Purification and separation of the 20S immunoproteasome from the constitutive proteasome and identification of the subunits by LC–MS

Dechavanne, Vincent; Vilbois, Francis; Glez, Loïc; Antonsson, Bruno

doi:10.1016/j.pep.2012.10.009

Cited by 10 publications

(7 citation statements)

References 29 publications

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“…To date, studies have assessed the involvement of the total proteasome population of a cell to determine the roles of these complexes in lung diseases 9 , 45 . With the advent of novel techniques that can target and purify immunoproteasomes, improved assessment of their role in disease conditions will be possible 69 . Furthermore, it will be important to differentiate between the immunoproteasome and mixed proteasome populations in order to attain more conclusive results.…”

Section: Resultsmentioning

confidence: 99%

Emerging role of immunoproteasomes in pathophysiology

Kaur

Batra

2016

Immunol Cell Biol

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The immunoproteasome is a proteasome variant that is found only in jawed vertebrates. It is responsible for degrading intracellular proteins to generate a major source of peptides with substantial major histocompatibility complex I binding affinity. The immunoproteasome also has roles in T-cell survival, differentiation and proliferation in various pathological conditions. In humans, any alteration in the expression, assembly or function of the immunoproteasome can lead to cancer, autoimmune disorders or inflammatory diseases. Although the roles of the immunoproteasome in cancer and neurodegenerative disorders have been extensively studied, its significance in other disease conditions has only recently become known. Therefore, there is renewed interest in the development of drugs, vaccines and biomarkers that target the immunoproteasome. The current review highlights the involvement of this complex in disease pathology in addition to the advances made in immunoproteasome research.

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Section: Resultsmentioning

confidence: 99%

Emerging role of immunoproteasomes in pathophysiology

Kaur

Batra

2016

Immunol Cell Biol

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“…However, constitutive proteasomes are ubiquitously present in all tissue types and even low amounts can interfere with immunoproteasome-specific research. Dechavanne et al (2013) report that hydrophobic interaction chromatography can successfully separate immunoproteasomes from residual constitutive proteasome contamination after purification.…”

Section: Methods For Pharmacological Proteasome Researchmentioning

confidence: 99%

A Practical Review of Proteasome Pharmacology

2019

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The ubiquitin proteasome system (UPS) degrades individual proteins in a highly regulated fashion and is responsible for the degradation of misfolded, damaged, or unneeded cellular proteins. During the past 20 years, investigators have established a critical role for the UPS in essentially every cellular process, including cell cycle progression, transcriptional regulation, genome integrity, apoptosis, immune responses, and neuronal plasticity. At the center of the UPS is the proteasome, a large and complex molecular machine containing a multicatalytic protease complex. When the efficiency of this proteostasis system is perturbed, misfolded and damaged protein aggregates can accumulate to toxic levels and cause neuronal dysfunction, which may underlie many neurodegenerative diseases. In addition, many cancers rely on robust proteasome activity for degrading tumor suppressors and cell cycle checkpoint inhibitors necessary for rapid cell division. Thus, proteasome inhibitors have proven clinically useful to treat some types of cancer, especially multiple myeloma. Numerous cellular processes rely on finely tuned proteasome function, making it a crucial target for future therapeutic intervention in many diseases, including neurodegenerative diseases, cystic fibrosis, atherosclerosis, autoimmune diseases, diabetes, and cancer. In this review, we discuss the structure and function of the proteasome, the mechanisms of action of different proteasome inhibitors, various techniques to evaluate proteasome function in vitro and in vivo, proteasome inhibitors in preclinical and clinical development, and the feasibility for pharmacological activation of the proteasome to potentially treat neurodegenerative disease.

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“…Standard-, immuno-and intermediate-proteasomes can be separated due to their differences in surface hydrophobicity (Kloss et al 2009;Dechavanne et al 2013). Accordingly, we have subjected rat liver 20S proteasomes to hydrophobic interaction chromatography and thereby dividing them into three subpopulations designated Ι, ΙΙ, and ΙΙΙ with subpopulation Ι being the predominant form of 20S proteasomes (Fig.…”

Section: Separation Of 20s Proteasome Into Subpopulationsmentioning

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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Purification and separation of the 20S immunoproteasome from the constitutive proteasome and identification of the subunits by LC–MS

Cited by 10 publications

References 29 publications

Emerging role of immunoproteasomes in pathophysiology

Emerging role of immunoproteasomes in pathophysiology

A Practical Review of Proteasome Pharmacology

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

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