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Beta amyloid and Tau proteins (transglutaminase substrates) Osmosis & Neuroscientifically Challenged

FOTGCREN HYPOTHESIS: A tale of bugs and foods: Hwp1 versus gluten and casein (v3)    • A tale of bugs and foods: Hwp1 versus...   GROSSO 2012: https://www.ncbi.nlm.nih.gov/pubmed/2... Alzheimer's disease (AD) is the most common neurodegenerative disorder and is another disease in which Tissue Transglutaminase (TG2) is implicated ( Lesort, et al., 2000). It is marked by neuronal loss throughout the brain including the hippocampus, which manifests as memory deficits and cognitive impairment ( Purves, 2004). Aβ amyloid-containing extracellular Alzheimer plaques and tau-containing intraneuronal neurofibrillary tangles constitute characteristic microscopic features of AD. TRANSGLUTAMINASE: Evidence from in vitro and cell culture studies indicate that TG2 cross-links both AD-related proteins, tau and Aβ amyloid ( Lesort, et al., 2000). Postmortem brain analyses of AD patients have provided evidence for increased expression and activity of TG2 compared to age-matched controls. Evidence for increased TG2 activity in AD is detected by the presence of increased SDS-insoluble GGEL bonds in AD brains ( Kim,et al., 1999). TAU Early biochemical and kinetic studies of tau demonstrated that it is a substrate of TG2, and that TG2 cross-linking of tau makes it more recognizable to an antibody that detects a pathologic conformation of this peptide ( Lesort, et al., 2000). A subsequent study showed that incubation of tau with TG2 in vitro causes the formation of filaments in a calcium-dependent manner ( Appelt & Balin, 1997). Notably, the co-localization of TG2 with tau aggregates in AD brains is consistent with tau being a substrate of TG2 ( Appelt, et al., 1996 ). These data demonstrate a correlation between the presence of TG2 and the pathology of AD. BETA-AMYLOID Aβ peptide of amyloid plaques can also be cross-linked by TG2 (Ikura et al., 1993; Zhang et al., 1998c; Moore et al., 2009) forming trimers, tetramers, and hexamers of synthetic, partial-length Aβ in in vitro studies (Zhang et al., 1998c). Both lysine residues found in full length Aβ peptide are susceptible to TG2-mediated cross-linking and are involved in TG-catalyzed polymerization ( Rasmussen et al.,1994). This cross-linking of Aβ by TG2 can be inhibited by TG2 inhibitors monodansylcadaverine and spermine ( Zhang et al., 1997). TG2 can also cross-link amyloid precursor protein (APP) in the presence of calcium forming dimers and higher order multimers (Ho et al.,1994).