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Research article summary (published 29 Sep 2009):

Characterization of the trypsin-like protease (Ha-TLP2) constitutively expressed in the integument of the cotton bollworm, Helicoverpa armigera.

Full Abstract

Trypsins belong to the serine endoproteases. They are the most important proteases in insects because of their key roles in food digestion and zymogens activation. But there has been little study of the trypsins in the integuments of insects. In this work, we cloned a trypsin-like protease gene from Helicoverpa armigera and named it trypsin-like protease 2 (Ha-TLP2). Semi-quantitative reverse transcription PCR analysis showed that Ha-TLP2 is constitutively expressed in the integument and can be down-regulated by 20-hydroxyecdysone (20E) and up-regulated by the juvenile hormone (JH) analog methoprene. Immunohistochemistry showed that Ha-TLP2 is located not only in the epidermis, but also in new and old cuticles. Immunoblotting and gelatin-SDS-PAGE revealed that Ha-TLP2 is constitutively expressed with activity in the integument during larval feeding, molting, and metamorphosis. This evidence suggests that Ha-TLP2 is involved in the remodeling of the integument.

 

Author information

Author/s: Liu, Yang (Y); Sui, Yi-Peng (YP); Wang, Jin-Xing (JX); Zhao, Xiao-Fan (XF);

Affiliation: School of Life Sciences, Shandong University, Jinan 250100, Shandong, China.

Journal and publication information

Publication Type: Journal Article; Research Support, Non-U.S. Gov't

Journal: Archives of insect biochemistry and physiology (Arch Insect Biochem Physiol), published in United States. (Language: eng)

Reference: 2009-Oct; vol 72 (issue 2) : pp 74-87

Dates: Created 2009/09/09; Completed 2009/10/28;

PMID: 19557747, status: MEDLINE (last retrieval date: 10/28/2009, IMS Date: )

Sourced from the National Library of Medicine. Abstract text and other information may be subject to copyright.

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MeSH headings (categories)

This article was linked to the MESH Headings shown below.

Associated Chemicals: Insect Proteins (0) ; Trypsin (EC 3.4.21.4)

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