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Gene Review

Trdn  -  triadin

Mus musculus

Synonyms: 2310045H21Rik, EG432451, TDN, Triadin, triadin 1, ...
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Disease relevance of Trdn


High impact information on Trdn

  • Interestingly, the proteins involved in the Ca2+-release cascade (ryanodine receptor, junctin, and triadin) were downregulated, whereas Ca2+-uptake proteins (Ca2+-ATPase and phospholamban) were unchanged or slightly increased [3].
  • These cells, upon withdrawal of mitogens for 5-7 d, were shown by Western blot analysis to express key triadic proteins, including skeletal triadin, calsequestrin, FK506-binding protein, 12 kD, sarco(endo)plasmic reticulum calcium-ATPase1, and dihydropyridine receptors [4].
  • Immunofluorescence labelings of differentiating myocytes with antibodies against alpha1 and alpha2 subunits of DHPRs, RyRs, and triadin show that the skeletal isoforms of all four proteins are abundantly expressed upon differentiation, they appear concomitantly, and they are colocalized [5].
  • In addition, HRCBP interacts with triadin, a protein associated with the ryanodine receptor and thought to be involved in calcium release [1].
  • To better understand the role of triadin 1 in excitation-contraction coupling in the heart, we generated transgenic mice with targeted overexpression of triadin 1 to mouse atrium and ventricle, employing the alpha-myosin heavy chain promoter to drive protein expression [2].

Biological context of Trdn


Anatomical context of Trdn

  • Although a 92-kDa immunoreactive protein could be tentatively identified in myocardium as triadin 3, its expression level was insignificant (</=5%) compared with that of triadin 1 [9].
  • All antibodies detected two prominent proteins of molecular masses 35 and 40 kDa on immunoblots from cardiac microsomes, including the antibody that recognizes only triadin 1 [9].
  • Cardiac myocytes from triadin 1-overexpressing mice exhibited depressed contractility; Ca(2+) transients decayed at a slower rate, and cell shortening and relengthening were diminished [2].
  • The junctions show coupling between exterior membranes and SR, and an apparently normal content and disposition of triadin and calsequestrin [10].
  • In normal differentiating muscle fibers DHPRs, triadin and RyRs are located in intensely immunolabeled foci that are randomly distributed across the fiber [11].

Associations of Trdn with chemical compounds


Physical interactions of Trdn

  • Localization and characterization of the calsequestrin-binding domain of triadin 1. Evidence for a charged beta-strand in mediating the protein-protein interaction [14].
  • Collectively, these results demonstrate a role for triadin as the linkage between the junctional foot protein and dihydropyridine receptor creating a ternary complex at the triad junction in skeletal muscle [13].

Regulatory relationships of Trdn

  • To better understand the role of triadin 1 in SR-Ca(2+) release, we studied the time-dependent expression of SR proteins and contractility in atria of 3-, 6-, and 18-wk-old transgenic mice overexpressing canine cardiac triadin 1 under control of the alpha-myosin heavy chain (MHC) promoter [6].

Other interactions of Trdn

  • Its calcium binding properties, localization to the SR, and interaction with triadin suggest that HRCBP is involved in calcium handling by the SR [1].
  • Confirming this, overexpression of triadin 1 in transgenic mouse hearts produced both the 35-kDa deglycosylated and the 40-kDa glycosylated mobility forms [9].
  • Moreover, triadin 1 appears to anchor calsequestrin to the ryanodine receptor [12].
  • The SR Ca-ATPase has more diffuse distribution than triadin in both normal and dyspedic fibers [11].

Analytical, diagnostic and therapeutic context of Trdn


  1. Increased susceptibility to isoproterenol-induced cardiac hypertrophy and impaired weight gain in mice lacking the histidine-rich calcium-binding protein. Jaehnig, E.J., Heidt, A.B., Greene, S.B., Cornelissen, I., Black, B.L. Mol. Cell. Biol. (2006) [Pubmed]
  2. Cardiac hypertrophy and impaired relaxation in transgenic mice overexpressing triadin 1. Kirchhefer, U., Neumann, J., Baba, H.A., Begrow, F., Kobayashi, Y.M., Reinke, U., Schmitz, W., Jones, L.R. J. Biol. Chem. (2001) [Pubmed]
  3. Regulation of Ca2+ signaling in transgenic mouse cardiac myocytes overexpressing calsequestrin. Jones, L.R., Suzuki, Y.J., Wang, W., Kobayashi, Y.M., Ramesh, V., Franzini-Armstrong, C., Cleemann, L., Morad, M. J. Clin. Invest. (1998) [Pubmed]
  4. A transgenic myogenic cell line lacking ryanodine receptor protein for homologous expression studies: reconstitution of Ry1R protein and function. Moore, R.A., Nguyen, H., Galceran, J., Pessah, I.N., Allen, P.D. J. Cell Biol. (1998) [Pubmed]
  5. Coordinated incorporation of skeletal muscle dihydropyridine receptors and ryanodine receptors in peripheral couplings of BC3H1 cells. Protasi, F., Franzini-Armstrong, C., Flucher, B.E. J. Cell Biol. (1997) [Pubmed]
  6. Altered function in atrium of transgenic mice overexpressing triadin 1. Kirchhefer, U., Baba, H.A., Kobayashi, Y.M., Jones, L.R., Schmitz, W., Neumann, J. Am. J. Physiol. Heart Circ. Physiol. (2002) [Pubmed]
  7. Age-dependent biochemical and contractile properties in atrium of transgenic mice overexpressing junctin. Kirchhefer, U., Baba, H.A., Hanske, G., Jones, L.R., Kirchhof, P., Schmitz, W., Neumann, J. Am. J. Physiol. Heart Circ. Physiol. (2004) [Pubmed]
  8. Cardiac remodeling and atrial fibrillation in transgenic mice overexpressing junctin. Hong, C.S., Cho, M.C., Kwak, Y.G., Song, C.H., Lee, Y.H., Lim, J.S., Kwon, Y.K., Chae, S.W., Kim, d.o. .H. FASEB J. (2002) [Pubmed]
  9. Identification of triadin 1 as the predominant triadin isoform expressed in mammalian myocardium. Kobayashi, Y.M., Jones, L.R. J. Biol. Chem. (1999) [Pubmed]
  10. Morphology and molecular composition of sarcoplasmic reticulum surface junctions in the absence of DHPR and RyR in mouse skeletal muscle. Felder, E., Protasi, F., Hirsch, R., Franzini-Armstrong, C., Allen, P.D. Biophys. J. (2002) [Pubmed]
  11. Correct targeting of dihydropyridine receptors and triadin in dyspedic mouse skeletal muscle in vivo. Takekura, H., Franzini-Armstrong, C. Dev. Dyn. (1999) [Pubmed]
  12. Transgenic triadin 1 overexpression alters SR Ca2+ handling and leads to a blunted contractile response to beta-adrenergic agonists. Kirchhefer, U., Jones, L.R., Begrow, F., Boknik, P., Hein, L., Lohse, M.J., Riemann, B., Schmitz, W., Stypmann, J., Neumann, J. Cardiovasc. Res. (2004) [Pubmed]
  13. Extraction of junctional complexes from triad junctions of rabbit skeletal muscle. Motoike, H.K., Caswell, A.H., Smilowitz, H.M., Brandt, N.R. J. Muscle Res. Cell. Motil. (1994) [Pubmed]
  14. Localization and characterization of the calsequestrin-binding domain of triadin 1. Evidence for a charged beta-strand in mediating the protein-protein interaction. Kobayashi, Y.M., Alseikhan, B.A., Jones, L.R. J. Biol. Chem. (2000) [Pubmed]
  15. Role of ryanodine receptors in the assembly of calcium release units in skeletal muscle. Protasi, F., Franzini-Armstrong, C., Allen, P.D. J. Cell Biol. (1998) [Pubmed]
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