Literature DB >> 12770497

Dietary regulation of serine proteinases that are resistant to serine proteinase inhibitors.

R M. Broadway1.   

Abstract

Ingestion of Kunitz soybean trypsin inhibitor (STI) by larval Helicoverpa zea, Agrotis ipsilon, and Trichoplusia ni extended the retention time of food in the digestive tract and increased the level of activity of proteolytic enzymes that were not susceptible to inhibition by STI. The level of enhancement of activity of STI-resistant (STI-R) enzyme(s) was directly influenced by the dosage and timing of exposure to STI. However, not all proteinase inhibitors (PIs) enhanced the level of proteinase inhibitor resistant (PI-R) enzymes, even if those PIs inhibited a significant proportion of enzyme activity. These findings suggest that a complex system may be responsible for the regulation of proteolytic enzymes in the midgut of larval Lepidoptera, and one hypothesis for this regulation is proposed.

Entities:  

Year:  1997        PMID: 12770497     DOI: 10.1016/s0022-1910(97)00028-0

Source DB:  PubMed          Journal:  J Insect Physiol        ISSN: 0022-1910            Impact factor:   2.354


  22 in total

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5.  Integrated Transcriptomic and Proteomic Analyses Suggest the Participation of Endogenous Protease Inhibitors in the Regulation of Protease Gene Expression in Helicoverpa armigera.

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7.  Functional divergence in tandemly duplicated Arabidopsis thaliana trypsin inhibitor genes.

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8.  Manipulation of endogenous trypsin proteinase inhibitor production in Nicotiana attenuata demonstrates their function as antiherbivore defenses.

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9.  Silencing geranylgeranyl diphosphate synthase in Nicotiana attenuata dramatically impairs resistance to tobacco hornworm.

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