Fine structure of synapses on dendritic spines

Frotscher, Michael; Studer, Daniel Franz; Graber, Werner Adrian; Chai, Xuejun; Nestel, Sigrun; Zhao, Shanting (2014). Fine structure of synapses on dendritic spines. Frontiers in neuroanatomy, 8, p. 94. Frontiers Research Foundation 10.3389/fnana.2014.00094

[img]
Preview
Text
fnana-08-00094.pdf - Published Version
Available under License Creative Commons: Attribution (CC-BY).

Download (5MB) | Preview

Camillo Golgi's "Reazione Nera" led to the discovery of dendritic spines, small appendages originating from dendritic shafts. With the advent of electron microscopy (EM) they were identified as sites of synaptic contact. Later it was found that changes in synaptic strength were associated with changes in the shape of dendritic spines. While live-cell imaging was advantageous in monitoring the time course of such changes in spine structure, EM is still the best method for the simultaneous visualization of all cellular components, including actual synaptic contacts, at high resolution. Immunogold labeling for EM reveals the precise localization of molecules in relation to synaptic structures. Previous EM studies of spines and synapses were performed in tissue subjected to aldehyde fixation and dehydration in ethanol, which is associated with protein denaturation and tissue shrinkage. It has remained an issue to what extent fine structural details are preserved when subjecting the tissue to these procedures. In the present review, we report recent studies on the fine structure of spines and synapses using high-pressure freezing (HPF), which avoids protein denaturation by aldehydes and results in an excellent preservation of ultrastructural detail. In these studies, HPF was used to monitor subtle fine-structural changes in spine shape associated with chemically induced long-term potentiation (cLTP) at identified hippocampal mossy fiber synapses. Changes in spine shape result from reorganization of the actin cytoskeleton. We report that cLTP was associated with decreased immunogold labeling for phosphorylated cofilin (p-cofilin), an actin-depolymerizing protein. Phosphorylation of cofilin renders it unable to depolymerize F-actin, which stabilizes the actin cytoskeleton. Decreased levels of p-cofilin, in turn, suggest increased actin turnover, possibly underlying the changes in spine shape associated with cLTP. The findings reviewed here establish HPF as an appropriate method for studying the fine structure and molecular composition of synapses on dendritic spines.

Item Type:

Journal Article (Original Article)

Division/Institute:

04 Faculty of Medicine > Pre-clinic Human Medicine > Institute of Anatomy

UniBE Contributor:

Studer, Daniel Franz and Graber, Werner Adrian

Subjects:

600 Technology > 610 Medicine & health

ISSN:

1662-5129

Publisher:

Frontiers Research Foundation

Language:

English

Submitter:

Ruslan Hlushchuk

Date Deposited:

09 Oct 2014 11:27

Last Modified:

10 Dec 2014 01:19

Publisher DOI:

10.3389/fnana.2014.00094

PubMed ID:

25249945

Uncontrolled Keywords:

actin cytoskeleton cofilin dendritic spine electron microscopy high-pressure freezing immunogold labeling

BORIS DOI:

10.7892/boris.59095

URI:

https://boris.unibe.ch/id/eprint/59095

Actions (login required)

Edit item Edit item
Provide Feedback