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Related Experiment Videos

Paneth cell trypsin is the processing enzyme for human defensin-5.

Dipankar Ghosh1, Edith Porter, Bo Shen

  • 1Department of Immunology, The Cleveland Clinic Foundation, 9500 Euclid Ave., Cleveland, OH 44195, USA.

Nature Immunology
|May 22, 2002
PubMed
Summary

Trypsin in human Paneth cells processes antimicrobial peptide human alpha-defensin 5 (HD5) propeptide. This protease is key for innate immunity regulation in the small intestine.

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Area of Science:

  • Immunology
  • Gastroenterology
  • Molecular Biology

Background:

  • Human alpha-defensin 5 (HD5) is an antimicrobial peptide found in Paneth cells of the small intestine.
  • Unlike other defensins, HD5 is stored as a propeptide within secretory vesicles.
  • HD5 is stored in high quantities, sufficient for microbicidal activity in the intestinal lumen.

Purpose of the Study:

  • To investigate the mechanism of HD5 propeptide processing in human Paneth cells.
  • To identify the specific protease responsible for activating HD5.
  • To elucidate the role of this processing in small intestinal innate immunity.

Main Methods:

  • Immunohistochemistry to detect trypsin isozymes and HD5 colocalization in Paneth cells.
  • In vitro protease assays using purified HD5 propeptide and Paneth cell trypsin.

Related Experiment Videos

  • Analysis of HD5 cleavage products by comparing in vitro results with in vivo isolated peptides.

    • Main Results:

    • A specific pattern of trypsin isozymes was identified in Paneth cells.
    • Trypsin was found to colocalize with HD5 within Paneth cells.
    • Paneth cell trypsin efficiently cleaved HD5 propeptide into forms identical to those found in the intestinal lumen.

    Conclusions:

    • Trypsin acts as a prodefensin convertase in human Paneth cells.
    • Trypsin plays a crucial role in the activation of HD5 and the regulation of innate immunity in the small intestine.