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Proteolytic processing of human intestinal lactase-phlorizin hydrolase precursor is not a prerequisite for correct
J Grünberg1, U Luginbühl, E E Sterchi
1Institute of Biochemistry and Molecular Biology, Faculty of Medicine, University of Berne, Switzerland.
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.