用小角中子散射研究神经酰胺对脂质结构域稳定性的影响:酰基链长和不饱和的作用

IF 3.4 3区 生物学 Q2 BIOCHEMISTRY & MOLECULAR BIOLOGY
Mitchell DiPasquale , Tye G. Deering , Dhimant Desai , Arun K. Sharma , Shantu Amin , Todd E. Fox , Mark Kester , John Katsaras , Drew Marquardt , Frederick A. Heberle
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引用次数: 5

摘要

神经酰胺和二酰基甘油是一类能够成核和稳定有序脂质结构域的脂质,这些结构与一系列生物过程有关。以往的研究利用荧光报告分子探索神经酰胺酰基链结构对富鞘脂有序相的影响。在这里,我们使用小角中子散射(SANS)来研究神经酰胺和二酰基甘油促进结构域形成的能力,这些结构域形成的结构域混合物DPPC/DOPC/胆固醇。SANS是一种强大的、无探针的技术,用于询问膜的非均质性,因为它对氢的稳定同位素质子和氘有不同的敏感性。具体来说,中子对比是通过脂质的选择性氘化产生的,从而能够检测分散在质子化不饱和脂质的基质中富集的氘化饱和脂质的纳米级结构域。使用大的单层囊泡,我们发现用C16:0或C18:0神经酰胺或16:0二酰基甘油(dag)取代10 mol%的DPPC后,脂质结构域持续到更高的温度。然而,当DPPC被短链(C6:0或C12:0)或超长链(C24:0)神经酰胺,或具有任何长度的不饱和酰基链的神经酰胺(C6:1(3), C6:1(5), C18:1和C24:1)以及C18:1- day取代时,脂质结构域被破坏,在比DPPC/DOPC/胆固醇系统更低的温度下熔化。这些结果显示了神经酰胺酰基链长度和不饱和如何影响脂质结构域,并暗示了细胞膜如何通过产生不同的神经酰胺物种来改变其功能。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

Influence of ceramide on lipid domain stability studied with small-angle neutron scattering: The role of acyl chain length and unsaturation

Influence of ceramide on lipid domain stability studied with small-angle neutron scattering: The role of acyl chain length and unsaturation

Influence of ceramide on lipid domain stability studied with small-angle neutron scattering: The role of acyl chain length and unsaturation

Ceramides and diacylglycerols are groups of lipids capable of nucleating and stabilizing ordered lipid domains, structures that have been implicated in a range of biological processes. Previous studies have used fluorescence reporter molecules to explore the influence of ceramide acyl chain structure on sphingolipid-rich ordered phases. Here, we use small-angle neutron scattering (SANS) to examine the ability of ceramides and diacylglycerols to promote lipid domain formation in the well-characterized domain-forming mixture DPPC/DOPC/cholesterol. SANS is a powerful, probe-free technique for interrogating membrane heterogeneity, as it is differentially sensitive to hydrogen’s stable isotopes protium and deuterium. Specifically, neutron contrast is generated through selective deuteration of lipid species, thus enabling the detection of nanoscopic domains enriched in deuterated saturated lipids dispersed in a matrix of protiated unsaturated lipids. Using large unilamellar vesicles, we found that upon replacing 10 mol% DPPC with either C16:0 or C18:0 ceramide, or 16:0 diacylglycerol (dag), lipid domains persisted to higher temperatures. However, when DPPC was replaced with short chain (C6:0 or C12:0) or very long chain (C24:0) ceramides, or ceramides with unsaturated acyl chains of any length (C6:1(3), C6:1(5), C18:1, and C24:1), as well as C18:1-dag, lipid domains were destabilized, melting at lower temperatures than those in the DPPC/DOPC/cholesterol system. These results show how ceramide acyl chain length and unsaturation influence lipid domains and have implications for how cell membranes might modify their function through the generation of different ceramide species.

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来源期刊
Chemistry and Physics of Lipids
Chemistry and Physics of Lipids 生物-生化与分子生物学
CiteScore
7.60
自引率
2.90%
发文量
50
审稿时长
40 days
期刊介绍: Chemistry and Physics of Lipids publishes research papers and review articles on chemical and physical aspects of lipids with primary emphasis on the relationship of these properties to biological functions and to biomedical applications. Accordingly, the journal covers: advances in synthetic and analytical lipid methodology; mass-spectrometry of lipids; chemical and physical characterisation of isolated structures; thermodynamics, phase behaviour, topology and dynamics of lipid assemblies; physicochemical studies into lipid-lipid and lipid-protein interactions in lipoproteins and in natural and model membranes; movement of lipids within, across and between membranes; intracellular lipid transfer; structure-function relationships and the nature of lipid-derived second messengers; chemical, physical and functional alterations of lipids induced by free radicals; enzymatic and non-enzymatic mechanisms of lipid peroxidation in cells, tissues, biofluids; oxidative lipidomics; and the role of lipids in the regulation of membrane-dependent biological processes.
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