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MTPN  -  myotrophin

Homo sapiens

Synonyms: GCDP, MYOTROPHIN, Myotrophin, Protein V-1, V-1
 
 
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Disease relevance of MTPN

  • From these observations, we conclude that myotrophin is present in normal human hearts, is found at higher levels in dilated cardiomyopathic human hearts, and may play a role in the initiation of cardiac hypertrophy as well as in normal growth of cardiac myocytes in humans [1].
  • We verify that recombinant human myotrophin produces cardiomyocyte hypertrophy, and we demonstrate for the first time that elevated levels of myotrophin/V-1 protein mRNA are expressed in human dilated cardiomyopathic hearts [2].
  • One adenoma that had a brisk cortisol response in vivo, also had in vitro cortisol responses that were inhibited by a specific V1 antagonist [3].
  • V-1 Immunitor (V1) is a therapeutic vaccine comprising pooled HIV antigens formulated into an oral pill [4].
  • Recent V1 studies demonstrated body weight gain, increase in CD4 and CD8 cells, decrease in viral load, and improved survival of end-stage AIDS patients [4].
 

High impact information on MTPN

 

Biological context of MTPN

 

Anatomical context of MTPN

  • Peptide-reactive CD4(+) T cells recognized recombinant Bet v 1 protein, indicating that these peptides are produced by the MHC class II Ag processing pathway [10].
  • V-1 binding inhibited the ability of CP to cap the barbed ends of actin filaments [11].
  • The contribution of myotrophin to NFkappaB-mediated gene transcription and preservation of cardiac muscle mass remains to be investigated further [9].
  • The V1 messenger ribonucleic acid (mRNA) was detected in normal adrenal cortex and in all tumors [3].
  • Using immunoglobulins highly specific for V1 and V3 in autopsy samples we have observed that the human left ventricle is mostly composed of a V3 isoform (HV3) and that small amounts (1 to 15%) of a V1 type (HV1) are present in foetal and some adult hearts [12].
 

Associations of MTPN with chemical compounds

  • Recombinant myotrophin was found to stimulate protein synthesis by fivefold, as analyzed by incorporation studies using [3H] lysine [8].
  • To illustrate the utility of this labeling, we tagged the NF-kappaB p50 transcription factor with benzophenone, cross-linked with UV light, and observed increased levels of p50 homodimerization in the presence of DNA and the binding protein myotrophin [13].
  • Among the 6 recently operated patients who had been subjected to the vasopressin test in vivo, the tumor V1 mRNA levels were higher in the 4 responders (9.5 x 10(3) to 5.0 x 10(4)) than in the 2 nonresponders (2.0 x 10(2) and 1.8 x 10(3)) [3].
  • Proline mutants were used to show that the minor kinetic phases observed for myotrophin arise from heterogeneity of the ground states due to cis-trans isomerisation of prolyl as well as non-prolyl peptide bonds [14].
  • Variable expression of the V1 vasopressin receptor modulates the phenotypic response of steroid-secreting adrenocortical tumors [3].
 

Other interactions of MTPN

 

Analytical, diagnostic and therapeutic context of MTPN

  • Myotrophin purified from human dilated cardiomyopathic hearts is composed of a single polypeptide chain having an apparent molecular mass of 12 kD, determined by SDS-PAGE [1].
  • Western blot analysis showed the presence of myotrophin in both dilated cardiomyopathic and normal human hearts [1].
  • To evaluate the role of myotrophin in the initiation of the human dilated cardiomyopathic heart, we have isolated and purified myotrophin to homogeneity (approximately 50,000-fold) as defined by reverse-phase high-performance liquid chromatography and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) [1].
  • Sequence analysis indicators high homology (>90%) between all species at both the nucleotide and amino acid levels, and Southern blot analysis of genomic DNA from diverse species verifies that myotrophin/V-1 is a highly conserved gene [2].
  • We analyzed the interaction of recombinant myotrophin and nuclear extracts prepared from neonatal and adult cardiomyocytes; gel mobility shift assay showed that myotrophin bound to kappaB DNA [7].

References

  1. Myotrophin in human cardiomyopathic heart. Sil, P., Misono, K., Sen, S. Circ. Res. (1993) [Pubmed]
  2. cDNA sequence and characterization of the gene that encodes human myotrophin/V-1 protein, a mediator of cardiac hypertrophy. Anderson, K.M., Berrebi-Bertrand, I., Kirkpatrick, R.B., McQueney, M.S., Underwood, D.C., Rouanet, S., Chabot-Fletcher, M. J. Mol. Cell. Cardiol. (1999) [Pubmed]
  3. Variable expression of the V1 vasopressin receptor modulates the phenotypic response of steroid-secreting adrenocortical tumors. Arnaldi, G., Gasc, J.M., de Keyzer, Y., Raffin-Sanson, M.L., Perraudin, V., Kuhn, J.M., Raux-Demay, M.C., Luton, J.P., Clauser, E., Bertagna, X. J. Clin. Endocrinol. Metab. (1998) [Pubmed]
  4. V-1 Immunitor: oral therapeutic AIDS vaccine with prophylactic potential. Jirathitikal, V., Sooksathan, P., Metadilogkul, O., Bourinbaiar, A.S. Vaccine (2003) [Pubmed]
  5. Activation of nuclear factor-kappaB is necessary for myotrophin-induced cardiac hypertrophy. Gupta, S., Purcell, N.H., Lin, A., Sen, S. J. Cell Biol. (2002) [Pubmed]
  6. Assignment of myotrophin to human chromosome band 7q33-->q35 by in situ hybridization. Mitra, S., Timur, A.A., Gupta, S., Wang, Q., Sen, S. Cytogenet. Cell Genet. (2001) [Pubmed]
  7. Myotrophin-kappaB DNA interaction in the initiation process of cardiac hypertrophy. Gupta, S., Sen, S. Biochim. Biophys. Acta (2002) [Pubmed]
  8. Stimulation of protein (collagen) synthesis in sponge cells by a cardiac myotrophin-related molecule from Suberites domuncula. Schröder, H.C., Krasko, A., Batel, R., Skorokhod, A., Pahler, S., Kruse, M., Müller, I.M., Müller, W.E. FASEB J. (2000) [Pubmed]
  9. Myotrophin in human heart failure. O'Brien, R.J., Loke, I., Davies, J.E., Squire, I.B., Ng, L.L. J. Am. Coll. Cardiol. (2003) [Pubmed]
  10. Functional Analysis of Birch Pollen Allergen Bet v 1-Specific Regulatory T Cells. Nagato, T., Kobayashi, H., Yanai, M., Sato, K., Aoki, N., Oikawa, K., Kimura, S., Abe, Y., Celis, E., Harabuchi, Y., Tateno, M. J. Immunol. (2007) [Pubmed]
  11. Binding of Myotrophin/V-1 to Actin-capping Protein: IMPLICATIONS FOR HOW CAPPING PROTEIN BINDS TO THE FILAMENT BARBED END. Bhattacharya, N., Ghosh, S., Sept, D., Cooper, J.A. J. Biol. Chem. (2006) [Pubmed]
  12. Left ventricular isomyosins in normal and hypertrophied rat and human hearts. Schwartz, K., Apstein, C., Mercadier, J.J., Lecarpentier, Y., de la Bastie, D., Bouveret, P., Wisnewsky, C., Swynghedauw, B. Eur. Heart J. (1984) [Pubmed]
  13. Transglutaminase-catalyzed site-specific conjugation of small-molecule probes to proteins in vitro and on the surface of living cells. Lin, C.W., Ting, A.Y. J. Am. Chem. Soc. (2006) [Pubmed]
  14. Biophysical characterisation of the small ankyrin repeat protein myotrophin. Lowe, A.R., Itzhaki, L.S. J. Mol. Biol. (2007) [Pubmed]
  15. 1,25(OH)(2)-vitamin D(3) actions on cell proliferation, size, gene expression, and receptor localization, in the HL-1 cardiac myocyte. Nibbelink, K.A., Tishkoff, D.X., Hershey, S.D., Rahman, A., Simpson, R.U. J. Steroid Biochem. Mol. Biol. (2007) [Pubmed]
  16. Sustainable production of bioactive compounds from sponges: primmorphs as bioreactors. Schröder, H.C., Brümmer, F., Fattorusso, E., Aiello, A., Menna, M., de Rosa, S., Batel, R., Müller, W.E. Prog. Mol. Subcell. Biol. (2003) [Pubmed]
 
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