{'fraction_non_alphanumeric': 0.03766816143497758, 'fraction_numerical': 0.007174887892376682, 'mean_word_length': 7.086956521739131, 'pattern_counts': {'":': 0, '<': 0, '<?xml version=': 0, '>': 0, 'https://': 0, 'lorem ipsum': 0, 'www.': 0, 'xml': 0}, 'pii_count': 0, 'substrings_counts': 0, 'word_list_counts': {'cursed_substrings.json': 0, 'profanity_word_list.json': 0, 'sexual_word_list.json': 0, 'zh_pornsignals.json': 0}}
Constitutive expression of β‐N‐acetylhexosaminidase in a microglial cell line: Transcriptional modulation by lipopolysaccharide and serum factors

We investigated the expression of the α‐ and β‐subunits of the lysosomal enzyme β‐N‐acetylhexosaminidase in the BV‐2 microglial cell line under different culture conditions. β‐N‐acetylhexosaminidase from BV‐2 microglia cells was separated into its constituent isoenzymes on diethylaminoethyl (DEAE) cellulose, and its activity was monitored with 4‐methylumbelliferyl‐β‐N‐acetylglucosamine and 4‐methylumbelliferyl‐β‐N‐acetylglucosamine‐6‐sulphate substrates. Forms corresponding to the mouse isoenzymes A and B were present in the cells incubated in serum‐supplemented medium as well as in serum‐free medium. Lipopolysaccharide, a well‐known activator of microglia in vitro, added to the BV‐2 cells in serum‐supplemented medium induced a decrease in the specific enzymatic activity determined with the 4‐methylumbelliferyl‐β‐N‐acetylglucosamine substrate. Lipopolysaccharide had no effect on hexosaminidase isoenzyme pattern of BV‐2 cells in serum‐supplemented medium.