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Megalomicin disrupts lysosomal functions

P Bonay1, M Fresno, B Alarcón

  • 1Centro de Biologia Molecular Severo Ochoa, CSIC-Universidad Autonoma de Madrid, Cantoblanco, Spain.

Journal of Cell Science
|August 1, 1997
PubMed
Summary

Megalomicin (MGM) rapidly swells lysosomes and blocks protein degradation. This drug impairs lysosome delivery and acidification, impacting cellular waste removal and antigen processing.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Megalomicin (MGM) disrupts Golgi complex morphology and inhibits protein transport.
  • This leads to accumulation of poorly sialylated glycoproteins.

Purpose of the Study:

  • To investigate the effects of MGM on lysosomal function and protein degradation.
  • To elucidate the mechanism behind MGM's cellular impact.

Main Methods:

  • Treatment of cultured cells with MGM.
  • Analysis of lysosomal swelling and degradation of T cell antigen receptor CD36 subunit.
  • Tracking fluid phase markers and endocytosed ovalbumin using Percoll density gradients.
  • Assessing epidermal growth factor receptor delivery to lysosomes.
  • In vitro assay of ATP-dependent lysosomal acidification.

Main Results:

  • MGM caused rapid lysosomal swelling and inhibited degradation of newly synthesized CD36.
  • MGM prevented degradation of fluid phase markers, which accumulated in endosomal fractions.
  • Delivery of membrane-bound epidermal growth factor receptor to lysosomes was also inhibited.
  • MGM strongly inhibited ATP-dependent lysosomal acidification in vitro.

Conclusions:

  • MGM impairs lysosomal function by inhibiting the delivery of endocytosed materials.
  • MGM disrupts lysosomal acidification, potentially explaining its in vivo effects.
  • MGM affects both soluble and membrane-bound protein degradation pathways within lysosomes.

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