Phosphorylation and biosynthesis of high molecular weight proteins of tumor nuclear matrix

Bazarnova, T. M.; Buldyaeva, T. V.; Filatova, L. S.; Akopov, S. B.; Zbarsky, I. B.

doi:10.1038/cr.1998.20

Cited by 3 publications

(2 citation statements)

References 19 publications

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“…The reason of the overexpression of the 19S particle characterizing the 26S proteasome pool in carcinoma is clear. The high level of the protein metabolism is typical for malignant tumors [32,33] which, in turn, requires the high level of the proteolytic enzymes including the 26S proteasomes. However, the cause of the immune proteasome overexpression is more complicated.…”

Section: Changes In the Proteasome Pool In The Development Of Human Pmentioning

confidence: 99%

Changes in proteasome pool in human papillary thyroid carcinoma development

et al. 2011

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Searching the antitumor drug targets among proteasomes, “ubiquitous” enzyme systems, may provide a new impulse to the antitumor drug discovery. In this study, changes in the proteasome pool in the development of human papillary thyroid carcinoma were determined. Proteasome activities were evaluated by hydrolysis of commercial fluorogenic peptides. Changes in the expression of the total proteasome pool, proteasome 19S activator and proteolytic constitutive subunits X(β5), Y(β1) and immune subunits LMP7 (β5i) and LMP2 (β1i) were investigated by Western blotting. The distribution of the proteasome subunits in thyroid gland cells was detected by immunohistochemistry. It was shown that the chymotrypsin- and caspase-like activities as well as the expression of the total proteasome pool, proteasome 19S activator and immune subunits increased gradually in the tumors at the T2N0M0 and T3N0M0 stages in comparison with the control tissues. Among the structures studied, the expression of the 19S activator and immune proteasomes, which contain the LMP2 (β1i) subunit, was enhanced to the largest degree in tumor cells. The data obtained may be implicated in a new therapeutic strategy. Taking into consideration the antitumor function of the immune proteasomes, we advance the 19S activator as the target for the development of a novel antitumor therapy.

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Section: Changes In the Proteasome Pool In The Development Of Human Pmentioning

confidence: 99%

Changes in proteasome pool in human papillary thyroid carcinoma development

et al. 2011

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“…The increased level of the 26S proteasomes in hepatocellular carcinoma is easy to understand. High protein metabolism is typical for malignant tumours, including liver cancer [24, 25], which, in turn, requires more proteolytic enzymes, such as the 26S proteasomes. …”

Section: Resultsmentioning

confidence: 99%

Changes in the Proteasome Pool during Malignant Transformation of Mouse Liver Cells

et al. 2010

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Multiple forms of proteasomes regulate cellular processes by destroying proteins or forming the peptides involved in those processes. Various pathologies, including carcinogenesis, are related to changes in the functioning of the proteasome forms. In this study, we looked at the changes in the pool of liver proteasomes during nodular regenerative hyperplasia and formation of adenoma and hepatocellular carcinoma in mice treated with Dipin, followed by partial liver resection. The relative content of various proteasome forms was determined using Western blot analysis. The chymotrypsin–like activity of proteasomes was assessed from the hydrolysis of the commercial Suc–LLVY–AMC substrate. It was found that changes in the proteasome pool appeared already during the formation of diffuse nodules, the changes being the increased expression of the X(β5) constitutive subunit and the LMP7(β5i) and LMP2(β1i) immune subunits, accompanied by the increase of the total proteasome pool and the decrease in the chymotrypsin–like activity. These changes were more pronounced in hepatocellular carcinoma. The content of the total proteasome pool and the LMP2(β1i) immune subunit and the chymotrypsin–like activity in adenoma were intermediate compared to those in the samples of liver with diffuse nodules and carcinoma. In addition, the level of the Rpt6 subunit present in the 19S proteasome activator was increased in carcinoma. Our results indicate that nodular regenerative hyperplasia and adenomatosis may be stages preceding carcinogenesis. We also conclude that there is a need to find signalling pathways that change the expression of various proteasome subunits during carcinogenesis. The 19S proteasome activator, which is overexpressed in malignant tumours, can be a promising target for the development of new anticancer drugs.

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Exclusion of immune proteasomes from mouse ascitic carcinoma Krebs-II cells

Astakhova

Шарова

2006

Biol Bull Russ Acad Sci

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Phosphorylation and biosynthesis of high molecular weight proteins of tumor nuclear matrix

Cited by 3 publications

References 19 publications

Changes in proteasome pool in human papillary thyroid carcinoma development

Changes in proteasome pool in human papillary thyroid carcinoma development

Changes in the Proteasome Pool during Malignant Transformation of Mouse Liver Cells

Exclusion of immune proteasomes from mouse ascitic carcinoma Krebs-II cells

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