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FTIR-microspectroscopy of prion-infected nervous tissue
- Source :
- Biochimica et Biophysica Acta (BBA) - Biomembranes. (7):948-959
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Abstract
- The family of transmissible spongiform encephalopathies (TSE), also termed prion diseases, is a group of fatal, neurodegenerative diseases characterized by the accumulation of a misfolded protein, the disease-associated prion protein PrPSc. This glycoprotein differs in secondary structure from its normal, cellular isoform PrPC, which is physiologically expressed mostly by neurons. Scrapie is a prion disease first described in the 18th century in sheep and goats, and has been established as a model in rodents to study the pathogenesis and pathology of prion diseases. Assuming a multitude of molecular parameters change in the tissue in the course of the disease, FTIR microspectroscopy has been proposed as a valuable new method to study and identify prion-affected tissues due to its ability to detect a variety of changes in molecular structure and composition simultaneously. This paper reviews and discusses results from previous FTIR microspectroscopic studies on nervous tissue of scrapie-infected hamsters in the context of histological and molecular alterations known from conventional pathogenesis studies. In particular, data from studies reporting on disease-specific changes of protein structure characteristics, and also results of a recent study on hamster dorsal root ganglia (DRG) are discussed. These data include an illustration on how the application of a brilliant IR synchrotron light source enables the in situ investigation of localized changes in protein structure and composition in nervous cells or tissue due to PrPSc deposition, and a demonstration on how the IR spectral information can be correlated with results of complementary studies using immunohistochemistry and x-ray fluorescence techniques. Using IR microspectroscopy, some neurons exhibited a high accumulation of disease-associated prion protein evidenced by an increased amount of β-sheet at narrow regions in or around the infected nervous cells. However, not all neurons from terminally diseased hamsters showed PrPSc deposition. Generally, the average spectral differences between all control and diseased DRG spectra are small but consistent as demonstrated by independent experiments. Along with studies on the purified misfolded prion protein, these data suggest that synchrotron FTIR microspectroscopy is capable of detecting the misfolded prion protein in situ without the necessity of immunostaining or purification procedures.
- Subjects :
- Gene isoform
Prions
animal diseases
Biophysics
Scrapie
Context (language use)
Biology
Biochemistry
Nervous System
Prion Diseases
Pathogenesis
Protein structure
Cricetinae
Spectroscopy, Fourier Transform Infrared
Synchrotron infrared microspectroscopy
medicine
Animals
Dorsal root ganglia
chemistry.chemical_classification
Nervous tissue
PrPC
Cell Biology
Chemical mapping
Virology
Cell biology
nervous system diseases
medicine.anatomical_structure
chemistry
Cats
Cattle
Glycoprotein
Immunostaining
PrPSc
Subjects
Details
- Language :
- English
- ISSN :
- 00052736
- Issue :
- 7
- Database :
- OpenAIRE
- Journal :
- Biochimica et Biophysica Acta (BBA) - Biomembranes
- Accession number :
- edsair.doi.dedup.....f2b4e0d927e2a776035873687468d777
- Full Text :
- https://doi.org/10.1016/j.bbamem.2006.05.026