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1996
DOI: 10.1303/aez.31.135
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Signal Transudation for Cecropin B Gene Expression in Adherent Hemocytes of the Silkworm, Bombyx mori (Lepidoptera: Bombycidae)

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Cited by 15 publications
(8 citation statements)
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“…PKA isotypes affect a myriad of cellular functions in invertebrates, including insects 32 , 33 , 34 . Haemocytes of the silkworm Bombyx mori require an unidentified PKA isotype to produce cecropins (antibacterial proteins) 35 , 36 . Based on the use of H‐89, an inhibitor of PKA isotypes, a type of PKA may limit G. mellonella haemocyte adhesion 8 .…”
Section: Discussionmentioning
confidence: 99%
“…PKA isotypes affect a myriad of cellular functions in invertebrates, including insects 32 , 33 , 34 . Haemocytes of the silkworm Bombyx mori require an unidentified PKA isotype to produce cecropins (antibacterial proteins) 35 , 36 . Based on the use of H‐89, an inhibitor of PKA isotypes, a type of PKA may limit G. mellonella haemocyte adhesion 8 .…”
Section: Discussionmentioning
confidence: 99%
“…Divalent calcium, cyclic AMP and G-proteins lead to cecropin gene activation in Bombyx mori hemocytes (Choi et al, 1995). Such gene activation did not require tyrosine kinase or Ca 2+ /calmodulin-dependent kinase (Shimabukuro et al, 1996;Foukas et al, 1998). Peptidoglycan and lipopolysaccharides induced cecropin B synthesis by pathways involving protein kinase A and C but not by myosin light chain kinase .…”
Section: Introductionmentioning
confidence: 92%
“…17) Furthermore, factors involved in signal transduction for induction of antimicrobial peptide gene expression have also been analyzed in specific tissues. 17,19) Recently, two novel antimicrobial peptides have been identified from B. mori. First, an Enbocin gene was cloned using a partial cDNA fragment detected by differential hybridization as a probe.…”
mentioning
confidence: 99%