Spilberg I, Mandell B, Mehta J, Sullivan T, Simchowitz L
J Lab Clin Med. 1978 Aug;92(2):297-302.
The peptide Gly-His-Gly is shown to be chemotactic for human neutrophils in vitro and for rabbit neutrophils in vivo but to be unable to induce lysosomal enzyme release from human neutrophils at sublytic concentrations. The failure of this chemotactic peptide to elicit lysosomal enzyme release provides evidence that interactions with a chemotactic receptor does not necessarily activate chemotaxis and exocytosis in the human neutrophil, thus suggesting that the presumed common pathway of exocytosis and chemotaxis may be divergent at the cell receptor and/or postreceptor level.
肽Gly-His-Gly在体外对人中性粒细胞具有趋化作用,在体内对兔中性粒细胞具有趋化作用,但在亚溶细胞浓度下不能诱导人中性粒细胞释放溶酶体酶。这种趋化肽未能引发溶酶体酶释放,这表明与趋化受体的相互作用不一定会激活人中性粒细胞的趋化作用和胞吐作用,因此提示胞吐作用和趋化作用的假定共同途径可能在细胞受体和/或受体后水平上存在分歧。