Proteolytic processing of human intestinal lactase‐phlorizin hydrolase precursor is not a prerequisite for correct sorting in Madin Darby canine kidney (MDCK) cells
- 17 December 1992
- journal article
- Published by Wiley in FEBS Letters
- Vol. 314 (3) , 224-228
- https://doi.org/10.1016/0014-5793(92)81476-3
Abstract
Maturation or 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.Keywords
This publication has 24 references indexed in Scilit:
- Maturation of human lactase‐phlorizin hydrolase Proteolytic cleavage of precursor occurs after passage through the Golgi complexFEBS Letters, 1992
- Basolateral sorting in MDCK cells requires a distinct cytoplasmic domain determinantCell, 1991
- The biosynthetic basis of adult lactase deficiency.Journal of Clinical Investigation, 1990
- Distinct transport vesicles mediate the delivery of plasma membrane proteins to the apical and basolateral domains of MDCK cells.The Journal of cell biology, 1990
- The trans Golgi Network: Sorting at the Exit Site of the Golgi ComplexScience, 1986
- Cell Surface Polarity in EpitheliaAnnual Review of Cell Biology, 1985
- Expression and intracellular transport of microvillus membrane hydrolases in human intestinal epithelial cells.The Journal of cell biology, 1985
- Biosynthesis of intestinal microvillar proteins intracellular processing of lactase-phlorizin hydrolaseBiochemical and Biophysical Research Communications, 1984
- Evidence for biosynthesis of lactase-phlorizin hydrolase as a single-chain high-molecular weight precursorBiochimica et Biophysica Acta (BBA) - General Subjects, 1984
- Studies of small intestine during development I. Distribution and activity of ß-galactosidaseBiochimica et Biophysica Acta, 1962