In another fungal species, Botrytis cinerea, which is a fungus causing losses of commercially important fruits, vegetables and vineyards worldwide, ABC-transporter upregulation was associated with drug resistance due to the use of fungicides. B. cinerea drug resistance is spreading, thus arguing against a fitness cost due to ABC-transporter upregulation. Regarding PUP1, no other homologues were found yet involved in microbial pathogenesis and therefore the exact role of the product encoded by this gene in C. glabrata pathogenesis remains an open question. LOUREIRIN-B cortical neurons and BSMC sensitive to amyloid protein were susceptible to 15d-PGJ2. 15d-PGJ2 bound specifically to the two cells, suggesting that 15d-PGJ2 played an important role in amyloidoses not only in the central nervous system but also in the peripheral tissues. The specific binding sites of 15d-PGJ2 were detected in the neuronal subcellular fractions of nuclear, cytosol and plasma membrane, but not in the Tulathromycin B microsomal fraction. 15dPGJ2 binds to the nuclear receptor, PPARc and the cytosolic protein, Ras. In peripheral tissues including nerves, chemoattractant receptor-homologous molecule expressed on Th2 cells has been identified as a type 2 receptor for PGD2, and reported to be also a membrane receptor for 15d-PGJ2. Contrary to its mRNA, little protein of DP2 has yet been detected in the central nerve. Furthermore, we ruled out the possibility that the specific binding site of 15d-PGJ2 in the plasma membrane of cortical neurons was DP2. First, few binding sites of PGD2 are detected in plasma membranes from rat cortices. Although binding sites of ?12-PGJ2 and PGJ2 are also detected in plasma membranes, those are displaced most potently by 15d-PGJ2 among PGD2 metabolites. Second, a DP2 selective agonist, 15d-PGD2 do not affect the cell number of neuronal cells and BSMC. Enolase 1 and Enolase 2 belong to a superfamily of abundantly expressed carbon-oxygen lyases known for the catalysis of 2phosphoglycerate to phosphoenolpyruvate. Ubiquitous enolase1 and neuron specific enolase 2 exist as monomers and also as dimmers on the neuronal membrane surface. Recent studies have demonstrated that enolases possess different regulatory properties from glycolysis in the brain. Enolase1 is one of the most consistently up-regulated and oxidatively modified proteins in brain of subjects of early-onset AD. Enolase1 and enolase 2 are autoantigen targets in post-streptococcal autoimmune disease of central nervous system. The anti-enolase antibodies induce neuronal apoptosis. Enolase 2 is part of neuronal PMOs, and the anti-enolase2 antibody can inhibit PMO activity on the plasma membrane. Pyruvate kinase transfers a phophate from phosphoenolpyruvate to ADP. Pyruvate kinase is also defined as the autoantigen, and its antibodies induce neuronal apoptosis. The significant increase in pyruvate kinase activity is found in frontal and temporal cortex of AD brains. Pyruvate kinase is elevated in the cortical neurons undergoing Ab-mediated apoptosis. Pyruvate kinase is co-precipitated with fAb. Biotinylated 15dPGJ2 binds to PKM1 in mesangial cells, supporting our results. Tubulin has been identified as a membrane component of synaptosomes and various plasma membranes. Both tubulin a and b have been shown to associate with the amyloid deposits of familial amyloidosis and to bind to the Ab sequence of APP. Moreover, tubulin b is retained by a monomeric Ab column, and co-precipitated with fAb. The tau protein interacts with tubulin to stabilize microtubules and promote tubulin assembly into microtubules. PGJ2 induces caspase-mediated cleavage of tau, generating Dtau, an aggregation prone form known to seed tau aggregation prior to neurofibrillary tangle formation. Hyperphosphorylation of the tau protein can result in the self-assembly of tangles of paired helical filaments and straight filaments, which are involved in the pathogenesis of AD. Biotinylated 15d-PGJ2 binds to tubulin b in mesangial cells, supporting our results.