期刊
CELLULAR PHYSIOLOGY AND BIOCHEMISTRY
卷 51, 期 4, 页码 1544-1565出版社
KARGER
DOI: 10.1159/000495645
关键词
Fluorescence microscopy; Mechanical stimulation; Piezo1; PMCA; PDMS stretching; Calcium exchanges
资金
- MaxSynBio consortium - Federal Ministry of Education and Research (BMBF) of Germany [FKZ 031A359L]
- MaxSynBio consortium - Max Planck Society (MPG)
- UCLouvain (FSR)
- UCLouvain (Actions de Recherches concertees, ARC)
- F.R.S-FNRS
- Salus Sanguinis foundation
Background/Aims: Red blood cells (RBC) have been shown to exhibit stable submicrometric lipid domains enriched in cholesterol (chol), sphingomyelin (SM), phosphatidylcholine (PC) or ganglioside GM1, which represent the four main lipid classes of their outer plasma membrane leaflet. However, whether those lipid domains co-exist at the RBC surface or are spatially related and whether and how they are subjected to reorganization upon RBC deformation are not known. Methods: Using fluorescence and/or confocal microscopy and well-validated probes, we compared these four lipid-enriched domains for their abundance, curvature association, lipid order, temperature dependence, spatial dissociation and sensitivity to RBC mechanical stimulation. Results: Our data suggest that three populations of lipid domains with decreasing abundance coexist at the RBC surface: (i) chol-enriched ones, associated with RBC high curvature areas; (ii) GM1/PC/chol-enriched ones, present in low curvature areas; and (iii) SM/PC/chol-enriched ones, also found in low curvature areas. Whereas cholenriched domains gather in increased curvature areas upon RBC deformation, low curvatureassociated lipid domains increase in abundance either upon calcium influx during RBC deformation (GM1/PC/chol-enriched domains) or upon secondary calcium efflux during RBC shape restoration (SM/PC/chol-enriched domains). Hence, abrogation of these two domain populations is accompanied by a strong impairment of the intracellular calcium balance. Conclusion: Lipid domains could contribute to calcium influx and efflux by controlling the membrane distribution and/or the activity of the mechano-activated ion channel Piezo1 and the calcium pump PMCA. Whether this results from lipid domain biophysical properties, the strength of their anchorage to the underlying cytoskeleton and/or their correspondence with inner plasma membrane leaflet lipids remains to be demonstrated. (C) 2018 The Author(s) Published by S. Karger AG, Basel
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