Open AccessADAMTS13 and 15 are not regulated by the full length and N-terminal domain forms of TIMP-1, -2, -3 and -4
Author(s) -
Cenqi Guo,
Anastasia Tsigkou,
Meng Huee Lee
Publication year - 2015
Publication title -
biomedical reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.607
H-Index - 25
eISSN - 2049-9442
pISSN - 2049-9434
DOI - 10.3892/br.2015.535
Subject(s) - adamts , metalloproteinase , disintegrin , matrix metalloproteinase , adamts13 , chemistry , tissue inhibitor of metalloproteinase , cancer research , microbiology and biotechnology , von willebrand factor , biology , biochemistry , immunology , thrombospondin , platelet
A disintegrin and metalloproteinase with thombospondin motifs (ADAMTS) 13 and 15 are secreted zinc proteinases involved in the turnover of von Willebrand factor and cancer suppression. In the present study, ADAMTS13 and 15 were subjected to inhibition studies with the full-length and N-terminal domain forms of tissue inhibitor of metalloproteinases (TIMPs)-1 to -4. TIMPs have no ability to inhibit the ADAMTS proteinases in the full-length or N-terminal domain form. While ADAMTS13 is also not sensitive to the hydroxamate inhibitors, batimastat and ilomastat, ADAMTS15 can be effectively inhibited by batimastat ( K i app 299 nM). In conclusion, the present results indicate that TIMPs are not the regulators of these two ADAMTS proteinases.