Causes of nondiffusing lipid in the plasma membrane of mammalian spermatozoa

Wolf, David E.; Lipscomb, Adrienne C.; Maynard, Valerie M.

doi:10.1021/bi00403a004

Cited by 51 publications

(35 citation statements)

References 39 publications

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“…liquid states [76,78]. In this respect, most of the non-diffusing fraction which was observed in the plasma membrane of spermatozoa [46-481 was retained in lipid bilayers prepared from lipids extracted from these membranes [83]. As another possibility, lipid microdomains might originate from a protein lattice trapping lipid molecules and acting like a fence preventing lipids from laterally diffusing [13,44,80].…”

Section: Lipid Microdomains In Membranesmentioning

confidence: 99%

Lipid lateral diffusion and membrane organization

et al. 1989

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It is shown that investigating the lateral motion of lipids in biological membranes can provide useful information on membrane lateral organization.After labeling membranes with extrinsic or intriinsic lipophihc fluorescent probes, fluorescence recovery aRer photobleaching experiments strongly suggests that specialized cells like spermatozoa, eggs and epithelia exhibit surface membrane regionalization or macrocompartmentation and that lateral microheterogeneities or lipid microdomains exist in the plasma membrane of many cellular systems.

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Section: Lipid Microdomains In Membranesmentioning

confidence: 99%

Lipid lateral diffusion and membrane organization

et al. 1989

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“…Instead, their presence is inferred from the behavior of membrane probes that is not predicted by, or consistent with, the properties of a continuous, fluid, lipid bilayer. Such domains then are defined by the experiments that detect them, for example in terms of heterogeneities of fluorescence lifetimes (Klausner et al, 1980;Karnovsky et al, 1982) or of lateral diffusion coefficients (Wolf et al, 1981;Handyside et al, 1982;Wolf et al, 1988).…”

mentioning

confidence: 99%

Differences between the lateral organization of conventional and inositol phospholipid-anchored membrane proteins. A further definition of micrometer scale membrane domains.

Edidin

Stroynowski

1991

The Journal of Cell Biology

123

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Abstract. Plasma membranes of many cells appear to be divided into domains, areas whose composition and function differ from the average for an entire membrane. We have previously used fluorescence photobleaching and recovery to demonstrate one type of membrane domain, with dimensions of micrometers (Yechiel, E., and M. Edidin. 1987. J. Cell Biol. 105: 755-760). The presence of membrane domains is inferred from the dependence of the apparent mobile fraction of labeled molecules on the size of the membrane area probed. We now find that by this definition classical class I MHC molecules, H-2D b, are concentrated in domains in the membranes of K78-2 hepatoma cells, while the nonclassical class I-related molecules, Qa-2, are free to pass the boundaries of these domains. The two proteins are highly homologous but differ in their mode of anchorage to the membrane lipid bilayer. H-2D b is anchored by a transmembrane peptide, while Qa-2 is anchored by a glycosylphosphatidylinositol (GPI) anchor. A mutant class I protein with its external portion derived from Qa-2 but with transmembrane and cytoplasmic sequences from a classical class I molecule shows a dependence of its mobile fraction on the area of membrane probed, while a mutant whose external portions are a mixture of classical and nonclassical class I sequences, GPI-linked to the bilayer, does not show this dependence and hence by our definition is not restricted to membrane domains.

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“…Lipid composition, particularly cholesterol/phospholipid ratios, may in fact play a mechanistic role in capacitation and the acrosome reaction (5,6). Unlike lipids in somatic cell plasma membranes, a large fraction of sperm plasma membrane lipid is not free to diffuse (7)(8)(9). When bilayers are reconstituted from organic-phase extracts of ram sperm plasma membrane (lipid from the anterior region of the sperm head), a large fraction of the lipid is immobile.…”

mentioning

confidence: 99%

“…sperm head with minimal acrosomal and mitochondrial contamination (1,9). Lipids were extracted from these vesicles as described (9), by a modification of the technique of Bligh and Dyer (24).…”

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Lipid domains in the ram sperm plasma membrane demonstrated by differential scanning calorimetry.

Wolf

Maynard

McKinnon

et al. 1990

Proc. Natl. Acad. Sci. U.S.A.

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Mammalian sperm plasma membranes, in contrast to those of mammalian somatic cells, exhibit a significant fraction of lipid that does not diffuse laterally in the plane of the membrane. This nondiffusing fraction results from lipid-ipid interactions. Similar nondiffusing fractions are found in mixed-lipid model systems that contain coexistent gel and fluid domains. These results suggest that the sperm plasma membrane may also exhibit lateral phase segregations of lipids and may contain significant amounts of gel-phase lipid. In this paper we use differential scanning calorimetry to show that, in contrast to the plasma membranes of mammalian somatic cells, the plasma membrane from the anterior region of the head of ram sperm exhibits at least two major endothermic transitions, one centered at -260C and one centered at 60°C. The heats of these transitions are consistent with gel-to-fluid transitions in model membranes. These transitions are observed both in plasma membrane vesicles and in rehydrated lipid extracts made from these vesicles. These results demonstrate that at physiological temperatures the lipids of the ram sperm plasma membrane are segregated into coexistent fluid and gel domains.

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Causes of nondiffusing lipid in the plasma membrane of mammalian spermatozoa

Cited by 51 publications

References 39 publications

Lipid lateral diffusion and membrane organization

Lipid lateral diffusion and membrane organization

Differences between the lateral organization of conventional and inositol phospholipid-anchored membrane proteins. A further definition of micrometer scale membrane domains.

Lipid domains in the ram sperm plasma membrane demonstrated by differential scanning calorimetry.

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