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Measuring Enzymatic Activity of Neurodevelopmental Disorder-Associated Deubiquitylating Enzymes via an In Vitro Ubiquitin Chain Cleavage Assay
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Lysyl oxidase-like 2 processing by factor Xa modulates its activity and substrate preference.

Huilei Wang1, Alan Poe1, Marta Martinez Yus2

  • 1Department of Biomedical Engineering, Johns Hopkins University School of Medicine, 733 N Broadway, Baltimore, MD, 21205, USA.

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Factor Xa (FXa) processes Lysyl oxidase-like 2 (LOXL2), altering its extracellular matrix cross-linking and collagen substrate preference in vascular smooth muscle cells, potentially impacting fibrotic diseases.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Vascular Biology

Background:

  • Lysyl oxidase-like 2 (LOXL2) is crucial for extracellular matrix (ECM) remodeling in diseases like cardiovascular disease.
  • The proteases that process LOXL2 and the functional consequences remain largely unknown.
  • LOXL2 exists in both full-length and processed forms within cells and tissues.

Purpose of the Study:

  • To identify the protease responsible for LOXL2 processing.
  • To elucidate the functional consequences of LOXL2 processing in vascular smooth muscle cells.
  • To explore the implications of LOXL2 processing in disease.

Main Methods:

  • Protease identification assays.
  • In situ studies using vascular smooth muscle cells.
  • Analysis of ECM cross-linking activity and substrate preference.
  • Investigation of LOXL2 interactions with other LOX family members.

Main Results:

  • Factor Xa (FXa) was identified as the protease that cleaves LOXL2 at Arg-338.
  • LOXL2 processing by FXa did not alter soluble LOXL2 enzymatic activity.
  • In vascular smooth muscle cells, FXa-mediated LOXL2 processing reduced ECM cross-linking and shifted substrate preference from collagen IV to collagen I.
  • Processing increased LOXL2 interaction with prototypical LOX, suggesting a compensatory mechanism.

Conclusions:

  • FXa processes LOXL2, modulating its function in the vascular ECM.
  • LOXL2 processing by FXa may have significant implications in pathologies involving LOXL2 and FXa, such as fibrotic diseases.
  • This interaction highlights a potential regulatory pathway for LOXL2 activity in the vascular environment.