<原著>マウス腹腔内マクロファージのザイモサン貪食について

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概要

• 論文の詳細を見る

• The cell membrane and cytoskeletons of mouse peritoneal macrophages at various stages of phagocytosis of zymosan or latex particles were visualized by scanning electron microscopy (SEM). Zymosan particles were phagocytosed through the characteristic "craters" on the cell surface within 15 min of incubation. After further incubation for 15 min, the zymosan particles were engulfed into the cell and accumulated around the perinuclear region. On the other hand, latex particles were phagocytosed in the conventional style. This difference was confirmed by SEM of the cytoskeleton. At the early stage of phagocytosis, the craters appeared, and the cytoskeleton formed a basket-like shape around the zymosan particles from a distance. At the later stage of plagocytosis, zymosan particles were engulfed into the cell, and the cytoskeleton became attached to and redistributed radially around the zymosan particles at the perinuclear region. On the macrophages phagocytosing latex particles, the basket-like shape of cytoskeleton and the distance were not observed during the phagocytosis. To determine what kind of cytoskeleton distributes during the phagocytosis of zymosan, the cytoskeletons were double stained with rhodamine-phalloidin for F-actin and with indirect immunofluorescence for vimentin or actin binding proteins, α-actinin, calmodulin, clathrin, myosin or gelsolin, and observed with a phase contrast microscope equipped with epifluorescence optics. Within 15 min of incubation, F-actin accumulated and formed a ring around the zymosan particles at the peripheral region. Vimentin and actin binding proteins were also distributed in the same pattern as F-actin. After further incubation for 15 min, the ringed accumulation of cytoskeletons and actin binding proteins disappeared. The distribution of these cytoskeletons and actin binding proteins of macrophages phagocytosing latex particles was similar to that observed during zymosan phagocytosis. The effect of the major constituents of zymosan on zymosan binding to the cell membrane of macrophage at 4℃ was investigated. The yeast β-glucan and the algal β-glucan (laminarin) markedly indibited zymosan binding to the cell membrane and the inhibitory effect was does dependent, but mannan and N-acetyl-D-glucosamine did not affect it. These results suggest that, the receptor of macrophage for zymosan is the β-glucan receptor.

• 近畿大学の論文
• 1991-03-25

著者

• 本田 秀明

  近畿大学医学部細菌学教室

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