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Sequence specificity and transcriptional activation in the binding of lactoferrin to DNA.

机译:乳铁蛋白与DNA结合时的序列特异性和转录激活。

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Lactoferrin, an iron-binding glycoprotein found in high concentrations in human milk and other epithelial secretions and in the secondary (specific) granules of neutrophils, is thought to be responsible for primary defence against microbial infection, mainly as a result of lactoferrin sequestration of iron required for microbial growth. Many other functions have been attributed to lactoferrin, including immunomodulation and cell growth regulation (reviewed in ref. 4). Some of these functions appear to be at least in part independent of the iron-binding activity of lactoferrin. It also has been consistently observed that lactoferrin interacts avidly with nucleic acids. Lactoferrin enhancement of the activity of natural killer and lymphokine-activated killer cells in vitro is inhibited by RNA and DNA. Lactoferrin taken up by K562 human myelogenous leukaemia cells appears in the nucleus where it is bound to DNA. We report here that binding of lactoferrin to DNA occurs under stringent conditions with distinct sequence specificity, and that interaction between lactoferrin and these sequences intracellularly leads to transcriptional activation.
机译:乳铁蛋白是一种铁结合糖蛋白,存在于人乳和其他上皮分泌物中以及嗜中性粒细胞的次级(特定)颗粒中,浓度很高,被认为是抵抗微生物感染的主要防御手段,主要是由于乳铁蛋白螯合了铁微生物生长所必需的。乳铁蛋白还有许多其他功能,包括免疫调节和细胞生长调节(参见参考文献4)。这些功能中的一些似乎至少部分独立于乳铁蛋白的铁结合活性。还一直观察到乳铁蛋白与核酸紧密地相互作用。乳铁蛋白增强天然杀伤细胞和淋巴因子激活的杀伤细胞在体外的活性被RNA和DNA抑制。 K562人骨髓性白血病细胞吸收的乳铁蛋白出现在与DNA结合的细胞核中。我们在这里报告,乳铁蛋白与DNA的结合发生在具有不同序列特异性的严格条件下,并且乳铁蛋白与这些细胞内序列之间的相互作用导致转录激活。

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