Multiple cardiac proteasome subtypes differ in their susceptibility to proteasome inhibitors

Kloß, Alexander; Meiners, Silke; Ludwig, Antje; Dahlmann, Burkhardt

doi:10.1093/cvr/cvp217

Cited by 59 publications

(46 citation statements)

References 53 publications

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“…The abundance of intermediate proteasomes β5i in human liver and colon is in line with the previous detection of high amounts of subunit β5i with low amounts of β1i and β2i in these tissues (25). Human heart mostly contained standard proteasomes, in line with a recent study performed in rat heart (24).…”

Section: Discussionsupporting

confidence: 90%

“…Intermediate proteasomes were observed in transfected cells and were suggested to partly account for the heterogeneity of proteasome preparations isolated from rat muscle, which displayed varying physicochemical and functional properties and contained varying compositions in catalytic β subunits (18)(19)(20)(21)(22)(23). Such heterogeneity was also observed in rodent heart (20,24) and in human colon and liver (25). Posttranslational modifications, such as phopshorylation, acetylation, or methylation, were suggested to also contribute to this heterogeneity (20,22,26,27).…”

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confidence: 99%

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Two abundant proteasome subtypes that uniquely process some antigens presented by HLA class I molecules

Guillaume

Chapiro

Stroobant

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

190

273

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Most antigenic peptides presented by MHC class I molecules result from the degradation of intracellular proteins by the proteasome. In lymphoid tissues and cells exposed to IFNγ, the standard proteasome is replaced by the immunoproteasome, in which all of the standard catalytic subunits β1, β2, and β5 are replaced by their inducible counterparts β1i, β2i, and β5i, which have different cleavage specificities. The immunoproteasome thereby shapes the repertoire of antigenic peptides. The existence of additional forms of proteasomes bearing a mixed assortment of standard and inducible catalytic subunits has been suggested. Using a new set of unique subunit-specific antibodies, we have now isolated, quantified, and characterized human proteasomes that are intermediate between the standard proteasome and the immunoproteasome. They contain only one (β5i) or two (β1i and β5i) of the three inducible catalytic subunits of the immunoproteasome. These intermediate proteasomes represent between one-third and one-half of the proteasome content of human liver, colon, small intestine, and kidney. They are also present in human tumor cells and dendritic cells. We identified two tumor antigens of clinical interest that are processed exclusively either by intermediate proteasomes β5i ) or by intermediate proteasomes β1i-β5i (MAGE-A10 [254][255][256][257][258][259][260][261][262] ). The existence of these intermediate proteasomes broadens the repertoire of antigens presented to CD8 T cells and implies that the antigens presented by a given cell depend on their proteasome content.antigen processing | antigenic peptide | immunoproteasome | tumor antigen | MAGE

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Section: Discussionsupporting

confidence: 90%

mentioning

confidence: 99%

Two abundant proteasome subtypes that uniquely process some antigens presented by HLA class I molecules

Guillaume

Chapiro

Stroobant

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

190

273

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“…Briefly, this consists of the following steps: a fractionated protein precipitation with ammonium sulphate, chromatography on DEAE-Sephacel, gel filtration on Superose 6 and anion exchange chromatography on Mono Q. In the last purification step, a hydrophobic interaction chromatography was performed on a Resource-Phe column for separation of proteasome subpopulations (Kloss et al 2009). …”

Section: Purification Of 20s Proteasomes and Separation Of Proteasomementioning

confidence: 99%

“…We have shown previously that proteasomes of rat liver all comprised intermediate-type subunit compositions (Dahlmann et al 2000;Schmidt et al 2006). Taking advantage of their different surface hydrophobicity, we separated 20S proteasomes from rat heart into three subpopulations two of them comprising intermediate-type and one containing standard proteasomes (Kloss et al 2009). In the present investigation, we found that 20S proteasomes from liver of young and aged rats could also be separated into three subpopulations.…”

Section: Introductionmentioning

confidence: 99%

Molecular alterations in proteasomes of rat liver during aging result in altered proteolytic activities

Gohlke

Mishto

Textoris-Taube

et al. 2013

AGE

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Aging induces alterations of tissue protein homoeostasis. To investigate one of the major systems catalysing intracellular protein degradation we have purified 20S proteasomes from rat liver of young (2 months) and aged (23 months) animals and separated them into three subpopulations containing different types of intermediate proteasomes with standard-and immunosubunits. The smallest subpopulation ΙΙΙ and the major subpopulation Ι comprised proteasomes containing immuno-subunits β1i and β5i beside small amounts of standard-subunits, whereas proteasomes of subpopulation ΙΙ contained only β5i beside standard-subunits. In favour of a relative increase of the major subpopulation Ι, subpopulation ΙΙ and ΙΙΙ were reduced for about 55 % and 80 %, respectively, in aged rats. Furthermore, in all three 20S proteasome subpopulations from aged animals standard-active site subunits were replaced by immunosubunits. Overall, this transformation resulted in a relative increase of immuno-subunit-containing proteasomes, paralleled by reduced activity towards short fluorogenic peptide substrates. However, depending on the substrate their hydrolysing activity of long polypeptide substrates was significantly higher or unchanged. Furthermore, our data revealed an altered MHC class I antigen-processing efficiency of 20S proteasomes from liver of aged rats. We therefore suggest that the age-related intramolecular alteration of hepatic proteasomes modifies its cleavage preferences without a general decrease of its activity. Such modifications could have implications on protein homeostasis as well as on MHC class I antigen presentation as part of the immunosenescence process.

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“…The latter protect 3'UTRs of RNA from endonucleolytic degradation. 56 To avoid this complication, the protease activity of proteasomes was inactivated by either incubation with MG132 inhibitor 57 or with ethanol wash prior to their addition to A431 cells. The completeness of proteasomal inactivation by MG132 or signals have been shown to change the phosphorylation state of proteasomes.…”

Section: S Proteasome Exhibits Endoribonuclease Activity Controlledmentioning

confidence: 99%

26S proteasome exhibits endoribonuclease activity controlled by extra-cellular stimuli

Куличкова¹,

Цимоха²,

Fedorova³

et al. 2010

Cell Cycle

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Multiple cardiac proteasome subtypes differ in their susceptibility to proteasome inhibitors

Abstract: These data show that different inhibitors have differential inhibitory effects on the various cardiac proteasome subtypes. Different cardiac subtypes are inhibited by the same dose of proteasome inhibitor to a different extent.

Cited by 59 publications

References 53 publications

Two abundant proteasome subtypes that uniquely process some antigens presented by HLA class I molecules

Two abundant proteasome subtypes that uniquely process some antigens presented by HLA class I molecules

Molecular alterations in proteasomes of rat liver during aging result in altered proteolytic activities

26S proteasome exhibits endoribonuclease activity controlled by extra-cellular stimuli

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