Src is a non-receptor protein tyrosine kinase ubiquitously expressed in animals. It is involved
in various cellular processes, including the innate immune response in mammals. However,
less is known about the function of insect Src. Here we presented a homologue of Src in silkworm
(Bombyx mori), named as BmSrc by phylogenetic analysis, homologous comparison and domain
prediction. BmSrc contains the conserved phosphorylation residues and possesses tyrosine kinase
activity. The expression pattern of BmSrc mRNA was specific in developmental stages and tissues.
The highest expression of BmSrc was detected in moth stage, and the gonads showed the highest
expression during larval stage. We then found over-expression of BmSrc in BmE cell resulted in an
increase of p38 mitogen-activated protein kinase (p38 MAPK) and Akt phosphorylation but a decrease
in extracellular signal–regulated kinase (ERK) phosphorylation. Finally, we demonstrated that
BmSrc promoted the production of antimicrobial peptides (AMPs). These results implied that BmSrc
is involved in immune response of silkworm possibly through activating p38 MAPK and Akt signaling
pathway. Our study may provide reference for further investigation of the biological function of
BmSrc in Bombyx mori.
Keywords: Src, p38 MAPK, ERK, Akt, antimicrobial peptide, silkworm.
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