Proteolytic processing of human intestinal lactase-phlorizin hydrolase precursor is not a prerequisite for correct sorting in Madin Darby canine kidney (MDCK) cells

FEBS Lett. 1992 Dec 21;314(3):224-8. doi: 10.1016/0014-5793(92)81476-3.

Abstract

Maturation of lactase-phlorizin hydrolase (LPH) (EC 3.2.1.23-62) requires proteolytic processing of precursor (pro-LPH) to mature microvillus membrane enzyme (m-LPH). Subcellular site and function of this processing are unknown. We studied the processing and sorting of human LPH expressed permanently in MDCK cells. LPH was inserted into the apical membrane and small amounts were found basolateral. Of the LPH immunoprecipitated from the apical membrane, 42% was in the mature, i.e. proteoytically processed form; on the basolateral membrane it was 20%. Thus, LPH-processing occurs after sorting and is not necessary for surface expression.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Biological Transport
  • Butyrates / pharmacology
  • Butyric Acid
  • Cell Line
  • Dogs
  • Enzyme Precursors / metabolism*
  • Epithelium / enzymology
  • Gene Expression Regulation, Enzymologic / drug effects
  • Humans
  • Intestines / enzymology*
  • Lactase
  • Lactase-Phlorizin Hydrolase / metabolism*
  • Multienzyme Complexes / metabolism
  • Precipitin Tests
  • Protein Processing, Post-Translational*
  • Transfection
  • beta-Galactosidase / metabolism*

Substances

  • Butyrates
  • Enzyme Precursors
  • Multienzyme Complexes
  • Butyric Acid
  • Lactase
  • beta-Galactosidase
  • Lactase-Phlorizin Hydrolase