Proteasome Expression in Ovarian Heterotopic Allografts of Wistar and August Rats under Induction of Donor-Specific Tolerance

Astakhova, T. Yu.; Божок, Г. А.; Alabedal’karim, N. M.; Karpova, Ya. D.; Lyupina, Yu. V.; Ushakova, E. M.; Legach, E. I.; Bondarenko, T. N.; Шарова, Н. П.

doi:10.1134/s1062360419050023

Cited by 5 publications

(5 citation statements)

References 14 publications

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“…It indicates the universal role of the proteasomes with LMP2 subunit in the tumor development. By analogy with the role of LMP2 subunit and PA28αβ activator in the survival of allotransplant [ 19 ], we believe that these proteasome components are important for the survival of tumor cells. In the present study, we discovered that the great increase in LMP2 activity is related to proteasome subtype containing PA28αβ activator.…”

Section: Resultsmentioning

confidence: 99%

“…However, what can be the role of PA28αβ activator in tumor cells? Previously, we detected that the high levels of PA28αβ activator and LMP2 (but not LMP7) subunit in allograft cells were associated with the allograft engraftment regardless of donor-recipient differences [ 19 ]. We assume that LMP2 subunit and PA28αβ activator embedded in the same proteasome structure, are involved in ensuring the survival of rectal cancer cells, foreign for an organism.…”

Section: Resultsmentioning

confidence: 99%

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Proteasomes in Patient Rectal Cancer and Different Intestine Locations: Where Does Proteasome Pool Change?

Erokhov

Куликов

Karpova

et al. 2021

Cancers

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A special problem in the surgery of rectal cancer is connected with a need for appropriate removal of intestine parts, along with the tumor, including the fragment close to the sphincter. To determine the length of fragments to remove, it is necessary to reveal areas without changes in molecule functioning, specific for tumor. The purpose of the present study was to investigate functioning the proteasomes, the main actors in protein hydrolysis, in patient rectal adenocarcinoma and different intestine locations. Chymotrypsin-like and caspase-like activities, open to complex influence of different factors, were analyzed in 43–54 samples by Suc-LLVY-AMC- and Z-LLE-AMC-hydrolysis correspondingly. Both activities may be arranged by the decrease in the location row: cancer→adjacent tissue→proximal (8–20 cm from tumor) and distal (2 and 4 cm from tumor) sides. These activities did not differ noticeably in proximal and distal locations. Similar patterns were detected for the activities and expression of immune subunits LMP2 and LMP7 and expression of 19S and PA28αβ activators. The largest changes in tumor were related to proteasome subtype containing LMP2 and PA28αβ that was demonstrated by native electrophoresis. Thus, the results indicate a significance of subtype LMP2-PA28αβ for tumor and absence of changes in proteasome pool in distal fragments of 2–4 cm from tumor.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Proteasomes in Patient Rectal Cancer and Different Intestine Locations: Where Does Proteasome Pool Change?

Erokhov

Куликов

Karpova

et al. 2021

Cancers

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“…In addition, proteasome subtype β1i, β2i (also known as MECL-1, with trypsin-like activity), and β5, without β5i, can be formed [142]. The high expression of proteasomes containing subunit β1i, but not β5i, is associated with the development of immunological tolerance [143]. β1i is required for the adaptation of rat ventricular cardiomyocytes to reach pressure overload [144].…”

Section: Mixed Proteasomementioning

confidence: 99%

Targeted Protein Degradation: Principles and Applications of the Proteasome

Kim,

Chey

et al. 2023

Cells

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The proteasome is a multi-catalytic protease complex that is involved in protein quality control via three proteolytic activities (i.e., caspase-, trypsin-, and chymotrypsin-like activities). Most cellular proteins are selectively degraded by the proteasome via ubiquitination. Moreover, the ubiquitin–proteasome system is a critical process for maintaining protein homeostasis. Here, we briefly summarize the structure of the proteasome, its regulatory mechanisms, proteins that regulate proteasome activity, and alterations to proteasome activity found in diverse diseases, chemoresistant cells, and cancer stem cells. Finally, we describe potential therapeutic modalities that use the ubiquitin–proteasome system.

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“…The functions of the immune proteasomes in immune processes are not limited by the formation of antigenic epitopes for the MHC class I system. The subtype of the immune proteasomes containing the large multifunctional peptidase 2 LMP2 (but not LMP7) subunit is related to the development of the immunological tolerance to the allograft [87]. In the transplant cells, this proteasome subtype is likely to produce special peptides that inhibit the activity of cytotoxic T-lymphocytes.…”

Section: Ubiquitin Proteasome Systemmentioning

confidence: 99%

“…Interestingly, the detected dependence of proteasome expression in the tumor on the presence or absence of ERα touches the proteasome subtype containing the proteolytic subunit LMP2 (but not LMP7). Obviously, this proteasome subtype in tumor cells, as well as in allograft cells, is involved in the development of immunological tolerance [87].…”

Section: Mutual Regulation Of Estrogen Receptors and Ubiquitin Proteamentioning

confidence: 99%

Estrogen Receptors and Ubiquitin Proteasome System: Mutual Regulation

et al. 2020

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This review provides information on the structure of estrogen receptors (ERs), their localization and functions in mammalian cells. Additionally, the structure of proteasomes and mechanisms of protein ubiquitination and cleavage are described. According to the modern concept, the ubiquitin proteasome system (UPS) is involved in the regulation of the activity of ERs in several ways. First, UPS performs the ubiquitination of ERs with a change in their functional activity. Second, UPS degrades ERs and their transcriptional regulators. Third, UPS affects the expression of ER genes. In addition, the opportunity of the regulation of proteasome functioning by ERs—in particular, the expression of immune proteasomes—is discussed. Understanding the complex mechanisms underlying the regulation of ERs and proteasomes has great prospects for the development of new therapeutic agents that can make a significant contribution to the treatment of diseases associated with the impaired function of these biomolecules.

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Proteasome Expression in Ovarian Heterotopic Allografts of Wistar and August Rats under Induction of Donor-Specific Tolerance

Cited by 5 publications

References 14 publications

Proteasomes in Patient Rectal Cancer and Different Intestine Locations: Where Does Proteasome Pool Change?

Proteasomes in Patient Rectal Cancer and Different Intestine Locations: Where Does Proteasome Pool Change?

Targeted Protein Degradation: Principles and Applications of the Proteasome

Estrogen Receptors and Ubiquitin Proteasome System: Mutual Regulation

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