N-acetyl-beta-D-glucosaminidase (NAG) isoenzymes release from human monocyte-derived macrophages in response to zymosan and human recombinant interferon-gamma.
Secretion of N-acetyl-beta-D-glucosaminidase (NAG) isoenzymes by human blood monocyte-derived macrophages in response to zymosan and human recombinant interferon-gamma was studied. Macrophages were found to release NAG in response to zymosan, but interferon-gamma has no effect on secretion. Isoenzyme separation by isoelectric focusing demonstrates that non stimulated and zymosan or interferon-gamma treated macrophages release predominantly NAG B and, to a lesser extent, NAG A isoenzymes. In all these conditions, the intracellular intermediate form NAG I could not be detected in the media. Thus, activated macrophages may not be the source of NAG intermediate forms I and P in pathological or maternal serum. In contrast, macrophages could contribute to a significant elevation of urinary activity and NAG B excretion in response to inflammatory conditions.
Bourbouze
R
R
Laboratoire de Chimie Biologique, Faculté de Pharmacie, Université Paris V, France.
Raffi
F
F
Dameron
G
G
Hali-Miraftab
H
H
Loko
F
F
Vilde
J L
JL
D000118:Acetylglucosaminidase / Q000302:isolation & purification / Q000378:metabolism*; D006801:Humans; D007371:Interferon-gamma / Q000494:pharmacology*; D007525:Isoelectric Focusing; D007527:Isoenzymes / Q000302:isolation & purification / Q000378:metabolism*; D008264:Macrophages / Q000187:drug effects / Q000201:enzymology*; D011994:Recombinant Proteins; D015054:Zymosan / Q000494:pharmacology*
D007527:Isoenzymes; D011994:Recombinant Proteins; D007371:Interferon-gamma; D015054:Zymosan; D000118:Acetylglucosaminidase