Subfield and layer-specific depletion in calbindin-D28K, calretinin and parvalbumin immunoreactivity in the dentate gyrus of amyloid precursor protein/presenilin 1 transgenic mice
Autor: | Miroljub Popović, María Caballero-Bleda, Inga Kadish, T. van Groen |
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Rok vydání: | 2008 |
Předmět: |
Male
Calbindins medicine.medical_specialty Mice Transgenic Granular layer Calbindin Article Presenilin Amyloid beta-Protein Precursor Mice S100 Calcium Binding Protein G Calcium-binding protein Internal medicine mental disorders Presenilin-1 Amyloid precursor protein medicine Animals Humans biology General Neuroscience Dentate gyrus Molecular biology Mice Inbred C57BL Parvalbumins Endocrinology Gene Expression Regulation nervous system Calbindin 1 Calbindin 2 Dentate Gyrus biology.protein Calretinin Parvalbumin |
Zdroj: | Neuroscience. 155:182-191 |
ISSN: | 0306-4522 |
DOI: | 10.1016/j.neuroscience.2008.05.023 |
Popis: | The depletion of neuronal calcium binding proteins deprives neurons of the capacity to buffer high levels of intracellular Ca 2+ and this leaves them vulnerable to pathological processes, such as those present in Alzheimer's disease (AD). The aim of the present study was to investigate the expression of the calcium binding proteins, calbindin-D28K, calretinin and parvalbumin in the dentate gyrus (DG) of amyloid precursor protein (APP)/presenilin 1 (PS1) transgenic (Tg) mice and their non-Tg littermates, as well as the relation with the deposition of human amyloid β (Aβ). We measured the expression of these three proteins at seven different rostro-caudal levels, and in the molecular, granular and polymorphic layers of the DG. We found that, except in the most caudal part of the DG, there is a substantial loss of calbindin-D28K immunoreactivity in all three layers of the DG in APP/PS1 mice compared with the non-Tg mice. Significant loss of calretinin immunoreactivity is present in most of the polymorphic layer of the DG of APP/PS1 mice compared with the non-Tg mice, as well as in the rostral and intermediate part of the inner molecular layer. Compared with the non-Tg mice parvalbumin immunoreactivity is significantly reduced throughout the whole polymorphic layer as well as in the rostral and intermediate part of the granular layer of DG in APP/PS1 mice. The relatively preservation of calbindin immunoreactivity in the caudal part of molecular and granular layers as well as calretinin immunoreactivity in the caudal part of polymorphic layer of the DG is likely related to the lower Aβ expression in those parts of DG. The present data suggest an involvement of calcium-dependent pathways in the pathogenesis of AD and indicate that there exists a subfield and layer-specific decrease in immunoreactivity which is related to the type of calcium-binding protein in APP/PS1 mice. Moreover, it seems that APP expression affects more the calbindin expression then parvalbumin and calretinin expression in the DG of APP/PS1 Tg mice. |
Databáze: | OpenAIRE |
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