Hemagglutinin and neuraminidase, which protrude from the outer

surface of the influenza virus, are found to be two glycoproteins associated with lipid rafts of infected cells (Scheiffele et al., 1997). When the virus replicates itself from host cells, it also uses the plasma membrane of its host; this might explain why lipidomics analyses reported that the envelope of influenza virus was mainly made-up of mamalian lipid rafts-related lipids. This suggests that the influenza virus may bud from lipid rafts (Takeda et al., 2003). The see more human immunodeficiency virus envelope is also enriched in lipid rafts-related lipids; thus cell entry and budding of this virus may both depend on lipid rafts (Aloia et al., 1988, Fittipaldi et al., 2003 and Ono and Freed, 2001). Activation of local apoptotic processes in different neurons is physiologically important. Neuron elimination through apoptosis may represent an important process allowing brain plasticity during fetal development and the first JQ1 ic50 years of postnatal life. However, neuronal cell death at the adult stage in human is often associated with diseases. Various changes in the cellular plasma membrane during pathological

neuronal loss have been described. Some types of neurodegeneration can be caused by prions, composed of naturally occurring PrPC protein in a missfolded stage (PrPSc). PrPSc found in infectious material has a different structure than natural occurring PrPC, making it more resistant

to proteases. It has been suggested that lipid rafts may play a role in the conversion of PrPC to PrPSc, which is suggested to be central in the pathogenesis of prion diseases (Campana et al., 2005). The interactions between lipid rafts and Dipeptidyl peptidase PrP localization and trafficking have been recently reviewed (Lewis and Hooper, 2011). Alzheimer’s disease has also been identified as a protein misfolding disease. This disease has been suggested to be caused by accumulation of abnormally folded amyloid-β-peptide (Aβ) and tau proteins in the brain. The “senile” plaques contain Aβ and are linked to loss of neurons. The Aβ-peptide has a size of 4 kDa and is derived from the amyloid precursor protein by sequential enzymatic cleavage by β-secretase and γ-secretase (Mattson, 2004). Alternative proteolytic cleavage of amyloid precursor protein in the middle of the Aβ region by α-secretase precludes the formation of amyloidogenic Aβ (Mattson, 2004). It has been reported that β- and γ-secretases, as well as Aβ, are localized, at least in part, in lipid rafts (Lee et al., 1998, Riddell et al., 2001 and Wada et al., 2003). Considering this point, it is interesting to note that cholesterol depletion has been shown to inhibit β-cleavage and Aβ formation (Simons et al., 1998), while promoting α-cleavage (Kojro et al., 2001).