title: [Chymotripsin-like activity and subunit composition of proteasomes in human cancers].
abstract: Activity of the proteasome, polyfunctional enzymatic complex, is known to undergo changes during cancer development. This phenomenon is, probably, caused by the changes in subunit composition of proteasomes. In present work, we studied chymotrypsin-like activity of proteasomes, subunit composition and their association in breast cancer, head and neck squamous cell carcinoma, endometrial cancer, renal cancer, bladder cancer, stomach cancer and colorectal cancer. The increase of proteasome activity was revealed in most cancer tissues compared with adjacent tissues except for the renal cell carcinoma. Changes in proteasome activity in cancer tissues compared with correspondent normal tissues were accompanied by modification of its subunit composition. High proteasome activity was observed in combination with an increased expression of immune subunits and/or proteasome activator PA28, associated with activity of 20S proteasome. In breast cancer, head and neck squamous cell carcinoma, bladder cancer, stomach cancer and colorectal cancer we additionally found higher expression of Rpt6 subunit of 26S proteasome. Correlations between chymotrypsin like proteasome activity and subunit expressions were found in human cancer tissues. In summary, we suggest that proteasome ac- tivation and changes in its subunit composition plays an important role in cancer pathogenesis.
authors.forename: I V
authors.initials: IV
authors.lastname: Kondakova
authors.forename: L V
authors.initials: LV
authors.lastname: Spirina
authors.forename: V D
authors.initials: VD
authors.lastname: Koval
authors.forename: E E
authors.initials: EE
authors.lastname: Shashova
authors.forename: E L
authors.initials: EL
authors.lastname: Choinzonov
authors.forename: E V
authors.initials: EV
authors.lastname: Ivanova
authors.forename: L A
authors.initials: LA
authors.lastname: Kolomiets
authors.forename: A L
authors.initials: AL
authors.lastname: Chernyshova
authors.forename: E M
authors.initials: EM
authors.lastname: Slonimskaya
authors.forename: E A
authors.initials: EA
authors.lastname: Usynin
authors.forename: S G
authors.initials: SG
authors.lastname: Afanasyev
mesh_terms: D000074183:ATPases Associated with Diverse Cellular Activities; D048868:Adaptor Proteins, Signal Transducing / Q000235:genetics / Q000378:metabolism; D045744:Cell Line, Tumor; D053818:Chymases / Q000378:metabolism*; D006801:Humans; D060588:LIM Domain Proteins / Q000235:genetics / Q000378:metabolism; D009124:Muscle Proteins / Q000235:genetics / Q000378:metabolism; D009369:Neoplasms / Q000201:enzymology*; D046988:Proteasome Endopeptidase Complex / Q000235:genetics / Q000378:metabolism*; D021122:Protein Subunits / Q000378:metabolism; D014157:Transcription Factors / Q000235:genetics / Q000378:metabolism
chemical_list: D048868:Adaptor Proteins, Signal Transducing; D060588:LIM Domain Proteins; D009124:Muscle Proteins; C092282:PSMC5 protein, human; C085047:PSME1 protein, human; D021122:Protein Subunits; D014157:Transcription Factors; D053818:Chymases; D046988:Proteasome Endopeptidase Complex; D000074183:ATPases Associated with Diverse Cellular Activities