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Presence of both constitutive and inducible forms of heat shock protein 70 in the cerebral cortex and hippocampal synapses.

Moon, Il Soo and Park, In Sick and Schenker, Leslie T. and Kennedy, Mary B. and Moon, Jung-Il and Jin, Ingnyol (2001) Presence of both constitutive and inducible forms of heat shock protein 70 in the cerebral cortex and hippocampal synapses. Cerebral Cortex, 11 (3). pp. 238-248. ISSN 1047–3211. https://resolver.caltech.edu/CaltechAUTHORS:20120424-154211643

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Abstract

Heat shock proteins serve as molecular chaperones in a protein "holding and folding" system. Protein sequencing, extraction and immunoblot analyses indicate that Hsc70, a constitutive form, is a major component of the rat postsynaptic density (PSD) fraction, while Hsp70, an inducible form, is present at the basal level. Immunohistochemical studies show that expression of Hsc70 is high, but that of Hsp70 is low, in the cerebral cortex and hippocampal formation. In dissociated hippocampal neurons, both Hsp70 and Hsc70 immunoreactivities are distributed throughout the soma and dendrites. In dendrites, there are many stained puncta which are mostly co-localized with PSD-95, a postsynaptic marker. Interestingly, variation in staining intensity of the puncta is significantly larger for Hsp70 than for Hsc70 in 2-week-old cultures, but becomes less significant in 5(1/2)-week-old cultures. At the electron microscopic level, both Hsp70 and Hsc70 are mainly associated with asymmetrical PSDs. However, Hsc70 is also associated with amorphous subsynaptic structures and spine apparatus-like cisternae. Our data indicate that both Hsp70 and Hsc70 are present in PSDs but are differentially distributed at subsynaptic sites, and provide a potential candidate system for a "synaptic tag".


Item Type:Article
Related URLs:
URLURL TypeDescription
http://dx.doi.org/10.1093/cercor/11.3.238 DOIArticle
http://cercor.oxfordjournals.org/content/11/3/238PublisherArticle
ORCID:
AuthorORCID
Kennedy, Mary B.0000-0003-1369-0525
Additional Information:© 2001 Oxford University Press. We thank Soon Nam Baek and Kyong Won Kim in Dongguk University for technical support. This work was supported by Korea Research Foundation (KRF-99-015-DI0100) to I.S.M., and NIH grant nos NS28710 and NS17760 to M.B.K.
Funders:
Funding AgencyGrant Number
Korea Research FoundationKRF-99-015-DI0100
NIHNS28710
NIHNS17760
Issue or Number:3
Record Number:CaltechAUTHORS:20120424-154211643
Persistent URL:https://resolver.caltech.edu/CaltechAUTHORS:20120424-154211643
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:30318
Collection:CaltechAUTHORS
Deposited By: Melanie Stefan
Deposited On:25 Apr 2012 15:05
Last Modified:03 Oct 2019 03:49

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