Goetzl E J, Rothenberg J, Weber E L, Sinn C M, Austen K F
Clin Exp Immunol. 1980 May;40(2):249-55.
An eosinophil chemotactic activity was identified in extracts of tumour tissue and cerebrospinal fluid from a patient with a histiocytic lymphoma of the brain and spinal cord that was infiltrated extensively with eosinophils and associated with peripheral blood eosinophilia. The histiocytic lymphoma-derived eosinophils chemotactic factor, termed ECF-HL, exhibited a mol. wt of 13,000-14,000 by filtration on Sephadex G-50, was highly acidic based on its elution from a high pressure anion exchange column at pH 2 x 3 - 2 x 1, and was susceptible to inactivation by proteolytic digestion. ECF-HL was absent from extracts of control human brain tissue, glioblastomas, other lymphomas and a variety of carcinomas that lacked an accumulation of eosinophils. Partially purified ECF-HL had no chemokinetic activity, but rendered eosinophils unresponsive to other chemotactic factors. Thus ECF-HL is structurally and functionally distinct from other recognized peptides that are preferentially chemotactic for eosinophils.
在一名脑和脊髓组织细胞淋巴瘤患者的肿瘤组织及脑脊液提取物中,鉴定出一种嗜酸性粒细胞趋化活性。该患者的脑和脊髓被嗜酸性粒细胞广泛浸润,并伴有外周血嗜酸性粒细胞增多。这种源自组织细胞淋巴瘤的嗜酸性粒细胞趋化因子,称为ECF-HL,经Sephadex G-50柱过滤,其分子量为13,000 - 14,000,基于其在pH 2×3 - 2×1条件下从高压阴离子交换柱上的洗脱情况,它呈强酸性,且易被蛋白水解消化失活。对照人脑组织、胶质母细胞瘤、其他淋巴瘤以及各种缺乏嗜酸性粒细胞聚集的癌组织提取物中均未检测到ECF-HL。部分纯化的ECF-HL没有化学促动活性,但能使嗜酸性粒细胞对其他趋化因子不产生反应。因此,ECF-HL在结构和功能上与其他已知的对嗜酸性粒细胞具有优先趋化作用的肽不同。