Journal
BMC NEUROSCIENCE
Volume 9, Issue -, Pages -Publisher
BMC
DOI: 10.1186/1471-2202-9-S2-S7
Keywords
-
Categories
Funding
- Institute for the Study of Aging (Alzdiscovery award)
- National Institute of Aging [IR2IAG0288II]
- Geoffrey Beene Cancer Research Center of Memorial Sloan-Kettering Cancer Center
Ask authors/readers for more resources
Both malignant transformation and neurodegeneration, as it occurs in Alzheimer's disease, are complex and lengthy multistep processes characterized by abnormal expression, post-translational modification, and processing of certain proteins. To maintain and allow the accumulation of these dysregulated processes, and to facilitate the step-wise evolution of the disease phenotype, cells must co-opt a compensatory regulatory mechanism. In cancer, this role has been attributed to heat shock protein 90 ( Hsp90), a molecular chaperone that maintains the functional conformation of multiple proteins involved in cell-specific oncogenic processes. In this sense, at the phenotypic level, Hsp90 appears to serve as a biochemical buffer for the numerous cancer-specific lesions that are characteristic of diverse tumors. The current review proposes a similar role for Hsp90 in neurodegeneration. It will present experimentally demonstrated, but also hypothetical, roles that suggest Hsp90 can act as a regulator of pathogenic changes that lead to the neurodegenerative phenotype in Alzheimer's disease.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available