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Galectin-8 modulates human osteoclast activity partly through isoform-specific interactions

Michèle Roy1, Léopold Mbous Nguimbus1, Papa Yaya Badiane1

  • 1Division of Rheumatology, Department of Medicine, Faculty of Medicine and Health Sciences, University of Sherbrooke, Sherbrooke, Canada.

Life Science Alliance
|February 23, 2024
PubMed

Insights

This study reveals galectin-8

Area of Science:

  • Osteoclast biology
  • Cell signaling
  • Molecular interactions

Background:

  • Alternative splicing of LGALS8 (galectin-8) in osteoclasts reduces long isoform expression.
  • Galectin-8's roles in cell-matrix interactions and danger recognition are known, but its function in osteoclasts was uncharacterized.
  • Osteoclast overactivity is linked to bone diseases.

Purpose of the Study:

  • To investigate the role of galectin-8 in human osteoclast function.
  • To determine the specific contributions of galectin-8 isoforms to osteoclast biology.
  • To identify galectin-8 interacting proteins in osteoclasts.

Main Methods:

  • Inhibition of galectin-8 expression in human osteoclasts.
  • Isoform-specific inhibition of galectin-8.
  • Liquid chromatography with tandem mass spectrometry (LC-MS/MS) proteomic analysis.
  • Confirmation of protein interactions in human osteoclasts.

Main Results:

  • Galectin-8 inhibition impacts bone resorption, osteoclast nuclearity, and mTORC1 signaling.
  • The short isoform of galectin-8 plays a primary role in bone resorption.
  • LC-MS/MS identified shared and short isoform-specific interacting proteins, including cell adhesion and lysosomal proteins.
  • Confirmed interactions with CLCN3, CLCN7, LAMP1, and LAMP2, which localize to secretory vesicles.

Conclusions:

  • Galectin-8 has direct roles in regulating osteoclast activity.
  • The short galectin-8 isoform is predominantly responsible for these effects.
  • Galectin-8 interacts with key proteins involved in osteoclast function and vesicle transport.

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