serum skeletal troponin I in inflammatory muscle disease Relation to creatine kinase, CKMB and cardiac troponin I. Annals of Rheumatic Diseases 59 750-752. 

Nikovits, W., Kuncio, G. Ordahl, C.P. (1986). The chicken fast skeletal troponin I gerte exon organization and sequence. Nucl Acids Res., 14, 3377-90. 

Skeletal troponin I Serum or plasma Immunoassay Sun et al. (2010), Vassallo et al. 

Foster, G. E., J. Nakano, A. W. Shed, J. A. Simpson, J. D. Road, and W. D. Reid (2012). Serum skeletal troponin I following inspiratory threshold loading in healthy young and middle-aged men. EurJ Appl Physiol 112 3547-3558. 

Simpson, J. A., R. Labugger, G. G. Hesketh, C. D Arsigny, D. O Donnell, N. Matsumoto, C. P. Collier, S. Iscoe, and J. E. Van Eyk (2002). Differential detection of skeletal troponin I isoforms in serum of a patient with rhabdomyolysis markers of muscle injury Clin Chem 48(7) 1112-1114. 

Soiichter, S., J. Mair, A. Roller, W. Gebert, D. Rama, C. Calzolari, E. Artner-Dworzak, and B. Puschendorf (1997). Skeletal troponin I as a marker of exercise-induced muscle damage. J Appl Physiol 83(4) 1076-1082. 

Takahashi, M., L. Lee, Q. Shi, Y. Gawad, and G. Jackowski (1996). Use of enzyme immunoassay for measurement of skeletal troponin-I utilizing isoform-specific monoclonal antibodies. Clin Biochem 29(4) 301-308. 

FIGURE 41.1 Rat skeletal troponin I (MSD ) assay linearity of dilution. 

---