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Updated: Jul 9, 2026

Characterizing Modulators of Protease-Activated Receptors with a Calcium Mobilization Assay Using a Plate Reader
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Naturally occurring ACE2 stalk variants are differentially released from the cell.

Florian Wiersch1, Christine Lux1, Julia Vanderliek-Kox1

  • 1Institute of Molecular Pharmacology, Medical Faculty, RWTH Aachen University, Aachen, Germany.

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|July 7, 2026
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Summary
This summary is machine-generated.

The ACE2 stalk region significantly influences ectodomain shedding, affecting soluble ACE2 release. Specific mutations, like P734L, increase ACE2 shedding and surface expression, impacting physiological roles.

Keywords:
ADAM10ADAM17Renin–angiotensin–aldosterone systemSNPsSoluble ACE2

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Angiotensin-converting enzyme 2 (ACE2) regulates the renin-angiotensin-aldosterone system (RAAS) and serves as the SARS-CoV-2 receptor.
  • ACE2 stabilizes the B0AT1 amino acid transporter, making its surface expression critical for physiological functions.
  • Soluble ACE2 is generated via ectodomain shedding, primarily by ADAM10 and ADAM17, but regulatory mechanisms are not fully understood.

Purpose of the Study:

  • To investigate the role of the ACE2 stalk region in ectodomain shedding.
  • To identify specific single-point mutations affecting ACE2 release and surface expression.
  • To determine if B0AT1 complex formation influences ACE2 shedding.

Main Methods:

  • Analysis of 11 naturally occurring single-point mutations in the ACE2 stalk region.
  • Quantification of soluble ACE2 release compared to wild-type (WT) ACE2.
  • Assessment of surface ACE2 and B0AT1 levels.
  • Investigation of ACE2 shedding in the presence of the B0AT1 complex.

Main Results:

  • Most ACE2 stalk region mutations significantly reduced ectodomain shedding.
  • The P734L and G726R mutations markedly increased ACE2 release.
  • ACE2_P734L variant showed enhanced surface expression, leading to increased B0AT1 surface levels.
  • B0AT1 complex formation did not impede ACE2 shedding by sheddases.

Conclusions:

  • The ACE2 stalk region is a critical determinant of ectodomain shedding efficiency.
  • Naturally occurring ACE2 variants can alter soluble ACE2 release, potentially contributing to interindividual pathophysiological differences.
  • Complex formation with B0AT1 does not restrict ACE2 shedding, suggesting sheddase access is not sterically hindered.