期刊
INSECT MOLECULAR BIOLOGY
卷 15, 期 6, 页码 823-834出版社
WILEY
DOI: 10.1111/j.1365-2583.2006.00686.x
关键词
cathepsin L; insect moulting; whole body; cuticle and epidermis layer; haemolymph; E-64; CLIK148; Helicoverpa armigera
资金
- NHLBI NIH HHS [HL27283, HL60942] Funding Source: Medline
Moulting is an essential process of insect development but little is known about cysteine proteases in the process. Here, we detail a proteolytic activity profile from fifth larval instar to new pupae of the lepidopteran Helicoverpa armigera. At fifth to sixth instar moulting, the activities were significantly higher than those in non-moulting stages, and were inhibited by the cysteine protease inhibitor, 2S, 3S-trans-epoxysuccinyl-L-leucylamido-3-methylbutane ethyl ester (E-64), or by the cathepsin L-selective inhibitor CLIK148. Further, a 1513 bp cathepsin L cDNA (Har-CL) was isolated from the H. armigera larval cuticle and epidermis layer. Har-CL gene expression, which is correlated closely with ecdysone, was higher during larval moulting. Injection of E-64 or CLIK148 resulted in delayed fifth to sixth instar moulting, suggesting an essential role for cathepsin L in larval moulting.
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