Neutral endopeptidase-24.11 (enkephalinase). Biosynthesis and localization in human fibroblasts.
The biosynthesis, glycosylation and subcellular localization of the neutral endopeptidase-24.11 were studied in cultured human fibroblasts. The enzyme was synthesized as a precursor (Mr 88,000) containing four or five N-linked oligosaccharides. Within 1 h the synthesis-mature (Mr 94,000) endopeptidase-24.11 was formed and contained sialylated oligosaccharides. The half-life of endopeptidase-24.11 was 3.7 days and in the presence of 10 mM-NH4Cl it increased to 6 days. Mature endopeptidase-24.11 was solubilized with 0.2% saponin and partitioned into Triton X-114. In intact fibroblasts, endopeptidase-24.11 was accessible to antibodies and to neuraminidase even when the treatment was performed at 4 degrees C. The localization of endopeptidase-24.11 to the plasma membrane in cultured fibroblasts was further demonstrated by immunocytochemistry.
D002462:Cell Membrane / Q000201:enzymology; D002478:Cells, Cultured; D004591:Electrophoresis, Polyacrylamide Gel; D005347:Fibroblasts / Q000201:enzymology; D006031:Glycosylation; D006801:Humans; D007150:Immunohistochemistry; D008666:Metalloendopeptidases / Q000096:biosynthesis / Q000378:metabolism*; D015260:Neprilysin; D013347:Subcellular Fractions / Q000201:enzymology
D008666:Metalloendopeptidases; D015260:Neprilysin