Alpha 2-macroglobulin and other proteinase inhibitors do not interfere with the secretion of amyloid precursor protein in mouse neuroblastoma cells

B De Strooper; F Van Leuven; H Van den Berghe

doi:10.1016/0014-5793(92)81048-q

Alpha 2-macroglobulin and other proteinase inhibitors do not interfere with the secretion of amyloid precursor protein in mouse neuroblastoma cells

FEBS Lett. 1992 Aug 10;308(1):50-3. doi: 10.1016/0014-5793(92)81048-q.

Authors

B De Strooper¹, F Van Leuven, H Van den Berghe

Affiliation

¹ Center for Human Genetics, University of Leuven, Belgium.

PMID: 1379551
DOI: 10.1016/0014-5793(92)81048-q

Abstract

A series of proteinase inhibitors active against proteinases of all four major classes, including highly purified and well-characterized alpha 2-macroglobulin, added to the cell culture medium of murine Neuro 2a neuroblastoma cells did not interfere with APP secretase activity. We therefore advance the hypothesis that APP secretase activity is localized in an intracellular compartment.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amyloid beta-Protein Precursor / metabolism*
Animals
Blotting, Northern
Electrophoresis, Gel, Pulsed-Field
Mice
Neuroblastoma / metabolism*
Protease Inhibitors / metabolism*
RNA / metabolism
Tumor Cells, Cultured
alpha-Macroglobulins / metabolism*

Substances

Amyloid beta-Protein Precursor
Protease Inhibitors
alpha-Macroglobulins
RNA