tmc-95a and Colonic-Neoplasms

tmc-95a has been researched along with Colonic-Neoplasms* in 1 studies

Other Studies

1 other study(ies) available for tmc-95a and Colonic-Neoplasms

Article	Year
TMC-95A, B, C, and D, novel proteasome inhibitors produced by Apiospora montagnei Sacc. TC 1093. Taxonomy, production, isolation, and biological activities. The Journal of antibiotics, 2000, Volume: 53, Issue:2 In our course of screening for novel proteasome inhibitors, TMC-95A and its diastereomers, TMC-95B to D, were isolated from the fermentation broth of Apiospora montagnei Sacc. TC 1093. TMC-95A inhibited the chymotrypsin-like (ChT-L), trypsin-like (T-L), and peptidylglutamyl-peptide hydrolyzing (PGPH) activities of 20S proteasome with IC50 values of 5.4nM, 200nM, and 60nM, respectively. TMC-95B inhibited these activities to the same extent as TMC-95A, while the inhibitory activities of TMC-95C and D were 20 to 150 times weaker than that of TMC-95A and B. TMC-95A did not inhibit m-calpain, cathepsin L, and trypsin at 30 microM, suggesting its high selectivity for proteasome. Taxonomy of the producing strain is also described. Topics: Chymotrypsin; Colonic Neoplasms; Cysteine Endopeptidases; Fermentation; HL-60 Cells; Humans; Hydrolysis; Inhibitory Concentration 50; Mitosporic Fungi; Multienzyme Complexes; Peptides; Peptides, Cyclic; Protease Inhibitors; Proteasome Endopeptidase Complex; Trypsin; Tumor Cells, Cultured	2000

Article

Year

TMC-95A, B, C, and D, novel proteasome inhibitors produced by Apiospora montagnei Sacc. TC 1093. Taxonomy, production, isolation, and biological activities.

The Journal of antibiotics, 2000, Volume: 53, Issue:2

In our course of screening for novel proteasome inhibitors, TMC-95A and its diastereomers, TMC-95B to D, were isolated from the fermentation broth of Apiospora montagnei Sacc. TC 1093. TMC-95A inhibited the chymotrypsin-like (ChT-L), trypsin-like (T-L), and peptidylglutamyl-peptide hydrolyzing (PGPH) activities of 20S proteasome with IC50 values of 5.4nM, 200nM, and 60nM, respectively. TMC-95B inhibited these activities to the same extent as TMC-95A, while the inhibitory activities of TMC-95C and D were 20 to 150 times weaker than that of TMC-95A and B. TMC-95A did not inhibit m-calpain, cathepsin L, and trypsin at 30 microM, suggesting its high selectivity for proteasome. Taxonomy of the producing strain is also described.

Topics: Chymotrypsin; Colonic Neoplasms; Cysteine Endopeptidases; Fermentation; HL-60 Cells; Humans; Hydrolysis; Inhibitory Concentration 50; Mitosporic Fungi; Multienzyme Complexes; Peptides; Peptides, Cyclic; Protease Inhibitors; Proteasome Endopeptidase Complex; Trypsin; Tumor Cells, Cultured

2000