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month download article/chapter apo ai/abca1-dependent perfringolysin o-based probes hdl3-mediated lipid efflux sphingolipid/cholesterol membrane domains detergent-resistant membrane complexes related subjects beta-cyclodextrin modulates lipid rafts-protein association raft-mediated trafficking detergent-resistant membranes prominin-1/cd133 splice variants distinct membrane domains post-golgi apical targeting basolateral plasma membranes cholesterol-dependent manner cholesterol-dependent binding full article pdf human hematopoietic stem cholesterol-binding protein prominin-1 carbohydrate-mediated golgi distinct lipid microdomains raft lipid depletion tissue research aims privacy choices/manage cookies plasma membrane cholesterol adult human kidney pentaspan membrane glycoprotein pentaspan membrane glycoproteins small membrane particles purified stem cells plasma membrane architecture cholesterol-binding protein anne-marie marzesco support hepatic regeneration atypical membrane microdomains detergent-insoluble complexes plasma membrane protrusions michaela wilsch-braeuninger neural stem cells article cell lipid rafts mediate apical plasma membrane epithelial cell model study membrane rafts article florek cell signaling pathways molecular cell biology polarized hepatic cells fargeas ca

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• Rodriguez-Boulan E, Gonzalez A (1999) Glycans in post-Golgi apical targeting: sorting signals or structural props?

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         headline:Prominin-2 is a cholesterol-binding protein associated with apical and basolateral plasmalemmal protrusions in polarized epithelial cells and released into urine
         description:Prominin-2 is a pentaspan membrane glycoprotein structurally related to the cholesterol-binding protein prominin-1, which is expressed in epithelial and non-epithelial cells. Although prominin-1 expression is widespread throughout the organism, the loss of its function solely causes retinal degeneration. The finding that prominin-2 appears to be restricted to epithelial cells, such as those found in kidney tubules, raises the possibility that prominin-2 functionally substitutes prominin-1 in tissues other than the retina and provokes a search for a definition of its morphological and biochemical characteristics. Here, we have investigated, by using MDCK cells as an epithelial cell model, whether prominin-2 shares the biochemical and morphological properties of prominin-1. Interestingly, we have found that, whereas prominin-2 is not restricted to the apical domain like prominin-1 but is distributed in a non-polarized fashion between the apical and basolateral plasma membranes, it retains the main feature of prominin-1, i.e. its selective concentration in plasmalemmal protrusions; prominin-2 is confined to microvilli, cilia and other acetylated tubulin-positive protruding structures. Similar to prominin-1, prominin-2 is partly associated with detergent-resistant membranes in a cholesterol-dependent manner, suggesting its incorporation into membrane microdomains, and binds directly to plasma membrane cholesterol. Finally, prominin-2 is also associated with small membrane particles that are released into the culture media and found in a physiological fluid, i.e. urine. Together, these data show that all the characteristics of prominin-1 are shared by prominin-2, which is in agreement with a possible redundancy in their role as potential organizers of plasma membrane protrusions.
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      headline:Prominin-2 is a cholesterol-binding protein associated with apical and basolateral plasmalemmal protrusions in polarized epithelial cells and released into urine
      description:Prominin-2 is a pentaspan membrane glycoprotein structurally related to the cholesterol-binding protein prominin-1, which is expressed in epithelial and non-epithelial cells. Although prominin-1 expression is widespread throughout the organism, the loss of its function solely causes retinal degeneration. The finding that prominin-2 appears to be restricted to epithelial cells, such as those found in kidney tubules, raises the possibility that prominin-2 functionally substitutes prominin-1 in tissues other than the retina and provokes a search for a definition of its morphological and biochemical characteristics. Here, we have investigated, by using MDCK cells as an epithelial cell model, whether prominin-2 shares the biochemical and morphological properties of prominin-1. Interestingly, we have found that, whereas prominin-2 is not restricted to the apical domain like prominin-1 but is distributed in a non-polarized fashion between the apical and basolateral plasma membranes, it retains the main feature of prominin-1, i.e. its selective concentration in plasmalemmal protrusions; prominin-2 is confined to microvilli, cilia and other acetylated tubulin-positive protruding structures. Similar to prominin-1, prominin-2 is partly associated with detergent-resistant membranes in a cholesterol-dependent manner, suggesting its incorporation into membrane microdomains, and binds directly to plasma membrane cholesterol. Finally, prominin-2 is also associated with small membrane particles that are released into the culture media and found in a physiological fluid, i.e. urine. Together, these data show that all the characteristics of prominin-1 are shared by prominin-2, which is in agreement with a possible redundancy in their role as potential organizers of plasma membrane protrusions.
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         Lipid raft
         Microvillus
         Prominosome
         MDCK cells
         Mouse (C57B16)
         Human Genetics
         Proteomics
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