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首页> 外文期刊>Biochemistry >The acute phase protein haptoglobin is a mammalian extracellular chaperone with an action similar to clusterin
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The acute phase protein haptoglobin is a mammalian extracellular chaperone with an action similar to clusterin

机译：急性期蛋白触珠蛋白是一种哺乳动物细胞外伴侣，其作用类似于簇蛋白

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Haptoglobin (Hp) is an acidic glycoprotein present in most body fluids of humans and other mammals. Although the functions of Hp are not yet fully understood, the available evidence indicates that it is likely to play an important role in suppressing inflammatory responses. Some earlier work suggested that Hp might be a newly identified member of a small group of extracellular chaperones found at significant levels in human body fluids. Previously, the only well-characterized member of this group was clusterin, which shares functional similarities with the small heat-shock proteins. We report here that Hp specifically inhibited the precipitation of a variety of proteins induced by either heat or oxidation, including proteins in unfractionated human serum. We also show that, like clusterin, Hp (i) inhibits the precipitation of stressed proteins by forming solubilized high molecular weight complexes with them, (ii) cannot protect enzymes from heat-induced loss of function, and (iii) lacks ATPase activity and the ability to independently refold proteins following stresses. Furthermore, we show that Hp has maximum chaperone activity at mildly alkaline pH and, unlike clusterin, does not undergo significant changes in oligomerization state coincident with pH-induced changes in chaperone activity. Our results raise the possibility that Hp may exert an anti-inflammatory action in vivo by inhibiting the inappropriate self-association of "damaged" (misfolded) extracellular proteins.
机译：肝珠蛋白（Hp）是一种酸性糖蛋白，存在于人类和其他哺乳动物的大多数体液中。尽管尚未完全了解Hp的功能，但现有证据表明Hp可能在抑制炎症反应中起重要作用。一些较早的研究表明，Hp可能是在人体液中大量发现的一小部分细胞外伴侣的新发现成员。以前，该组中唯一被充分表征的成员是Clusterin，它与小的热激蛋白具有功能相似性。我们在这里报告说，Hp特异地抑制了由热或氧化诱导的多种蛋白质的沉淀，包括普通人血清中的蛋白质。我们还显示，与簇蛋白一样，Hp（i）通过与它们形成可溶的高分子量复合物来抑制应激蛋白的沉淀，（ii）无法保护酶免受热诱导的功能丧失，并且（iii）缺乏ATPase活性和压力后独立重折叠蛋白质的能力。此外，我们显示Hp在温和的碱性pH值下具有最大的分子伴侣活性，并且与clusterin不同，在伴随IP诱导的分子伴侣活性变化的同时，寡聚状态不会发生显着变化。我们的结果提出了Hp可能通过抑制“受损”（错折叠）的细胞外蛋白的不适当的自缔合而在体内发挥抗炎作用的可能性。

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