» Articles » PMID: 18346202

Immunoproteasome Responds to Injury in the Retina and Brain

Overview
Journal J Neurochem
Specialties Chemistry
Neurology
Date 2008 Mar 19
PMID 18346202
Citations 43
Authors
Affiliations
Soon will be listed here.
Abstract

It is well known that immunoproteasome generates peptides for MHC Class I occupancy and recognition by cytotoxic T lymphocytes (CTL). The present study focused on evidence for alternative roles for immunoproteasome. Retina and brain were analyzed for expression of immunoproteasome subunits using immunohistochemistry and western blotting under normal conditions and after injury/stress induced by CTL attack on glia (brain) or neurons (retina). Normal retina expressed substantial levels of immunoproteasome in glia, neurons, and retinal pigment epithelium. The basal level of immunoproteasome in retina was two-fold higher than in brain; CTL-induced retinal injury further up-regulated immunoproteasome expression. Immunoproteasome up-regulation was also observed in injured brain and corresponded with expression in Purkinje cells, microglia, astrocytes, and oligodendrocytes. These results suggest that the normal environment of the retina is sufficiently challenging to require on-going expression of immunoproteasome. Further, immunoproteasome up-regulation with retinal and brain injury implies a role in neuronal protection and/or repair of damage.

Citing Articles

SPRTN metalloprotease participates in repair of ROS-mediated DNA-protein crosslinks.

Erber L, Groehler 4th A, Cyuzuzo C, Baker-Wainwright J, Maskey R, Li L Sci Rep. 2024; 14(1):30919.

PMID: 39730693 PMC: 11681236. DOI: 10.1038/s41598-024-81799-9.


Targeting Microglial Immunoproteasome: A Novel Approach in Neuroinflammatory-Related Disorders.

Malek N, Gladysz R, Stelmach N, Drag M ACS Chem Neurosci. 2024; 15(14):2532-2544.

PMID: 38970802 PMC: 11258690. DOI: 10.1021/acschemneuro.4c00099.


Glitches in the brain: the dangerous relationship between radiotherapy and brain fog.

Marino N, Bedeschi M, Vaccari M, Cambiaghi M, Tesei A Front Cell Neurosci. 2024; 18:1328361.

PMID: 38515789 PMC: 10956129. DOI: 10.3389/fncel.2024.1328361.


The proteasome: A key modulator of nervous system function, brain aging, and neurodegenerative disease.

Davidson K, Pickering A Front Cell Dev Biol. 2023; 11:1124907.

PMID: 37123415 PMC: 10133520. DOI: 10.3389/fcell.2023.1124907.


Omega-3 PUFAs Suppress IL-1β-Induced Hyperactivity of Immunoproteasomes in Astrocytes.

Zgorzynska E, Dziedzic B, Markiewicz M, Walczewska A Int J Mol Sci. 2021; 22(11).

PMID: 34063751 PMC: 8196670. DOI: 10.3390/ijms22115410.


References
1.
Cruz M, Elenich L, Smolarek T, Menon A, Monaco J . DNA sequence, chromosomal localization, and tissue expression of the mouse proteasome subunit lmp10 (Psmb10) gene. Genomics. 1998; 45(3):618-22. DOI: 10.1006/geno.1997.4977. View

2.
Chen P, Hochstrasser M . Autocatalytic subunit processing couples active site formation in the 20S proteasome to completion of assembly. Cell. 1996; 86(6):961-72. DOI: 10.1016/s0092-8674(00)80171-3. View

3.
Stohwasser R, Giesebrecht J, Kraft R, Muller E, Hausler K, Kettenmann H . Biochemical analysis of proteasomes from mouse microglia: induction of immunoproteasomes by interferon-gamma and lipopolysaccharide. Glia. 2000; 29(4):355-65. View

4.
McPherson S, Heuss N, Roehrich H, Gregerson D . Bystander killing of neurons by cytotoxic T cells specific for a glial antigen. Glia. 2005; 53(5):457-66. DOI: 10.1002/glia.20298. View

5.
Gregerson D, Lew K, McPherson S, Heuss N, Ferrington D . RPE cells resist bystander killing by CTLs, but are highly susceptible to antigen-dependent CTL killing. Invest Ophthalmol Vis Sci. 2006; 47(12):5385-94. DOI: 10.1167/iovs.06-0636. View