Concentrations of amyloid-β protein in cerebrospinal fluid increase with age in patients free from neurodegenerative disease
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Cited by (47)
Comparison between amyloid-PET and CSF amyloid-β biomarkers in a clinical cohort with memory deficits
2019, Clinica Chimica ActaCitation Excerpt :Results of age-dependent changes of Aβ42 concentrations in CSF are somewhat controversial. Several studies reported a linear decrease of CSF Aβ42 with age [44–46] while other studies showed no changes or an increase of Aβ42 [47–50]. However, several factors that might influence Aβ42 findings in CSF have to be taken into account that might explain those diametrical findings as sleep cycle and handling and storage of samples [51,52].
Mechanisms of protein misfolding: Novel therapeutic approaches to protein-misfolding diseases
2016, Journal of Molecular StructureCitation Excerpt :Similarly, the high concentration of Aβ peptide may as well affects AD. This was demonstrated by recent study that showed elevated levels of Aβ in CSF, which may be an index of age-related changes in the processing of the amyloid precursor protein leading to a high risk for AD [42]. Dominant negative mutations are important origins of protein misfolding thereby leading to conformational diseases.
Reduced expression of pain mediators and pain sensitivity in amyloid precursor protein over-expressing CRND8 transgenic mice
2013, NeuroscienceCitation Excerpt :Aβ peptides are well known to be the main component of deposits on plaques and tangles found in the brains of patients with Alzheimer’s disease (AD) and are thus involved in the pathogenesis of this disease (Roher et al., 1993). High levels of Aβ peptides were also detected in the cerebrospinal fluid of normal elderly subjects in addition to AD patients (van Gool et al., 1994). It has been shown that APP and its cleaved product Aβ peptides were expressed in small-sized dorsal root ganglion (DRG) neurons in rodents (Kawarabayashi et al., 1991; Sisodia et al., 1993) and humans (Naves et al., 1994), and involved in the survival and axonal growth of DRG neurons during development (Nishimura et al., 2003).
Large quantities of Aβ peptide are constitutively released during amyloid precursor protein metabolism in vivo and in vitro
2011, Journal of Biological ChemistryCitation Excerpt :Alternatively, cleavage of APP by α-secretase occurs within the Aβ domain, precluding the formation of Aβ and resulting in the secretion of sAPPα, a short peptide called p3, and a C-terminal domain, none of which are amyloidogenic. Both in vitro and in vivo evidence suggests that Aβ is secreted from cells under normal physiological conditions (3, 4, 7–9) but the absolute amount, an important consideration given its proposed roles and pharmacologic interest, has not been precisely calculated. In addition, the relative amount of intracellular versus extracellular Aβ production and its ultimate disposition in neurons is unclear (10).
CSF biomarker levels in early and late onset Alzheimer's disease
2009, Neurobiology of AgingCitation Excerpt :This overlap stresses the need for clinical follow-up of controls in future studies on common neurodegenerative diseases. Former studies describing CSF biomarker levels in healthy individuals found conflicting results (Green et al., 1999; Sjogren et al., 2001; van Gool et al., 1994). In a study with 231 healthy individuals, Sjogren et al. (2001) found CSF tau but not Aβ1–42 to be age dependent.
Site-specific effects of peptide lipidation on β-amyloid aggregation and cytotoxicity
2007, Journal of Biological Chemistry