BEGIN:VCALENDAR
VERSION:2.0
PRODID:-//Talks.cam//talks.cam.ac.uk//
X-WR-CALNAME:Talks.cam
BEGIN:VEVENT
SUMMARY:Redox-dependent modulation of haemostasis and vascular function by
  amyloid peptide beta: a new interpretation of the vascular component of d
 ementia. - Dr Giordano Pula\, University of Exeter Medical School
DTSTART:20171011T093000Z
DTEND:20171011T103000Z
UID:TALK89211@talks.cam.ac.uk
CONTACT:Patrick Flagmeier
DESCRIPTION:Alzheimer's disease (AD) is the most common neurodegenerative 
 cause of dementia in the elderly. AD is accompanied by the accumulation of
  amyloid peptides in the brain parenchyma and in the cerebral vessels. The
  sporadic form of AD accounts for about 95% of all cases. It is characteri
 zed by a late onset\, typically after the age of 65\, with a complex and s
 till poorly understood aetiology. Several observations point towards a cen
 tral role of cerebrovascular dysfunction in the onset of sporadic AD (SAD)
 . According to the "vascular hypothesis"\, AD may be initiated by vascular
  dysfunctions that precede and promote the neurodegenerative process. In a
 ccordance to this\, AD patients show increased stroke risk. It is now clea
 r that multiple bidirectional connections exist between AD and cerebrovasc
 ular disease\, and in this new scenario\, the effect of amyloid peptides o
 n vascular cells and blood platelets appears to be central to AD.\nReactiv
 e oxygen species (ROS) generation is critical in the regulation of platele
 ts\, which has important implications in the modulation of haemostasis and
  thrombosis. Interestingly\, amyloid β (Aβ) 1-42 peptide stimulated supe
 roxide anion formation in a concentration-dependent manner. Aβ peptide st
 imulated superoxide anion formation in a NOX-dependent manner\, as proved 
 by the use of VAS2870. Aβ 1-42 peptide displayed only moderate activity a
 s an aggregation stimulus\, but was able to significantly potentiate plate
 let aggregation in response to submaximal agonist concentrations\, such as
  0.03 unit/ml thrombin and 10 μM arachidonic acid. The inhibition of NOXs
  by 10 μM VAS2870 abolished Aβ-dependent potentiation of platelet aggreg
 ation in response to 10 μM arachidonic acid\, suggesting that the pro-thr
 ombotic activity of Aβ peptides depends on NOX activity. These finding sh
 ed some new light on the pro-thrombotic activity of Aβ peptides.\n
LOCATION:Department of Chemistry\, Cambridge\, Unilever lecture theatre
END:VEVENT
END:VCALENDAR