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Anoctamin-6 regulates ADAM sheddase function.

Martin Veit1, Katharina Isabelle Koyro1, Björn Ahrens1

  • 1Dept. of Dermatology, University of Kiel, 24105 Kiel, Germany.

Biochimica Et Biophysica Acta. Molecular Cell Research
|October 18, 2018
PubMed
Summary

Anoctamin-6 (ANO6) enhances ADAM17 sheddase activity by promoting calcium-dependent phosphatidylserine exposure. This ANO6 function regulates the release of key substrates like Amphiregulin and TGF-alpha.

Keywords:
ADAM17Anoctamin-6PhosphatidylserineScramblaseShedding

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • ADAM17 (a disintegrin and metalloproteinase) cleaves transmembrane proteins like TGF-alpha, Amphiregulin (AREG), and TNFR1, regulating cellular functions.
  • Surface exposure of phosphatidylserine (PS) is crucial for ADAM17 sheddase activity.
  • Anoctamin-6 (ANO6) is a calcium-dependent phospholipid scramblase.

Purpose of the Study:

  • To investigate the potential link between ANO6 scramblase activity and ADAM17 sheddase function.
  • To determine if ANO6 influences the release of ADAM17 substrates.

Main Methods:

  • Overexpression of ANO6 in HEK293T cells.
  • Treatment with calcium ionophores and PMA (a PKC-dependent ADAM17 activator).
  • Use of a constitutively active ANO6 mutant.
  • Inhibitor experiments targeting metalloproteinases.
  • siRNA-mediated downregulation of ANO6 in HUVECs.

Main Results:

  • ANO6 overexpression increased calcium-mediated PS exposure and enhanced AREG and TGF-alpha release.
  • Constitutively active ANO6 mutant induced spontaneous PS exposure and substrate release.
  • ANO6-mediated substrate cleavage broadened the spectrum of involved metalloproteinases.
  • ANO6 downregulation reduced ionophore-mediated TNFR1 release in HUVECs.

Conclusions:

  • ANO6 regulates ADAM17 sheddase activity through calcium-dependent PS exposure.
  • ANO6 may act as a key regulator of the ADAM metalloproteinase network at the plasma membrane.