Amyloid- and FDG-PET in sporadic Creutzfeldt-Jakob disease: Correlation with pathological prion protein in neuropathology. Issue 3 (4th May 2017)
- Record Type:
- Journal Article
- Title:
- Amyloid- and FDG-PET in sporadic Creutzfeldt-Jakob disease: Correlation with pathological prion protein in neuropathology. Issue 3 (4th May 2017)
- Main Title:
- Amyloid- and FDG-PET in sporadic Creutzfeldt-Jakob disease: Correlation with pathological prion protein in neuropathology
- Authors:
- Matías-Guiu, Jordi A.
Guerrero-Márquez, Carmen
Cabrera-Martín, María Nieves
Gómez-Pinedo, Ulises
Romeral, María
Mayo, Diego
Porta-Etessam, Jesús
Moreno-Ramos, Teresa
Carreras, José Luis
Matías-Guiu, Jorge - Abstract:
- ABSTRACT: Introduction. The role of positron emission tomography (PET) in Creutzfeldt-Jakob disease is less defined than in other neurodegenerative diseases. We studied the correlation between the uptake of 18 F-florbetaben and 18 F-fluorodeoxyglucose with pathological prion protein deposition in histopathology in a case.Methods. A patient with 80 y old with a rapid neurological deterioration with a confirmed diagnosis of CJD was studied. PET and MRI studies were performed between 13–20 d before the death. A region of interest analysis was performed using Statistical Parametric Mapping.Results. MRI showed atrophy with no other alterations. FDG-PET showed extensive areas of hypometabolism including left frontoparietal lobes as well as bilateral thalamus. Correlation between uptake of 18 F-florbetaben and pathological prion protein deposition was r = 0.786 (p < 0.05). Otherwise, correlation between uptake of 18 F-FDG and pathological prion protein was r = 0.357 (p = 0.385). Immunohistochemistry with β-amyloid did not show amyloid deposition or neuritic plaques.Conclusions. Our study supports the use of FDG-PET in the assessment of CJD. FDG-PET may be especially useful in cases of suspected CJD and negative MRI. Furthermore, this case report provides more evidence about the behavioral of amyloid tracers, and the possibility of a low-affinity binding to other non-amyloid proteins, such as the pathological prion protein, is discussed.
- Is Part Of:
- Prion. Volume 11:Issue 3(2017)
- Journal:
- Prion
- Issue:
- Volume 11:Issue 3(2017)
- Issue Display:
- Volume 11, Issue 3 (2017)
- Year:
- 2017
- Volume:
- 11
- Issue:
- 3
- Issue Sort Value:
- 2017-0011-0003-0000
- Page Start:
- 205
- Page End:
- 213
- Publication Date:
- 2017-05-04
- Subjects:
- amyloid -- Creutzfeldt-Jakob disease -- fluorodeoxyglucose -- positron emission tomography -- prion diseases -- prion protein -- magnetic resonance imaging
Protein folding -- Periodicals
Prions -- Periodicals
Proteins -- Biotechnology -- Periodicals
572.633 - Journal URLs:
- http://www.tandfonline.com/ ↗
http://www.tandfonline.com/toc/kprn20/current ↗ - DOI:
- 10.1080/19336896.2017.1314427 ↗
- Languages:
- English
- ISSNs:
- 1933-6896
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 6615.410000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 1057.xml