Human parotid secretory protein is a lipopolysaccharide-binding protein: identification of an anti-inflammatory peptide domain.

Human parotid secretory protein is a lipopolysaccharide-binding protein: identification of an anti-inflammatory peptide domain.
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DOI:
10.1007/s11010-011-0991-2
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发表时间:
2012-01
影响因子:
4.3
通讯作者:
Gorr, Sven-Ulrik
Gorr, Sven-Ulrik
中科院分区:
生物学3区
文献类型:
--
作者:
Abdolhosseini, Mahsa;Sotsky, Julie B.;Shelar, Anuradha P.;Joyce, Paul B. M.;Gorr, Sven-Ulrik

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腮腺分泌蛋白(Parotid Secretory Protein,PSP)(C20 orf 70)是一种功能未知的唾液蛋白。该蛋白属于粘膜分泌蛋白的腭、肺和鼻上皮克隆(PLC-E)家族,其被预测为在结构上类似于脂质结合和宿主防御蛋白,包括杀菌/渗透性增加蛋白和脂多糖结合蛋白。然而,PLC 1蛋白表现出显着的序列变异和不同的生物学功能已被提出为不同的家庭成员。本研究测试了PSP与急性时相蛋白脂多糖结合蛋白(LBP)的相似性的功能意义。PSP在人唾液中被鉴定出,并且可溶于75%乙醇,如其他磷脂酶A蛋白所示。PSP结合脂多糖,可被非离子去污剂洗脱,但不能被尿素或高盐洗脱。合成的PSP肽GL 13 NH 2,其对应于来自LBP的脂多糖抑制肽,抑制脂多糖与PSP和脂多糖结合蛋白的结合。PSP的其他区域的肽和对照肽多粘菌素B对PSP与脂多糖的结合没有影响。GL 13 NH 2还抑制脂多糖刺激的巨噬细胞分泌肿瘤坏死因子。其他PSP肽在该测定中没有影响。PSP肽对巨噬细胞活力没有影响或只有很小的影响。这些结果表明,PSP是一种脂多糖结合蛋白,在功能上与LBP相关,正如它们预测的结构相似性所表明的那样。
Parotid Secretory Protein (PSP) (C20orf70) is a salivary protein of unknown function. The protein belongs to the palate, lung and nasal epithelium clone (PLUNC) family of mucosal secretory proteins that are predicted to be structurally similar to lipid-binding and host defense proteins including bactericidal/permeability-increasing protein and lipopolysaccharide-binding protein. However, the PLUNC proteins exhibit significant sequence variation and different biological functions have been proposed for different family members. This study tested the functional implications of the proposed similarity of PSP to the acute phase protein Lipopolysaccharide-Binding Protein (LBP). PSP was identified in human saliva and was soluble in 75% ethanol, as shown for other PLUNC proteins. PSP binds lipopolysaccharide and can be eluted by non-ionic detergent, but not by urea or high salt. A synthetic PSP peptide, GL13NH2, which corresponds to a lipopolysaccharide-inhibiting peptide from LBP, inhibited the binding of lipopolysaccharide to both PSP and lipopolysaccharide-binding protein. Peptides from other regions of PSP and the control peptide polymyxin B showed no effect on the binding of PSP to lipopolysaccharide. GL13NH2 also inhibited lipopolysaccharide-stimulated secretion of tumor necrosis factor from macrophages. The other PSP peptides had no effect in this assay. PSP peptides had no or only minor effect on macrophage cell viability. These results indicate that PSP is a lipopolysaccharide-binding protein that is functionally related to LBP, as suggested by their predicted structural similarities.
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期刊: SCIENCE
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