Inhibitory activity of human lactoferrin and its peptide on chondroitin sulfate A-, CD36-, and thrombospondin-mediated cytoadherence of Plasmodium falciparum-infected erythrocytes
Inhibitory activity of human lactoferrin and its peptide on chondroitin sulfate A-, CD36-, and thrombospondin-mediated cytoadherence of Plasmodium falciparum-infected erythrocytes
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DOI：
10.1182/blood.v94.1.326.413a32_326_332
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发表时间：
1999-07-01
期刊：
影响因子：
20.3
通讯作者：
Sherman, IW
中科院分区：
文献类型：
--
作者：
Eda, S;Eda, K;Sherman, IW
乳铁蛋白 (LF) 是一种人血清蛋白，浓度为 100 μg/mL 时，可强烈抑制恶性疟原虫感染的红细胞 (PE) 与固定化硫酸软骨素 A (CSA) 结合白蛋白的粘附，并阻断 PE 与表达 CD36 的中国仓鼠卵巢 (CHO) 细胞以及浓度为 5 μg/mL 的固定化 CD36 的结合分别为100μg/mL和100μg/mL。生物素化的 LF 以可饱和的方式与 CD36 结合，并且这种结合被未标记的 LF 和抗 CD36 单克隆抗体 8A6 抑制，表明结合的特异性。另外，浓度为100μg/mL的LF抑制PE与固定化血小板反应蛋白(TSP)的结合，并且使用生物素化的LF证实了LF与TSP的特异性结合。 LF 以剂量依赖性方式抑制 PE 与 C32 无黑色素瘤细胞的结合。 LF 肽，Arg-Asn-Met Arg-Lys-Val Arg Gly-Pro-Pro-Val-Ser-Cys（LF 的氨基酸残基 25-37），已被认为有助于 LF 与各种材料（包括 CSA）结合，抑制 PE 与固定化 CSA 结合白蛋白、固定化 CD36、表达 CD36 的 CHO 细胞、固定化 TSP 和 C32无色素性黑色素瘤细胞，以及 LF 本身。这些结果表明，LF 肽可能为开发能够抑制 CSA、CD36 和 TSP 介导的 PE 细胞粘附的药物提供基础。 (C) 1999 年，美国血液学会。
Lactoferrin (LF), a human serum protein, strongly inhibited the adherence of Plasmodium falciparum-infected erythrocytes (PE) to immobilized chondroitin sulfate A (CSA)conjugated albumin at a concentration of 100 mu g/mL and blocked the PE binding to CD36-expressing Chinese hamster ovary (CHO) cells, as well as immobilized CD36 at concentrations of 5 mu g/mL and 100 mu g/mL, respectively. Biotinylated LF bound to CD36 in a saturable manner, and such binding was inhibited by unlabeled LF and the anti-CD36 monoclonal antibody, 8A6, suggesting specificity of binding. Additionally, LF inhibited PE binding to immobilized thrombospondin (TSP) at a concentration of 100 mu g/mL, and specific binding of LF to TSP was confirmed using biotinylated LF. LF inhibited PE binding to C32 amelanotic melanoma cells in a dose-dependent manner. A peptide of LF, Arg-Asn-Met Arg-Lys-Val Arg Gly-Pro-Pro-Val-Ser-Cys (amino acid residues 25-37 of LF), which has been suggested to contribute to LF binding to various materials, including CSA, inhibited PE binding to immobilized CSA conjugated albumin, immobilized CD36, CD36-expressing CHO cells, immobilized TSP, and C32 amelanotic melanoma cells, as well as LF itself. These results suggest that LF peptide may provide the basis for developing agents that are able to inhibit CSA-, CD36-, and TSP-mediated cytoadherence of PE. (C) 1999 by The American Society of Hematology.