Cytochalasin B: effect on lysosomal enzyme release from human leukocytes.

Cytochalasin B: effect on lysosomal enzyme release from human leukocytes.
复制标题

细胞松弛素 B:对人类白细胞溶酶体酶释放的影响。

DOI:
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发表时间:
1973
影响因子:
11.1
通讯作者:
G. Weissmann
G. Weissmann
中科院分区:
综合性期刊1区
文献类型:
--
作者:
R. Zurier;S. Hoffstein;G. Weissmann

文献摘要

被引文献

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研究了细胞松弛素B对人外周血白细胞的形态学和生化影响。与细胞松弛素B的人类多态基因孵育导致细胞核和细胞质扩散,但不导致溶酶体酶的自发释放。细胞松弛素B抑制颗粒摄取。因此,没有观察到吞噬空泡;相反,当细胞松弛素b处理的细胞受到酶散颗粒的攻击时,颗粒内容物直接排放到周围的培养基中。细胞松弛素B增强了人多形核白细胞溶酶体酶的释放,无论这些酶是否遇到酶酶颗粒或免疫复合物在非吞噬性密孔过滤器上。因此,细胞松弛素b处理的白细胞构成了定量研究溶酶体融合的模型系统。增强的酶释放被先前用影响环核苷酸积累的药物剂量(环核苷酸本身,前列腺素E(1))或干扰微管功能的化合物(例如秋水仙碱,长春花碱)治疗细胞阻断。这些观察结果表明,细胞松弛素B对吞噬细胞的一个作用是消除颗粒之间或与质膜合并的正常限制,并且溶酶体的易位需要完整的微管功能。
The morphological and biochemical consequences of treatment of human peripheral blood leukocytes with cytochalasin B were studied. Incubation of human polymorphs with cytochalasin B resulted in nuclear and cytoplasmic spreading, but not in spontaneous release of lysosomal enzymes. Cytochalasin B inhibited particle uptake. Consequently, phagocytic vacuoles were not observed; instead, granule contents were discharged directly into the surrounding medium when cytochalasin B-treated cells were challenged with zymosan particles. Cytochalasin B enhanced the release of lysosomal enzymes from human polymorphonuclear leukocytes whether these encountered zymosan particles or immune complexes on a nonphagocytosable Millipore filter. Cytochalasin B-treated leukocytes thus constitute a model system for quantitative study of lysosome fusion. Augmented enzyme release was blocked by prior treatment of cells with pharmacological doses of agents that influence the accumulation of cyclic nucleotides (cyclic nucleotides themselves, prostaglandin E(1)) or by compounds that interfere with microtubule function (e.g., colchicine, vinblastine). These observations suggest that one action of cytochalasin B on phagocytic cells is to remove the normal constraints to merger of granules, either with each other or with the plasma membrane, and that intact microtubule function is required for translocation of lysosomes.