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Related Experiment Videos

Analysis of lactase processing in rabbit

M Rossi1, L Maiuri, V M Salvati

  • 1Department of Pediatrics, University Federico II of Naples, Italy.

FEBS Letters
|December 27, 1993
PubMed
Summary
This summary is machine-generated.

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Proteolytic processing of intestinal lactase-phlorizin-hydrolase (LPH) involves post-Golgi events dependent on microtubule transport. Inhibitors confirmed these cleavages occur after the Golgi apparatus and require intact microtubules for proper transport.

Area of Science:

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Background:

  • Lactase-phlorizin-hydrolase (LPH) is a key intestinal enzyme.
  • Its proteolytic processing is crucial for function but not fully understood.
  • Previous studies suggested unique cleavage in humans.

Purpose of the Study:

  • To investigate the proteolytic processing of rabbit intestinal LPH.
  • To determine the cellular location and dependencies of LPH cleavage events.
  • To clarify if processing is linked to glycosylation or transport.

Main Methods:

  • Pulse-chase and continuous labeling experiments in organ culture.
  • Utilized glycosylation and processing inhibitors (monensin, brefeldin A, MDNM).
  • Employed anti-microtubular drug colchicine to assess transport dependence.

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Main Results:

  • Monensin and brefeldin A inhibited LPH precursor cleavages, indicating post-Golgi events.
  • Inhibition of glycosylation by MDNM did not prevent normal proteolytic processing.
  • Colchicine inhibited cleavages and caused precursor accumulation, suggesting microtubule-dependent transport.

Conclusions:

  • Rabbit LPH proteolytic processing occurs post-Golgi.
  • These cleavages are independent of glycosylation alterations.
  • Intact microtubule transport is essential for LPH proteolytic processing and maturation.