The DOI matches its Crossref record; 52 of the 52 references it cites were found in a registry or an index.
Phosphorylation by cAMP-dependent protein kinase inhibits the degradation of tau by calpain.
Open accessAbstract
The effects of cAMP-dependent protein kinase (cAMP-PK) phosphorylation on the degradation of the microtubule-associated protein tau by calpain were studied. Purified bovine brain tau that had been phosphorylated by cAMP-PK had a slower migration pattern on sodium dodecyl sulfate-polyacrylamide gels and a more acidic, less heterogeneous pattern on two-dimensional, nonequilibrium pH gradient electrophoresis (NEPHGE) gels compared with untreated tau. Phosphorylation of tau by cAMP-PK significantly inhibited its proteolysis by calpain compared with untreated tau. To our knowledge this is the first demonstration that phosphorylation of tau by a specific kinase results in increased resistance to hydrolysis by calpain. Tau dephosphorylated by alkaline phosphatase migrated more rapidly on sodium dodecyl sulfate-polyacrylamide gels and also showed an altered two-dimensional NEPHGE pattern. Dephosphorylation of tau had no effect on its susceptibility to calpain proteolysis, indicating that regulation of the susceptibility to calpain hydrolysis is due to the phosphorylation of a specific site(s). These results suggest a role for phosphorylation in regulating the degradation of tau. Abnormal phosphorylation could result in a protease-resistant tau population which may contribute to the formation of paired helical filaments in Alzheimer's disease.
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“phosphorylation of tau by PKA inhibits calpain-mediated tau proteolysis”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [210]
In the citing paper
“and NFTs are resistant to calpain cleavage [210, 211].”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [210]
Citations
Cites
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Goll, D. E., Thompson, V. F., Li, H., WEI, W., & Cong, J. (2003) · Physiological Reviews · doi:10.1152/physrev.00029.2002 · Cited by 2,899
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Clearance systems in the brain—implications for Alzheimer disease
Tarasoff-Conway, J. M., Carare, R. O., Osorio, R. S., Glodzik, L., Butler, T., Fieremans, E., Axel, L., Rusinek, H., Nicholson, C., Zlokovic, B. V., et al. (2015) · Nature Reviews Neurology · doi:10.1038/nrneurol.2015.119 · Cited by 1,678
Roles of tau protein in health and disease
Guo, T., Noble, W., & Hanger, D. P. (2017) · Acta Neuropathologica · doi:10.1007/s00401-017-1707-9 · Cited by 1,003
Metadata
- Authors
- Litersky, J. M., & Johnson, G. V.
- Affiliations
- University of Alabama (US)
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1992-01
- Volume
- 267
- Issue
- 3
- Pages
- 1563-1568
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1531327859
- Cited by
- 201
- References
- 52
- Citations by year
- 2026: 1 · 2024: 4 · 2023: 3 · 2022: 1 · 2021: 2 · 2020: 2 · 2018: 2 · 2017: 3 · 2016: 1 · 2015: 3 · 2013: 4 · 2012: 6
- FWCI
- 8.21
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5p01ag006569-13)
- National Institute on Aging (AG06569)
- National Institute of Neurological Disorders and Stroke (NS-27538)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Calpain Protease Function and Regulation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › S100 Proteins and Annexins
- Keywords
- tau protein, protein kinase A, phosphorylation, calpain, proteolysis, microtubule-associated proteins, dephosphorylation, protease resistance, Alzheimer's disease, paired helical filaments
- MeSH terms
- Animals, Autoradiography, Brain, Calpain, Cattle, Electrophoresis, Polyacrylamide Gel, Kinetics, Microtubules, Phosphorus Radioisotopes, Phosphorylation, Protein Kinases, Immunoblotting, Electrophoresis, Gel, Two-Dimensional, tau Proteins
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