Advertisement

Inflammation Research

, Volume 68, Issue 3, pp 181–184 | Cite as

Promotion of microtubule acetylation plays an important role in degranulation of antigen-activated mast cells

  • Atsushi Shiki
  • Yoshikazu Inoh
  • Satoru Yokawa
  • Tadahide FurunoEmail author
Short Communication
  • 74 Downloads

Abstract

Objective

The aim of this study was to investigate whether microtubule acetylation is triggered by antigen stimulation and how it affects mast cell degranulation.

Methods

The RBL-2H3 cell line was used as a model for mast cells. Acetylation of α-tubulin was analyzed by Western blotting. Intracellular distribution of α-tubulin and acetylated α-tubulin was observed by immunostaining. Degranulation was monitored by measuring the activity of β-hexosaminidase secreted into cell supernatants. Tukey–Kramer test was used to compare differences between groups.

Results

Microtubule acetylation proceeds globally in mast cell cytoplasm after antigen stimulation in addition to accelerated formation of microtubule-organizing centers. Pretreatment with 5Z-7-oxozeaenol (5 µmol/l), an inhibitor of TGF-β-activated kinase 1, which is a key activator of α-tubulin acetyltransferase 1, did not affect the distribution and acetylation of microtubules in resting cells; however, it significantly suppressed antigen-evoked microtubule acetylation and their reorganization, and subsequent degranulation (95.0 ± 1.2% inhibition, n = 3, P < 0.01).

Conclusions

These results provided new insight into the post-translational modifications of microtubule to regulate mast cell degranulation.

Keywords

Mast cell Degranulation Microtubule acetylation Microtubule-organizing center 

Notes

Acknowledgements

This study was supported by Grants from the Japan Society for the Promotion of Sciences Kakenhi grant numbers (17K08255 to YI and 17K07374 to TF).

Compliance with ethical standards

Conflict of interest

The authors declare that they have no conflict of interest.

References

  1. 1.
    Kalesnikoff J, Galli SJ. New developments in mast cell biology. Nat Immunol. 2008;9:1215–23.CrossRefGoogle Scholar
  2. 2.
    Nishida K, Yamasaki S, Ito Y, Kabu K, Hattori K, Tezuka T, Nishizumi H, Kitamura D, Goitsuka R, Geha RS, Yamamoto T, Yagi T, Hirano T. FcεRI-mediated mast cell degranulation requires calcium-independent microtubule-dependent translocation of granules to the plasma membrane. J Cell Biol. 2005;170:115–26.CrossRefGoogle Scholar
  3. 3.
    Song Y, Brady ST. Post-translational modifications of tubulin: pathways to functional diversity of microtubules. Trends Cell Biol. 2015;25:125–36.CrossRefGoogle Scholar
  4. 4.
    Shah N, Kumar S, Zaman N, Pan CC, Bloodworth JC, Lei W, Streicher JM, Hempel N, Mythreye K, Lee NY. TAK1 activation of alpha-TAT1 and microtubule hyperacetylation control AKT signaling and cell growth. Nat Commun. 2018;9:1696.CrossRefGoogle Scholar
  5. 5.
    Portran D, Schaedel L, Xu Z, Théry M, Nachury MV. Tubulin acetylation protects long-lived microtubules against mechanical ageing. Nat Cell Biol. 2017;19:391–8.CrossRefGoogle Scholar
  6. 6.
    Inoh Y, Haneda A, Tadokoro S, Yokawa S, Furuno T. Cationic liposomes suppress intracellular calcium ion concentration increase via inhibition of PI3 kinase pathway in mast cells. Biochim Biophys Acta. 2017;1859:2461–6.CrossRefGoogle Scholar
  7. 7.
    Sulimenko V, Hájková Z, Černohorská M, Sulimenko T, Sládková V, Dráberová L, Vinopal S, Dráberová E, Dráber P. Microtubule nucleation in mouse bone marrow-derived mast cells is regulated by the concerted action of GIT1/βPIX proteins and calcium. J Immunol. 2015;194:4099–111.CrossRefGoogle Scholar

Copyright information

© Springer Nature Switzerland AG 2018

Authors and Affiliations

  1. 1.School of PharmacyAichi Gakuin UniversityNagoyaJapan

Personalised recommendations