Acyl chain order and lateral domain formation in mixed phosphatidylcholine--sphingomyelin multilamellar and unilamellar vesicles.
Acyl chain order and lateral domain formation in mixed phosphatidylcholine--sphingomyelin multilamellar and unilamellar vesicles.
复制标题
混合磷脂酰胆碱-鞘磷脂多层和单层囊泡中的酰基链顺序和侧向结构域形成。
DOI:
10.1021/bi00527a010
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发表时间:
1981
期刊:
影响因子:
2.9
通讯作者:
Barenholz,Y
中科院分区:
文献类型:
--
作者:
Lentz,BR;Hoechli,M;Barenholz,Y
Barry R. Lentz,* Mathias Hoechli, and Yecheskael Barenholz abstract: The phase behavior of mixtures of dimyristoyl-phosphatidylcholine (DMPC) with V-palmitoylsphingosinephosphorylcholine (Ci6SPH) has been investigated in both small unilamellar and large multilamellar vesicles. The steady-state fluorescence polarization of 1, 6-diphenyl-1, 3, 5-hexatriene (DPH) has been used to detecttemperature-induced structural changes in these membranes. In addition, electron microscopy has revealed vastly different fracture-face mor-phologies for large multilamellar vesicles “jet-frozen” from different temperatures. These data have been iriterpreted in terms of proposed phase diagramsfor this lipid mixture. The shapes of the proposed phase diagrams have led us to conclude that phosphatidylcholine and sphingomyelin species of similar acyl chain length mix freely in both highly curved and un-curved bilayers, except at temperatures at which both lipids are in low-temperature, ordered phases. In addition, the similarity of these phase diagramsto phase diagrams for analogous mixtures of pure phosphatidylcholines suggested that sphingomyelin and phosphatidylcholine species might sub-stitute for each other in supporting the lamellar phase nec-essary to cell membrane structure. Finally, the anisotropy of DPH fluorescence was found to be essentially invariantwith sphingomyelin content at temperatures just above and below the solid-liquid phase separation in small unilamellar vesicles. This demonstrates that the sphingomyelin backbone, per se, does not order the membrane bilayer. These results are dis-cussed in terms of the possible role of sphingomyelin in con-trolling acyl chain order withiri mammaliancell membranes. e phase behavior of many of the component phospholipids of mammalian membranes has been studied extensively in f From theDepartments of Biochemistry (BRL) and Anatomy (MH), University of NorthCarolina at Chapel Hill, Chapel Hill, North Carolina 27514, and the Department of Biochemistry (YB), The He-brew University, Hadassah Medical School, Jerusalem, Israel. Received May 5, 1981. This investigation was supported by grants from the National Science Foundation (PCM 76-16761 and PCM 79-22733), the US Public Health Service (HL17576), and the US-Israel Binational Science Foundation (1688). BRL is a recipient of an Established Investigator award from the American Heart Association with funds contributed in part by the North Carolina Heart Association. A pre-liminary account of this work was presented at the 1981 meeting of the Biophysical Society in Denver, CO. recent years with a view toward defining the role of different phospholipid species in establishing membrane structure. While the ability of some species to form nonlamellar phases may be important tospecialized membrane functions (Cullis& DeKruijff, 1979), those species that spontaneously form lamellar mesomorphic phases in water should stabilize the essential bilayer structure of cell membranes. The choline phosphatides phosphatidylcholine and sphingomyelin are major components of mammalian membranes that form lamellar phases in excess water. Changes in the ratio of these two lipids have been correlated with the occurrence of various tissue malfunctions (Barenholz & Thompson, 1980) such as aging (Rouser & Solomon, 1969), atherosclerosis (Small & Shipley,