Heterogeneity of dipeptidyl peptidase IV from C6 rat glioma cells.
Dipeptidyl peptidase IV is known to be involved, due to both hydrolytic and non-hydrolytic mechanisms, in various cell functions of normal and cancer cells as well. In this report dipeptidyl peptidase IV substrate and pH preferences, some inhibition parameters, freezing/thawing sensitivity and stability against hydrolysis by trypsin were studied in C6 rat glioma cells. Our results confirmed substantial heterogeneity of dipeptidyl peptidase IV population. Such observation is important to avoid methodological artifacts and to decrease risk of misinterpretations in biological studies.
Malík
R
R
1st Department of Medical Chemistry and Biochemistry, 1st Faculty of Medicine, Charles University, Prague 2, Czech Republic.
Vlasicová
L
L
Kadlecová
L
L
Sedo
A
A
D000818:Animals; D018819:Dipeptidyl Peptidase 4 / Q000378:metabolism*; D004795:Enzyme Stability; D005615:Freezing; D005910:Glioma / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D007532:Isoleucine / Q000031:analogs & derivatives* / Q000494:pharmacology; D009842:Oligopeptides / Q000494:pharmacology; D011480:Protease Inhibitors / Q000494:pharmacology; D051381:Rats; D013379:Substrate Specificity; D013844:Thiazoles / Q000494:pharmacology; D014357:Trypsin / Q000378:metabolism / Q000494:pharmacology; D014407:Tumor Cells, Cultured
D009842:Oligopeptides; D011480:Protease Inhibitors; D013844:Thiazoles; C114061:isoleucyl-thiazolidide; D007532:Isoleucine; C041445:diprotin A; C041446:diprotin B; D018819:Dipeptidyl Peptidase 4; D014357:Trypsin