Differential incorporation of biotinylated polyamines by transglutaminase 2

Ju Hong Jeon, Chai Wan Kim, Dong Myung Shin, Kyu Il Kim, Sung Yup Cho, Joon Cheol Kwon, Kyung Ho Choi, Heun Soo Kang, In Gyu Kim

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24 Scopus citations

Abstract

Polyamine incorporation or cross-linking of proteins, post-translational modifications mediated by transglutaminase 2 (TGase 2), have been implicated in a variety of physiological functions including cell adhesion, extracellular matrix formation and apoptosis. To better understand the intracellular regulation mechanism of TGase 2, the properties of biotinylated polyamines as substrates for determining in situ TGase activity were analyzed. We synthesized biotinylated spermine (BS), and compared the in vitro and in situ incorporation of BS with that of biotinylated pentylamine (BP), which is an artificial polyamine derivative. When measured in vitro, BP showed a significantly higher incorporation rate than BS. In contrast, in situ incorporation of both BS and BP was not detected even in TGase 2-overexpressed 293 cells. Cells exposed to high calcium showed a marked increase of BP incorporation but not of BS. These data indicate that the in situ activity of TGase 2 gives different results with different substrates, and suggest the possibility of overrepresentation of in situ TGase 2 activity when assayed with BP. Therefore, careful interpretation or evaluation of in situ TGase 2 activity may be required.

Original languageEnglish (US)
Pages (from-to)180-184
Number of pages5
JournalFEBS Letters
Volume534
Issue number1-3
DOIs
StatePublished - Jan 16 2003

Keywords

  • Biotinylated spermine
  • Polyamine conjugation
  • Post-translational modification
  • Transglutaminase 2

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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    Jeon, J. H., Kim, C. W., Shin, D. M., Kim, K. I., Cho, S. Y., Kwon, J. C., Choi, K. H., Kang, H. S., & Kim, I. G. (2003). Differential incorporation of biotinylated polyamines by transglutaminase 2. FEBS Letters, 534(1-3), 180-184. https://doi.org/10.1016/S0014-5793(02)03836-X