Cited by 76Alzheimer's disease research and treatmentsS100 Proteins and AnnexinsDementia and Cognitive Impairment Research

The neuronal calcium sensor protein VILIP-1 is associated with amyloid plaques and extracellular tangles in Alzheimer’s disease and promotes cell death and tau phosphorylation in vitro: a link between calcium sensors and Alzheimer’s disease?

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Schnurra, I., Bernstein, H.-G., Riederer, P., Braunewell, K.-H.·2001·Neurobiology of Disease

Abstract

To investigate whether the observed association of intracellular neuronal calcium sensor (NCS) proteins with amyloid plaques and neurofibrillar tangles in Alzheimer brains is linked to a possible neuroprotective or neurotoxic activity of the protein, we performed cytotoxicity tests in PC12 cells transfected with the calcium sensor protein VILIP-1 (visinin-like protein) and the calcium buffer protein calbindin-D28K. Whereas VILIP-1 expression enhanced the neurotoxic effect of ionomycin already at low ionophore concentrations, calbindin-D28K protected against ionomycin-induced cytotoxicity only at high ionomycin and therefore calcium concentrations. However, in double-transfected cells calbindin-D28K rescued VILIP-1-mediated cytotoxicity at low ionomycin concentrations. Since VILIP-1 was found to be associated with fibrillar tangles in Alzheimer brains, we tested whether VILIP-1 has an influence on tau hyperphosphorylation. VILIP-1 expression enhanced hyperphosphorylation of tau protein compared to nontransfected or calbindin-D28K-transfected cells. These results raise the possibility that the observed reduction in VILIP-1-expressing cells may indicate a selective vulnerability of these neurons and that the calcium sensor protein is involved in the pathophysiology of Alzheimer's disease. The calcium sensor protein may influence tau phosphorylation and have a role in calcium-mediated neurotoxicity opposed to the previously discovered protective effect of calcium buffer proteins.

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Crossref · 10.1006/nbdi.2001.0432

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Authors
Schnurra, I., Bernstein, H.-G., Riederer, P., & Braunewell, K.-H.
Affiliations
  • Otto-von-Guericke-Universität Magdeburg (DE)
  • University of Würzburg (DE)
  • Humboldt-Universität zu Berlin (DE)
Venue
Neurobiology of Disease
Publisher
Elsevier BV
Published
2001-10
Volume
8
Issue
5
Pages
900-909
ISSN
0969-9961 (ISSN-L)
OpenAlex
W2089804237
Cited by
76
References
46
Citations by year
2026: 1 · 2025: 5 · 2024: 1 · 2023: 2 · 2022: 4 · 2020: 1 · 2019: 2 · 2017: 2 · 2016: 4 · 2015: 8 · 2014: 2 · 2013: 3 · 2012: 6
FWCI
1.20
Type
journal article
Language
en
Open access
Locations
  • Neurobiology of Disease (publishedVersion)
  • PubMed (publishedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders
  • College of Environmental Science and Forestry, State University of New York
  • Deutsche Forschungsgemeinschaft (Br-1579/2-1, Br-1579/3-1)
Topics
  • Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › S100 Proteins and Annexins
  • Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
Keywords
VILIP-1, neuronal calcium sensor proteins, Alzheimer's disease, amyloid plaques, neurofibrillary tangles, tau hyperphosphorylation, calbindin-D28k, ionomycin, PC12 cells, neuronal cell death
MeSH terms
Alzheimer Disease, Animals, Brain, Brain Chemistry, Calcium, Calcium-Binding Proteins, Humans, Ionophores, Nerve Tissue Proteins, Phosphorylation, Protein Processing, Post-Translational, Rabbits, Recombinant Fusion Proteins, Transfection, Ionomycin, PC12 Cells, Neurofibrillary Tangles, tau Proteins, Calcium Signaling, Receptors, Calcium-Sensing, Rats, Neurocalcin, Plaque, Amyloid, Calbindins, S100 Calcium Binding Protein G, Calbindin 1

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