Related Experiment Videos
Coated-platelets retain amyloid precursor protein on their surface
Calin I Prodan1, Robert Szasz, Andrea S Vincent
1Department of Neurology, University of Oklahoma Health Sciences Center, klahoma City, Oklahoma 73104, USA.
Platelets
|November 26, 2005
Summary
Coated-platelets retain full-length amyloid precursor protein (APP), unlike single-agonist activated platelets. Early Alzheimer's disease patients show higher coated-platelet levels, suggesting a role in aberrant APP processing.
Area of Science:
- Hematology
- Neuroscience
- Biochemistry
Background:
- Coated-platelets are activated platelets that retain surface proteins.
- Platelet activation influences amyloid precursor protein (APP) processing.
- Aberrant APP processing is implicated in Alzheimer's disease (AD).
Purpose of the Study:
- To investigate APP retention on coated-platelets.
- To compare coated-platelet production in Alzheimer's disease patients and controls.
Main Methods:
- Dual-agonist (collagen plus thrombin) activation of platelets to form coated-platelets.
- Western blot analysis to detect APP derivatization.
- Quantification of coated-platelet levels in AD patients and aged controls.
Main Results:
- Coated-platelets retain full-length APP on their surface, unlike single-agonist activated platelets.
- APP undergoes derivatization during coated-platelet synthesis.
- Least impaired AD patients exhibited significantly higher coated-platelet production compared to aged controls.
Conclusions:
- Coated-platelets represent a novel form of APP processing.
- Elevated coated-platelet levels in early AD suggest a potential role in the disease's pathology.
- Coated-platelets may serve as a biomarker or model for aberrant APP processing in AD.