Isolation and cloning of Ser4, a gene encoding a trypsin-like serine protease in Drosophila melanogaster

Ahrens, Jeffrey E.; Mahoney, Paul A.

doi:10.1016/s0167-4781(97)00146-2

Cited by 5 publications

(3 citation statements)

References 11 publications

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“…A trypsin-like serine protease is expressed at a high level in the larval gut in Drosophila melanogaster , suggesting its role in food digestion (Ahrens & Mahoney, 1998). In Lygus lineolaris , the main proteinases that exist in the gut and salivary glands are serine proteinases, especially trypsins (Zhu et al ., 2003).…”

Section: Introductionmentioning

confidence: 99%

The impacts of classical insect hormones on the expression profiles of a new digestive trypsin‐like protease (TLP) from the cotton bollworm, Helicoverpa armigera

Sui

Wang

Zhao

2009

Insect Molecular Biology

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Trypsin proteinases perform important roles in the protein digestion of an insect midgut. A 1042 bp fulllength cDNA was cloned from Helicoverpa armigera . The gene encoded a 32 kDa protein, with a predicted isoelectric point of 5.7. The amino acid sequence of the protein had a trypsin-like serine protease domain, and the gene was named Ha-TLP . The expression of the gene was tissue-specific and the transcript of Ha-TLP existed only in the midgut and was not found in the head-thorax, integument, fat body and haemocytes from 5th instar larvae, with similar expression levels between those in feeding larvae and in molting larvae. In the midgut, the gene transcription level declined from 6th instar 72 h after the larvae entered the wandering stage, and disappeared from 6th instar at 96 h until the pupal stage. By immunohistochemistry, Ha-TLP was detected in the cytoplasm of the midgut epithelial cells of the 6th instar feeding stage worms. The expression of Ha-TLP could be up-regulated by a juvenile hormone (JH) analog methoprene and down-regulated by 20-hydroxyecdysone (20E). These facts indicate that Ha-TLP was involved in food digestion during larval growth and probably up-regulated by JH and suppressed by extra 20E in vivo .

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Section: Introductionmentioning

confidence: 99%

The impacts of classical insect hormones on the expression profiles of a new digestive trypsin‐like protease (TLP) from the cotton bollworm, Helicoverpa armigera

Sui

Wang

Zhao

2009

Insect Molecular Biology

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“…BBI does indeed slow growth and development when fed to certain species of insects (Murdock et al ., 1987); however, we still do not know: (1) the receptors involved in detecting the presence of the inhibitor (if there are any); (2) the mechanism(s) that result in decreasing or abolishing the expression of susceptible proteases; (3) the mechanism(s) that cause the respective increases or ‘de novo’ synthesis of nonsusceptible or alternative proteases; (4) if BBI impacts cellular processes in insects beyond just the expression of proteases; or (5) is it possible to disrupt any of the aforementioned processes in order to make insects more susceptible to BBI? Drosophila melanogaster (Meigen) (hereafter referred to as Drosophila ) has been used as a model system for understanding the genetics, genomics and proteomics of physiological phenomena, including digestion (Ahrens & Mahoney, 1998; Ross et al ., 2003). Thus, new knowledge of the proteins and genes involved in the response of Drosophila to BBI may shed light on the molecular mechanisms by which digestive tissues respond to this dietary protease inhibitor.…”

Section: Introductionmentioning

confidence: 99%

Changes in Drosophila melanogaster midgut proteins in response to dietary Bowman–Birk inhibitor

Margam

Muir

et al. 2007

Insect Molecular Biology

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The midgut proteome of Drosophila melanogaster was compared in larvae fed dietary Bowman-Birk inhibitor (BBI) vs. larvae fed a control diet. By using two-dimensional gel electrophoresis, nine differentially expressed proteins were observed, which were associated with enzymes or transport functions such as sterol carrier protein X (SCPX), ubiquitin-conjugating enzyme, endopeptidase, receptor signalling protein kinase, ATP-dependent RNA helicase and alpha-tocopherol transport. Quantitative real-time PCR verified differential expression of transcripts coding for six of the proteins observed from the proteomic analysis. BBI evidently affects expression of proteins associated with protein degradation, transport and fatty acid catabolism. We then tested the hypothesis that SCPX was critical for the Drosophila third instars' response to BBI treatment. Inhibition of SCPX caused the third instars to become more susceptible to dietary BBI.

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“…Most reports of trypsins in insects focus on their protein digestion function in midgut, because they are the major midgut digestive enzymes for dietary proteins in many insects (Kunkel et al, 1985). Different trypsins have been reported in the midguts of Aedes aegypti (Noriega et al, 1996), Drosophila melanogaster (Ahrens and Mahoney, 1998), and Plodia interpunctella (Zhu et al, 2000). All are involved in food protein degradation.…”

Section: Introductionmentioning

confidence: 99%

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

Liu

Sui

Wang

et al. 2009

Arch Insect Biochem Physiol

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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.

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Isolation and cloning of Ser4, a gene encoding a trypsin-like serine protease in Drosophila melanogaster

Cited by 5 publications

References 11 publications

The impacts of classical insect hormones on the expression profiles of a new digestive trypsin‐like protease (TLP) from the cotton bollworm, Helicoverpa armigera

The impacts of classical insect hormones on the expression profiles of a new digestive trypsin‐like protease (TLP) from the cotton bollworm, Helicoverpa armigera

Changes in Drosophila melanogaster midgut proteins in response to dietary Bowman–Birk inhibitor

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

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