期刊
BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS
卷 1861, 期 10, 页码 2494-2506出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbagen.2017.07.012
关键词
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资金
- Japan Society for the Promotion of Science [2311001, 16H01358, 24110505, 26110704]
- Core Research for Evolutional Science and technology (CREST) project Creation of Fundamental Technologies for Understanding and Control of Biosystem Dynamics [24370055, 15H04351, 15H04495, 22380067, 23688014, 16H06386]
- Japan Science and Technology Agency (JST) [888041]
- Naito foundation
- Daiichi-Sankyo foundation
- Mizutani Foundation
- World Premiere Research Center Initiative (WPI) of MEXT
- Grants-in-Aid for Scientific Research [26110704, 16H01358, 24110505, 15H04495, 17K19521, 17H03666] Funding Source: KAKEN
Gangliosides are involved in a variety of biological roles and are a component of lipid rafts found in cell plasma membranes (PMs). Gangliosides are especially abundant in neuronal PMs and are essential to their physiological functions. However, the dynamic behaviors of gangliosides have not been investigated in living cells due to a lack of fluorescent probes that behave like their parental molecules. We have recently developed, using an entirely chemical method, four new ganglioside probes (GM1, GM2, GM3, and GD1b) that act similarly to their parental molecules in terms of raft partitioning and binding affinity. Using single fluorescent-molecule imaging, we have found that ganglioside probes dynamically enter and leave rafts featuring CD59, a GPI-anchored protein. This occurs both before and after stimulation. The residency time of our ganglioside probes in rafts with CD59 oligomers was 48 ms, after stimulation. The residency times in CD59 homodimer and monomer rafts were 40 ms and 12 ms, respectively. In this review, we introduce an entirely chemical-based ganglioside analog synthesis method and describe its application in single-molecule imaging and for the study of the dynamic behavior of gangliosides in cell PMs. Finally, we discuss how raft domains are formed, both before and after receptor engagement. This article is part of a Special Issue entitled Neuro-glycoscience, edited by Kenji Kadomatsu and Hiroshi Kitagawa.
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