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N-乙酰-β-D-氨基葡萄糖苷酶(NAG)同工酶在酵母聚糖和人重组干扰素-γ作用下从人单核细胞衍生的巨噬细胞中释放。

N-acetyl-beta-D-glucosaminidase (NAG) isoenzymes release from human monocyte-derived macrophages in response to zymosan and human recombinant interferon-gamma.

作者信息

Bourbouze R, Raffi F, Dameron G, Hali-Miraftab H, Loko F, Vilde J L

机构信息

Laboratoire de Chimie Biologique, Faculté de Pharmacie, Université Paris V, France.

出版信息

Clin Chim Acta. 1991 Jun 14;199(2):185-94. doi: 10.1016/0009-8981(91)90110-x.

DOI:10.1016/0009-8981(91)90110-x
PMID:1908363
Abstract

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.

摘要

研究了人血单核细胞衍生的巨噬细胞在响应酵母聚糖和人重组干扰素-γ时N-乙酰-β-D-氨基葡萄糖苷酶(NAG)同工酶的分泌情况。发现巨噬细胞在响应酵母聚糖时会释放NAG,但干扰素-γ对分泌没有影响。通过等电聚焦进行同工酶分离表明,未受刺激以及经酵母聚糖或干扰素-γ处理的巨噬细胞主要释放NAG B,其次是NAG A同工酶。在所有这些情况下,培养基中均未检测到细胞内中间形式NAG I。因此,活化的巨噬细胞可能不是病理或母体血清中NAG中间形式I和P的来源。相反,巨噬细胞可能会导致炎症条件下尿液活性和NAG B排泄量显著升高。

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