In vitro degradation of insulin-like peptide 3 by insulin-degrading enzyme.
Insulin-like peptide 3 (INSL3) is an insulin superfamily peptide hormone, primarily expressed in the testes and playing a key role in the fetus testes descent and suppression of male germ cell apoptosis. Insulin-degrading enzyme (IDE) is a zinc-metalloprotease, responsible for in vivo degradation of insulin, Abeta, and other peptide hormones. IDE has high expression level in the testes, implying it might be involved in INSL3 turnover in vivo. In present work, we studied in vitro degradation of INSL3 by IDE. Recombinant human IDE degraded human INSL3, but its degradation rate for INSL3 is more than a magnitude lower than that for insulin. However, IDE bound INSL3 and insulin with almost same affinity. IDE cleaved the peptide bond between B26R and B27W of INSL3, and released a pentapeptide, WSTEA, from the C-terminal of B-chain. Our present work suggested that IDE might play a role in INSL3 degradation in vivo.
Zhang
Wei-Jie
WJ
Institute of Protein Research, College of Life Sciences and Technology, Tongji University, 200092 Shanghai, China.
Luo
Xiao
X
Guo
Zhan-Yun
ZY
D000328:Adult; D000595:Amino Acid Sequence; D000818:Animals; D006801:Humans; D007328:Insulin / Q000235:genetics / Q000378:metabolism*; D007339:Insulysin / Q000378:metabolism*; D008297:Male; D008969:Molecular Sequence Data; D011485:Protein Binding; D011506:Proteins / Q000235:genetics / Q000378:metabolism*; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism
D007328:Insulin; C084797:Leydig insulin-like protein; D011506:Proteins; D011994:Recombinant Proteins; D007339:Insulysin