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Related Experiment Videos

Modulation of mannose receptor activity by proteolysis.

V L Shepherd1, R Abdolrasulnia, J Stephenson

  • 1VA Medical Center, Nashville, TN 37212.

The Biochemical Journal
|September 15, 1990
PubMed
Summary

Macrophage mannose receptor activity decreases during inflammation. Trypsin cleaves the receptor, releasing the binding domain and forming a 140 kDa fragment, potentially regulating glycoprotein clearance.

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Area of Science:

  • Immunology
  • Cell Biology
  • Biochemistry

Background:

  • Macrophages possess a cell surface receptor crucial for clearing extracellular glycoproteins.
  • This mannose receptor's activity is impaired in inflammatory conditions due to increased extracellular proteases.
  • Understanding receptor regulation during inflammation is vital for immune response studies.

Purpose of the Study:

  • To investigate the structural and activity changes of the macrophage mannose receptor upon trypsin treatment.
  • To elucidate the mechanism behind activation-associated receptor down-regulation.
  • To determine if trypsin proteolysis contributes to reduced glycoprotein clearance during inflammation.

Main Methods:

  • Treatment of intact macrophages and purified receptor with trypsin (1 µg/ml for 3 h).

Related Experiment Videos

  • Analysis of receptor fragments using SDS-PAGE and Coomassie Blue staining.
  • Assessment of ligand-binding activity and immunoreactivity of receptor fragments.
  • Surface labeling with Na125I to track protein domains.

    • Main Results:

    • Trypsin treatment generated a 140 kDa trypsin-resistant fragment from the mannose receptor.
    • This 140 kDa fragment lost its ligand-binding capability.
    • A smaller 35 kDa fragment was further degraded, and the 140 kDa fragment retained immunoreactivity and some iodinated residues.

    Conclusions:

    • The macrophage mannose receptor undergoes proteolytic cleavage by trypsin at the cell surface.
    • This process releases the ligand-binding domain and produces a membrane-associated 140 kDa fragment.
    • Trypsin-mediated down-regulation of mannose receptor activity may play a role in controlling glycoprotein clearance during inflammation.