Assembly of Proteins to Postsynaptic Densities after Transient Cerebral Ischemia

Hu, Bingren; Park, Minkyu; Martone, Maryann E.; Fischer, Wolfgang; Ellisman, Mark H.; Zivin, Justin A.

doi:10.1523/jneurosci.18-02-00625.1998

Cited by 154 publications

(148 citation statements)

References 70 publications

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“…This translocation of chelatable zinc ions from presynaptic terminals to postsynaptic neurons has been proposed to play an important role in the selective neuronal death resulting from ischemia, status epilepticus and trauma Tonder et al 1990;Koh et al 1996;Suh et al 2000; except for Cole et al 2000). Consistent with our in vitro observation that zinc ions promote the assembly of the PSD, after transient cerebral ischemia, a condition that lead to the accumulation of chelatable zinc in neurons (Tonder et al 1990;Koh et al 1996), the PSDs of hippocampal neurons became significantly thicker (Hu et al 1998). Similarly, after stimulation with high concentrations of KCl and with glutamate, treatments that also probably resulted in the translocation of presynaptic zinc to the postsynaptic neurons (Assaf and Chung 1984), PSDs in hippocampal neurons became thicker (Dosemeci et al 2001).…”

Section: Discussionsupporting

confidence: 86%

“…cross-sectional area, thickness and curvature, and the protein content of the PSD (e.g. Greenough et al 1978;Rutledge 1978;Rees et al 1985;Strevaag and Greenough 1985;Desmond and Levy 1986;Strack et al 1997;Hu et al 1998;Dosemeci et al 2001; except for the study of Sorra and Harris 1998). Time-lapse recording of the clusters of green fluorescence protein PSD95 in hippocampal neurons revealed rapid formation and remodeling of the PSD (Marrs et al 2001).…”

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confidence: 99%

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Structural role of zinc ions bound to postsynaptic densities

Jan

Chen

Tsai

et al. 2002

Journal of Neurochemistry

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Postsynaptic densities (PSDs) isolated from porcine cerebral cortices are large aggregates consisting of more than 30 different proteins. Inductively coupled plasma-mass spectrometric analyses revealed that isolated PSDs contained zinc at a concentration of 4.1 nmol per mg protein. Treatment with 8 M urea lead to dissociation of the PSDs into small components and, concomitantly, depletion of most of their bound zinc. After removal of the urea by dialysis, urea-dissociated PSD proteins did not reassemble into aggregates by themselves. Adding ZnCl 2 to urea-treated PSD samples resulted in the assembly of urea-dissociated proteins into large aggregates with morphology and protein composition closely resembling those of the original PSDs. Mg 2+ , Ca 2+ , Co 2+ , Cd 2+ , Cu 2+ , Mn 2+ , Fe 3+ , K + and Na + ions at higher concentrations also induced the aggregation of urea-dissociated PSD protein. The structures of the K + -, Na + -, Mg 2+ -and Ca 2+ -induced aggregates were distinct from that of the original PSDs. Our results indicate that the structure of the PSD could be disassembled and reassembled under in vitro conditions. They further suggest that Zn 2+ ions, by binding to certain zincbinding proteins, play an important role in the formation and maintenance of the structure of the PSD.

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Section: Discussionsupporting

confidence: 86%

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confidence: 99%

Structural role of zinc ions bound to postsynaptic densities

Jan

Chen

Tsai

et al. 2002

Journal of Neurochemistry

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“…The presence of brevican in this fraction has already been reported (Seidenbecher et al 1998;Niederöst et al 1999) and it was suggested to contribute to the nonpermissive properties of CNS myelin (Niederöst et al 1999). The light membrane fraction is a less well defined membrane subpopulation, which contains a mixture of endoplasmic reticulum, Golgi and plasma membranes as estimated by electron microscopy (Cohen et al 1977;Hu et al 1998). This fraction contains extrasynaptic marker molecules of neuronal membranes, such as BDNF receptor gp145trkB and gp95trkB or the 5-hydroxytryptamine receptor 2A (Hu et al (b) (a) Fig.…”

Section: Discussionmentioning

confidence: 84%

Brevican isoforms associate with neural membranes

Seidenbecher

Smalla

Fischer

et al. 2002

Journal of Neurochemistry

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Brevican is a neural-specific proteoglycan of the brain extracellular matrix, which is particularly abundant in the terminally differentiated CNS. It is expressed by neuronal and glial cells, and as a component of the perineuronal nets it decorates the surface of large neuronal somata and primary dendrites. One brevican isoform harbors a glycosylphosphatidylinositol anchor attachment site and, as shown by ethanolamine incorporation studies, is indeed glypiated in stably transfected HEK293 cells as well as in oligodendrocyte precursor Oli-neu cells. The major isoform is secreted into the extracellular space, although a significant amount appears to be tightly attached to the cell membrane, as it floats up in sucrose gradients. Flotation is sensitive to detergent treatment.Brevican is most prominent in the microsomal, light membrane and synaptosomal fractions of rat brain membrane preparations. The association with the particulate fraction is in part sensitive to chondroitinase ABC and phosphatidylinositolspecific phospholipase C treatment. Furthermore, brevican staining on the surface of hippocampal neurons in culture is diminished after hyaluronidase or chondroitinase ABC treatment. Taken together, this could provide a mechanism by which perineuronal nets are anchored on neuronal surfaces.

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“…However, ischemic conditions have since been shown to induce the formation of self-associated CaMKII clusters in a variety of systems (Dosemeci et al, 2000;Tao-Cheng et al, 2002;Hudmon et al, 1996), and it has been demonstrated that these clusters contaminate PSD-enriched fractions (Dosemeci et al, 2000). Since it has been shown that in vivo ischemia increases the thickness of the PSD (Hu et al, 1998), and that an in vitro ischemic treatment induces both CaMKII clustering and an increase in CaMKII labeling at the PSD (which correlates with an increase in PSD thickness) (Dosemeci et al, 2000), it is likely that the increase in CaMKII concentration in PSD-enriched fractions that we and others have observed represents both CaMKII translocation to the PSD and cluster formation.…”

Section: Discussionmentioning

confidence: 99%

αCaMKII autophosphorylation levels differ depending on subcellular localization

et al. 2007

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Calcium/calmodulin-dependent protein kinase II (CaMKII) has important roles in many processes in the central nervous system. It is enriched at the post-synaptic density (PSD), a localization which is thought to be critical for many of its proposed neuronal functions. In order to better understand the mechanisms that regulate association of CaMKII with the PSD, we compared the levels of autophosphorylation between PSD-associated kinase and kinase in other parts of the neuron. We were surprised to find that αCaMKII in a PSD-enriched fraction prepared from recovered hippocampal CA1-minislices had a relatively low level of threonine 286 (T286) phosphorylation and a relatively high level of threonine 305 (T305) phosphorylation. Furthermore, when the minislices were subjected to a treatment that mimics ischemic conditions, there was a significant translocation of αCaMKII to the PSD-enriched fraction accompanied with a dramatic reduction in T286 phosphorylation levels throughout the neuron. These findings have important implications for our understanding of the role of autophosphorylation in the localization of CaMKII.

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Assembly of Proteins to Postsynaptic Densities after Transient Cerebral Ischemia

Cited by 154 publications

References 70 publications

Structural role of zinc ions bound to postsynaptic densities

Structural role of zinc ions bound to postsynaptic densities

Brevican isoforms associate with neural membranes

αCaMKII autophosphorylation levels differ depending on subcellular localization

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