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Gene Review

TNNT1  -  troponin T type 1 (skeletal, slow)

Homo sapiens

Synonyms: ANM, FLJ98147, MGC104241, NEM5, STNT, ...
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Disease relevance of TNNT1


High impact information on TNNT1

  • Here, we show that AAVS1 is closely linked to the slow skeletal troponin T gene, TNNT1, which has been mapped previously to 19q13 [6].
  • The emission of ANM-modified alpha 1-PI is increased in intensity and blue shifted from the maximum in ANM-modified cysteine, consistent with a predominantly nonpolar environment [7].
  • We have modified the single cysteine residue of alpha 1-protease inhibitor (alpha 1-PI) with HgCl2, methylmethane thiosulfonate, oxidized glutathione (GSSG), and N-(1-anilinonaphthyl-4)maleimide (ANM) [7].
  • The amino acid sequence deduced from RCT10 cDNA exhibits 87%, 85%, and 72% homology with bovine, rabbit, and chicken cardiac TnTs, respectively, but less homology (57-59%) with the known skeletal TnTs from human, rat, rabbit, and chicken [8].
  • As with other monofunctional maleimides, incubation of thylakoids with ANM in the light, but not in the dark, causes energy transfer inhibition of photophosphorylation [9].

Chemical compound and disease context of TNNT1

  • Comparison of these results with the known, complete primary structure of tryptophanase from the K-12 strain of E. coli allowed the assignment of position 298 to the cysteine residue, which is more selectively modified by ANM under the conditions chosen and is involved in the maintenance of the catalytic activity [10].
  • TNT, creatine kinase (CK) and MB isoenzyme of creatine kinase (CK-MB) were monitored in 134 patients with angina pectoris [11].

Biological context of TNNT1


Anatomical context of TNNT1

  • A 200-bp sTnT amplicon specific to a human sTnT sequence was detected in all skeletal muscle specimens [4].
  • No evidence of sTnT mRNA was found in heart muscle [4].
  • Fluorescence of ANM bound at the dark-and light-accessible sites has been measured after isolation of CF1 from thylakoids [9].
  • The average number of glomerular macrophages per patient (ANM/P) was closely correlated with the degree of hematuria (P < 0.01) as well as with the degree of leukocyturia (P < 0.01) in the absence of any correlation with proteinuria, serum IgA levels or the interval between the detection of urine abnormalities and renal biopsy [15].
  • Sarcoplasmic reticulum membranes labeled with ANM at either SHN or SHD showed a characteristic fluorescence whose intensity reversibly changed in response to the removal and readdition of Ca2+ ions in the range of 10(-6) to 10(-7) M [16].

Associations of TNNT1 with chemical compounds

  • Fluorescence energy transfer from a tryptophan in a hydrophilic region of the epsilon subunit to ANM bound to the epsilon subunit but not to the gamma subunit has been observed [9].
  • A fluorescent maleimide derivative, N-(4-anilino-1-naphthyl) maleimide (ANM), a specific probe for thiol groups, reacted with human placental glutathione transferase (GST, EC, causing a complete inactivation of the enzyme in a few minutes [17].
  • Both these two truncated TnTs conferred a lower cooperativity and a higher Ca(2+) sensitivity on the Ca(2+)-activated force generation than did wild-type TnT, independent of the phosphorylation of TnI by cAMP-dependent protein kinase [18].
  • The local conformational changes in the tropomyosin molecule under various conditions were studied by means of fluorimetry using SH-directed fluorescent dyes, N-(1-anilinonaphthyl-4)maleimide (ANM) and N-(3-pyrene)maleimide (PRM) [19].

Other interactions of TNNT1


Analytical, diagnostic and therapeutic context of TNNT1

  • In adult sea bream sTnT expression was restricted to red muscle and, using northern blotting, a single low abundance transcript was identified for sTnT1sb (1260 nucleotides) and a single high abundance transcript was identified for sTnT2sb (1000 nucleotides) [23].
  • 2. Sequence analysis confirmed that MSL 366 is the cDNA for human slow skeletal muscle troponin T. A genomic clone has been isolated and linkage studies with DM are in progress [24].
  • Western blot analysis for the presence of the troponin-T (TNT) 30-kDa fragment, conducted only on samples from steers fed the 0% sunflower oil diet, demonstrated more proteolysis by d 3 PM in L than W or WxL [25].
  • Histological changes in the muscle were examined and biochemical changes in the muscle proteins were evaluated by SDS-PAGE and immunoblotting for troponin T (TNT) [26].
  • 1. Troponin T (TNT) expressed in various vertebrate skeletal and ascidian smooth muscles was examined by two-dimensional electrophoresis in combination with immunoblotting [27].


  1. A novel nemaline myopathy in the Amish caused by a mutation in troponin T1. Johnston, J.J., Kelley, R.I., Crawford, T.O., Morton, D.H., Agarwala, R., Koch, T., Schäffer, A.A., Francomano, C.A., Biesecker, L.G. Am. J. Hum. Genet. (2000) [Pubmed]
  2. Cellular fate of truncated slow skeletal muscle troponin T produced by Glu180 nonsense mutation in amish nemaline myopathy. Wang, X., Huang, Q.Q., Breckenridge, M.T., Chen, A., Crawford, T.O., Morton, D.H., Jin, J.P. J. Biol. Chem. (2005) [Pubmed]
  3. Polymerase chain reaction in the detection of mRNA transcripts from the slow skeletal troponin T (TNNT1) gene in myotonic dystrophy and normal muscle. Novelli, G., Gennarelli, M., Zelano, G., Sangiuolo, F., Lo Cicero, S., Samson, F., Dallapiccola, B. Cell Biochem. Funct. (1992) [Pubmed]
  4. RNA expression of cardiac troponin T isoforms in diseased human skeletal muscle. Ricchiuti, V., Apple, F.S. Clin. Chem. (1999) [Pubmed]
  5. Creatine kinase-mb fraction and cardiac troponin T to diagnose acute myocardial infarction after cardiopulmonary resuscitation. Müllner, M., Hirschl, M.M., Herkner, H., Sterz, F., Leitha, T., Exner, M., Binder, M., Laggner, A.N. J. Am. Coll. Cardiol. (1996) [Pubmed]
  6. Adeno-associated virus site-specifically integrates into a muscle-specific DNA region. Dutheil, N., Shi, F., Dupressoir, T., Linden, R.M. Proc. Natl. Acad. Sci. U.S.A. (2000) [Pubmed]
  7. Reversible inhibition of neutrophil elastase by thiol-modified alpha-1 protease inhibitor. Tyagi, S.C. J. Biol. Chem. (1991) [Pubmed]
  8. Isolation and characterization of cDNA clones encoding embryonic and adult isoforms of rat cardiac troponin T. Jin, J.P., Lin, J.J. J. Biol. Chem. (1989) [Pubmed]
  9. Selective modification of coupling factor 1 in spinach chloroplast thylakoids by a fluorescent maleimide. Nalin, C.M., Béliveau, R., McCarty, R.E. J. Biol. Chem. (1983) [Pubmed]
  10. Characterization of the reactivity of sulphydryl groups in tryptophanase by a dual-monitoring high-performance liquid chromatographic system with a site-directed fluorescent reagent. Honda, T., Cacace, M.G., Sada, A., Tokushige, M. J. Chromatogr. (1986) [Pubmed]
  11. Prognostic efficacy of troponin T measurement in angina pectoris. Yang, Z., Zhang, W., Liu, Y. Chin. Med. J. (1995) [Pubmed]
  12. Breakpoints of 19q13 translocations of benign thyroid tumors map within a 400 kilobase region. Belge, G., Garcia, E., Rippe, V., Fusco, A., Bartnitzke, S., Bullerdiek, J. Genes Chromosomes Cancer (1997) [Pubmed]
  13. Assignment of the slow troponin T (TNNT1) gene to chromosome 19 using polymerase chain reaction. Novelli, G., Gennarelli, M., Rocchi, M., Dallapiccola, B. Hum. Genet. (1992) [Pubmed]
  14. A new human slow skeletal troponin T (TnTs) mRNA isoform derived from alternative splicing of a single gene. Samson, F., Mesnard, L., Mihovilovic, M., Potter, T.G., Mercadier, J.J., Roses, A.D., Gilbert, J.R. Biochem. Biophys. Res. Commun. (1994) [Pubmed]
  15. Macrophages in childhood IgA nephropathy. Nagata, M., Akioka, Y., Tsunoda, Y., Komatsu, Y., Kawaguchi, H., Yamaguchi, Y., Ito, K. Kidney Int. (1995) [Pubmed]
  16. Studies on conformational transitions of Ca2+, Mg2+-adenosine triphosphatase of sarcoplasmic reticulum. I. Selective labeling of functionally distinct sulfhydryl groups with conformational probes and evidence for a Ca2+-dependent conformational change. Yasuoka-Yabe, K., Kawakita, M. J. Biochem. (1983) [Pubmed]
  17. Identification of a highly reactive sulphydryl group in human placental glutathione transferase by a site-directed fluorescent reagent. Lo Bello, M., Petruzzelli, R., De Stefano, E., Tenedini, C., Barra, D., Federici, G. FEBS Lett. (1990) [Pubmed]
  18. Functional changes in troponin T by a splice donor site mutation that causes hypertrophic cardiomyopathy. Nakaura, H., Morimoto, S., Yanaga, F., Nakata, M., Nishi, H., Imaizumi, T., Ohtsuki, I. Am. J. Physiol. (1999) [Pubmed]
  19. Studies on calcium ion-induced conformation changes in the actin-tropomyosin-troponin system by fluorimetry. III. Changes in the conformation of tropomyosin associated with functional states. Ohyashiki, T., Kanaoka, Y., Sekine, T. Biochim. Biophys. Acta (1976) [Pubmed]
  20. Isolation and cloning by a polymerase chain reaction of a genomic DNA fragment of the human slow skeletal troponin (TNNT1) gene. Novelli, G., Gennarelli, M., Sangiuolo, F., D'Agruma, L., Lo Cicero, S., Melchionda, S., Dallapiccola, B. Cell Biochem. Funct. (1993) [Pubmed]
  21. Mutations in the beta-tropomyosin (TPM2) gene--a rare cause of nemaline myopathy. Donner, K., Ollikainen, M., Ridanpää, M., Christen, H.J., Goebel, H.H., de Visser, M., Pelin, K., Wallgren-Pettersson, C. Neuromuscul. Disord. (2002) [Pubmed]
  22. The N-terminal region of troponin T is essential for the maximal activation of rat cardiac myofilaments. Chandra, M., Montgomery, D.E., Kim, J.J., Solaro, R.J. J. Mol. Cell. Cardiol. (1999) [Pubmed]
  23. Identification and analysis of teleost slow muscle troponin T (sTnT) and intronless TnT genes. Campinho, M.A., Power, D.M., Sweeney, G.E. Gene (2005) [Pubmed]
  24. Isolation and localization of a slow troponin (TnT) gene on chromosome 19 by subtraction hybridization of a cDNA muscle library using myotonic dystrophy muscle cDNA. Samson, F., Lee, J.E., Hung, W.Y., Potter, T.G., Herbstreith, M., Roses, A.D., Gilbert, J.R. J. Neurosci. Res. (1990) [Pubmed]
  25. Effects of biological type and dietary fat treatment on factors associated with tenderness: I. Measurements on beef longissimus muscle. Kuber, P.S., Busboom, J.R., Huff-Lonergan, E., Duckett, S.K., Mir, P.S., Mir, Z., McCormick, R.J., Dodson, M.V., Gaskins, C.T., Cronrath, J.D., Marks, D.J., Reeves, J.J. J. Anim. Sci. (2004) [Pubmed]
  26. Thyroid hormone regulates developmental changes in muscle during flounder metamorphosis. Yamano, K., Miwa, S., Obinata, T., Inui, Y. Gen. Comp. Endocrinol. (1991) [Pubmed]
  27. Generation of multiple troponin T isoforms is a common feature of the muscles in various chordate animals. Ohshima, S., Komiya, T., Takeuchi, K., Endo, T., Obinata, T. Comp. Biochem. Physiol., B (1988) [Pubmed]
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