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TTR  -  transthyretin

Gallus gallus

 
 
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High impact information on TTR

  • The embryo synthesizes every plasma protein including fetoproteins and "adult" proteins (prealbumin, albumin, and transferrin) [1].
  • In concordance with the intraoocytic localization in an endosomal compartment, ligand blotting and chemical cross-linking experiments revealed the presence of a approximately 115-kDa TTR-binding oocyte membrane protein [2].
  • Furthermore, in contrast to the serum levels of the yolk precursor lipoproteins, those of TTR were not significantly changed by estrogen; thus, TTR represents a newly defined, estrogen-independent class of yolk precursor proteins [2].
  • These data strongly suggest that oocytic TTR is derived from the circulation, where it is a constitutive component, and deposited into yolk as a result of endocytosis mediated by a specific receptor [2].
  • T3 is subsequently bound to its carrier protein, transthyretin (TTR), to allow transport through the cerebrospinal fluid [3].
 

Biological context of TTR

 

Anatomical context of TTR

 

Associations of TTR with chemical compounds

  • For transport in serum, retinol is bound to retinol-binding protein (RBP), which in turn forms a complex with transthyretin (TTR) [7].
  • The presence of serum transferrin, two embryo-specific alpha-globulins, and a prealbumin were demonstrated by acrylamide gel analysis [8].
 

Analytical, diagnostic and therapeutic context of TTR

  • Western blots of yolk collected from oocytes at different stages of growth show that both RBP and TTR, but not albumin, are more abundant at early stages relative to total yolk protein [7].

References

  1. Characterization of embryonic antigens in the plasma of developing chick embryos. Weller, E.M. Cancer Res. (1976) [Pubmed]
  2. Transport of serum transthyretin into chicken oocytes. A receptor-mediated mechanism. Vieira, A.V., Sanders, E.J., Schneider, W.J. J. Biol. Chem. (1995) [Pubmed]
  3. Type II iodothyronine deiodinase protein in chicken choroid plexus: additional perspectives on T3 supply in the avian brain. Verhoelst, C.H., Darras, V.M., Roelens, S.A., Artykbaeva, G.M., Van der Geyten, S. J. Endocrinol. (2004) [Pubmed]
  4. Competitive interactions of chlorinated phenol compounds with 3,3',5-triiodothyronine binding to transthyretin: detection of possible thyroid-disrupting chemicals in environmental waste water. Yamauchi, K., Ishihara, A., Fukazawa, H., Terao, Y. Toxicol. Appl. Pharmacol. (2003) [Pubmed]
  5. New genetic polymorphism recognized in the prealbumin region of chicken egg yolk. Kurył, J., Gasparska, J. Animal blood groups and biochemical genetics. (1983) [Pubmed]
  6. Demonstration of a novel molecular species in chick embryo brain: cellular retinol-binding protein, F-type. Sato, M., Omori, M., Muto, Y. J. Nutr. Sci. Vitaminol. (1979) [Pubmed]
  7. Transport and uptake of retinol during chicken oocyte growth. Vieira, A.V., Schneider, W.J. Biochim. Biophys. Acta (1993) [Pubmed]
  8. Serum protein synthesis in the early chick embryo. Kram, D., Klein, N.W. Dev. Biol. (1976) [Pubmed]
 
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