Lipid rafts in epithelial brush borders: atypical membrane microdomains with specialized functions.
Epithelial cells that fulfil high-throughput digestive/absorptive functions, such as small intestinal enterocytes and kidney proximal tubule cells, are endowed with a dense apical brush border. It has long been recognized that the microvillar surface of the brush border is organized in cholesterol/sphingolipid-enriched membrane microdomains commonly known as lipid rafts. More recent studies indicate that microvillar rafts, in particular those of enterocytes, have some unusual properties in comparison with rafts present on the surface of other cell types. Thus, microvillar rafts are stable rather than transient/dynamic, and their core components include glycolipids and the divalent lectin galectin-4, which together can be isolated as "superrafts", i.e., membrane microdomains resisting solubilization with Triton X-100 at physiological temperature. These glycolipid/lectin-based rafts serve as platforms for recruitment of GPI-linked and transmembrane digestive enzymes, most likely as an economizing effort to secure and prolong their digestive capability at the microvillar surface. However, in addition to microvilli, the brush border surface also consists of membrane invaginations between adjacent microvilli, which are the only part of the apical surface sterically accessible for membrane fusion/budding events. Many of these invaginations appear as pleiomorphic, deep apical tubules that extend up to 0.5-1 microm into the underlying terminal web region. Their sensitivity to methyl-beta-cyclodextrin suggests them to contain cholesterol-dependent lipid rafts of a different type from the glycolipid-based rafts at the microvillar surface. The brush border is thus an example of a complex membrane system that harbours at least two different types of lipid raft microdomains, each suited to fulfil specialized functions. This conclusion is in line with an emerging, more varied view of lipid rafts being pluripotent microdomains capable of adapting in size, shape, and content to specific cellular functions.
Danielsen
E Michael
EM
Department of Medical Biochemistry and Genetics, The Panum Institute, University of Copenhagen, Blegdamsvej 3, N DK-2200 Copenhagen, Denmark. midan@imbg.ku.dk
Hansen
Gert H
GH
D004847:Epithelial Cells / Q000378:metabolism* / Q000648:ultrastructure*; D008563:Membrane Lipids / Q000378:metabolism; D021962:Membrane Microdomains / Q000145:classification / Q000378:metabolism* / Q000648:ultrastructure*; D008565:Membrane Proteins / Q000378:metabolism*; D008871:Microvilli / Q000145:classification / Q000378:metabolism* / Q000648:ultrastructure*
D008563:Membrane Lipids; D008565:Membrane Proteins