title: ADAMTS13 and 15 are not regulated by the full length and N-terminal domain forms of TIMP-1, -2, -3 and -4.
abstract: 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 (Kiapp299 nM). In conclusion, the present results indicate that TIMPs are not the regulators of these two ADAMTS proteinases.
authors: Department of Biological Sciences, Xian Jiaotong-Liverpool University, Suzhou, Jiangsu 215123, P.R. China.
authors: Cenqi
authors: C
authors: Guo
authors: Department of Biological Sciences, Xian Jiaotong-Liverpool University, Suzhou, Jiangsu 215123, P.R. China.
authors: Anastasia
authors: A
authors: Tsigkou
authors: Department of Biological Sciences, Xian Jiaotong-Liverpool University, Suzhou, Jiangsu 215123, P.R. China.
authors: Meng Huee
authors: MH
authors: Lee
keywords: a disintegrin and metalloproteinase; a disintegrin and metalloproteinase with thombospondin type 1 motifs; enzyme inhibition; matrix metalloproteinase; tissue inhibitors of metalloproteinases