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ADAM10 and ADAM17 are degraded by lysosomal pathway via asparagine endopeptidase

Xingyu Zhang1, Li Tang1, Zhentao Zhang1

  • 1Department of Neurology, Renmin Hospital of Wuhan University, Wuhan, 430060, China.

Insights

The lysosomal protease AEP degrades ADAM10 and ADAM17, enzymes that protect against Alzheimer's disease (AD). AEP-mediated degradation of these enzymes may contribute to AD pathogenesis.

Area of Science:

  • Neuroscience
  • Molecular Biology
  • Biochemistry

Background:

  • ADAM10 and ADAM17 are metalloproteinases crucial for cleaving membrane-bound proteins.
  • These enzymes act as alpha-secretases, processing amyloid precursor protein (APP) and preventing amyloid-beta production, offering protection against Alzheimer's disease (AD).
  • The degradation pathways for ADAM10 and ADAM17 are currently unknown.

Purpose of the Study:

  • To elucidate the degradation pathway of ADAM10 and ADAM17.
  • To investigate the role of the lysosomal cysteine protease, AEP, in ADAM10/17 degradation.
  • To explore the potential link between AEP-mediated degradation and Alzheimer's disease pathogenesis.

Main Methods:

  • Investigated the degradation pathway of ADAM10 and ADAM17 using cellular and molecular biology techniques.
  • Examined the direct interaction and cleavage activity of AEP on ADAM10/17.
  • Utilized knockout models to assess the impact of AEP absence on ADAM10/17 levels in the brain.

Main Results:

  • ADAM10 and ADAM17 are degraded via the lysosomal pathway.
  • AEP directly cleaves ADAM10 and ADAM17.
  • AEP knockout leads to increased levels of ADAM10 and ADAM17 in the brain.

Conclusions:

  • The lysosomal cysteine protease AEP plays a significant role in degrading ADAM10 and ADAM17.
  • AEP-mediated degradation of ADAM10/17 may be implicated in the pathogenesis of Alzheimer's disease.
  • Targeting AEP could offer a novel therapeutic strategy for AD.

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