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Extracellular serine protease cascades have evolved in vertebrates and invertebrates to mediate a rapid defense response to wounding and infection. We have been investigating the enzyme system and its regulation by serine protease homologs (SPHs) and inhibitors (serpins) in a biochemical model insect, Manduca sexta. In collaboration with Dr. Kanost's group at Kansas State University, we are studying proteolytic activation of phenoloxidase (PO), Spӓtzle, and stress responsive peptide (SRP) precursors. PO catalyzes the formation of reactive compounds to kill pathogens and encapsulate parasites with a melanin sheath. Spӓtzle binds to Toll receptor to induce synthesis of antimicrobial peptides and other factors. SRPs block growth, cause hemocyte spreading, and stimulate immune signaling.
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Insect Biochemistry and Molecular Biology (2024)
Insect Biochemistry and Molecular Biologypp.104108, (2024)
Insect biochemistry and molecular biologypp.104108-104108, (2024)
Frontiers in immunology (2023): 1244792
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SCIENCE ADVANCESno. 51 (2023): eadk2756-eadk2756
Genesno. 3 (2022): 446-446
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