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宿主尿激酶型纤溶酶原激活剂参与疟原虫裂殖子从受感染红细胞的释放。

Host urokinase-type plasminogen activator participates in the release of malaria merozoites from infected erythrocytes.

作者信息

Roggwiller E, Fricaud A C, Blisnick T, Braun-Breton C

机构信息

Experimental Parasitology, URA CNRS 146, Institut Pasteur, Paris, France.

出版信息

Mol Biochem Parasitol. 1997 May;86(1):49-59. doi: 10.1016/s0166-6851(97)02848-x.

Abstract

Malaria infection of red blood cells is associated with plasminogen activation. Surface immunofluorescence and immunoprecipitation experiments, using specific polyclonal and monoclonal antibodies raised against human urokinase, demonstrate that this activity is due to the binding of host urokinase-type plasminogen activator to the surface of erythrocytes infected by mature forms of Plasmodium falciparum malaria parasites. Depletion of urokinase from the culture medium leads to the inhibition of merozoite release and the accumulation of segmenter-infected erythrocytes; this inhibition is reversed by the addition of human single-chain or two-chain urokinase. These findings are consistent with host urokinase being involved in the process of merozoite release from the red blood cell.

摘要

红细胞的疟疾感染与纤溶酶原激活有关。使用针对人尿激酶产生的特异性多克隆和单克隆抗体进行的表面免疫荧光和免疫沉淀实验表明,这种活性是由于宿主尿激酶型纤溶酶原激活剂与被恶性疟原虫成熟形式感染的红细胞表面结合所致。从培养基中去除尿激酶会导致裂殖子释放受到抑制以及被裂殖体感染的红细胞积累;添加人单链或双链尿激酶可逆转这种抑制作用。这些发现与宿主尿激酶参与裂殖子从红细胞释放的过程一致。

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