Journal of Life Science (생명과학회지)

Korean Society of Life Science (한국생명과학회)
권호 표지
DOI QR코드

DOI QR Code

Dimerization of Thyroglobulin in the Endoplasmic Reticulum

Thyroglobulin의 소포체내 dimerization

  • Published : 2003.06.01
Download PDF
⟨ Previous Next ⟩

Abstract

The kinetics of dimerization of a newly synthesized thyroglobulin (Tg), the precursor protein in the manufacture of thyroid hormone, was investigated in the endoplasmic reticulum of thyrocytes FRTL-5 cell line. The folded monomeric Tg was first detectable in a conformationally unstable form, from the examination of lysates of pulse labeled cultured thyrocytes by denaturing and nondenaturing gel electrophoresis by 15 min after biosynthesis. The first dimeric Tg was formed by 30 min after; the monomer declined and the dimer progressively increased, and 40 min after remarkable dimeric Tg form was found. Finally, dimerization was complete at 60 min after.

갑상선호르몬의 전구체인 thyroglobulin (Tg)이 어떻게 dimerization이 일어나는지를 조사하였다, 변성 혹은 비변성전기영동법으로 관찰한 결과 새롭게 만들어지기 시작한 Tg는 15분에 처음으로 구조적으로 불안정하지만 folded monomer가 관찰되었다. 그 이후에 monomer가 dimer로 바뀌어 결국 30분에 dimer Tg가 만들어지기 시작하여 40분에는 dimer Tg가 관찰되었다. 최종적으로 60분에 완전하게 dimerization된 Tg가 만들어졌다.

Keywords

References

  1. Arvan, P. and J. Lee. 1991. Regulated and constitutive protein targeting can be distinguished by secretory polarity in thyroid epithelial cells. J. Cell Bioi. 112, 365-376 https://doi.org/10.1083/jcb.112.3.365
  2. Baudry, N., P. J. Lejeune., P. Niccoli., L. Vinet., P. Carayon and B. Mallet. 1996. Dityrosine bridge for-mation and thyroid hormone synthesis are tightly linked and are both dependent on N-glycans. FEBS Lett. 396, 223-226 https://doi.org/10.1016/0014-5793(96)01107-6
  3. Deshpande, V. and S. G. Venkatesh. 1999. Thyro-globulin, the prothyroid hormone: chemistry, synthesis and degradation. Biochim. Biophys. Acta. 1430, 157-178 https://doi.org/10.1016/S0167-4838(99)00015-1
  4. Di Jesc, B., R. Pereira., E. Consiglio., S. Formisano., J. Satrustegui and I. V. Sandoval. 1998. Demonstration of a $Ca^{2+}$ requirement for thyroglobulin dimerization and export to the golgi complex. Eur. J. Biochem. 252, 583-590 https://doi.org/10.1046/j.1432-1327.1998.2520583.x
  5. Fewell, S. W., K. J. Travers., J. S. Weissman and J. L. Brodsky. The action of molecular chaperones in the early secretory pathway. 2001. Ann. Rev. Genet. 35, 149-191 https://doi.org/10.1146/annurev.genet.35.102401.090313
  6. Freudl, R., M. Klose and U. Henning. 1990. Export and sorting of the Escherichia coli outer membrane protein OmpA. J. Bioenerg. Biomembr. 22, 441-449 https://doi.org/10.1007/BF00763176
  7. Kim, P. S. and P. Arvan. 1991. Folding and assembly of newly synthesized thyroglobulin occurs in a pre-Golgi compartment. J. Biol. Chem. 266, 12412-12418
  8. Kim, P. S., D. Bole and P. Arvan. 1992. Transient aggregation of nascent thyroglobulin in the endoplasmic reticulum: relationship to the molecular chaperone, BiP. J. Cell BioI. 118, 541-549 https://doi.org/10.1083/jcb.118.3.541
  9. Kim, P. S., O. Y. Kwon and P. Arvan. 1996. An en-doplasmic reticulum storage disease causing congenital goiter with hypothyroidism. J. Cell Bioi. 133, 517-527 https://doi.org/10.1083/jcb.133.3.517
  10. Petaja-Repo, U. E., M. Hogue., A. Laperriere., P. Walk-er and M. Bouvier. 2000. Export from the endoplasmic reticulum represents the limiting step in the maturation and cell surface expression of the human delta opioid receptor. J. Biol. Chem. 275, 13727-13736 https://doi.org/10.1074/jbc.275.18.13727