Characterization of Kunitz-type protease inhibitor purified from hemolymph of Galleria mellonella larvae.

Abstract:

:We characterized a Kunitz-type protease inhibitor (Gm KTPI) obtained from the hemolymph of Galleria mellonella larvae immunized with Escherichia coli. The structural analysis of the cloned cDNA showed that it consists of 56 residues derived from the precursor of 75 amino acids. The peptide was constitutively produced in the fat bodies, but not in the midgut nor the integument of larvae. In our analysis of stage-dependent expression, its transcript was detected within the midgut, the fat bodies and the integument of the prepupae, which undergo tissue remodeling. The inhibition assays showed that Gm KTPI was capable of inhibiting only the trypsin-like activity of the larval midgut extracts. Furthermore, it was determined that Gm KTPI induced the activation of extracellular signal-regulated kinase (ERK) in the fat bodies and integument cells, and this kinase is known to perform a central role in cell proliferation signaling. Its effect on ERK activation was also verified in a control experiment using a human endothelial cell culture. Collectively, it was suggested that Gm KTPI might be responsible for the protection of other tissues against proteolytic attack by trypsin-like protease(s) from larval midgut during metamorphosis, and might play a role in the proliferation of cells in the fat body and integument.

authors

Lee JH,Kim CH,Shin YP,Park HJ,Park S,Lee HM,Kim BS,Lee IH

doi

10.1016/j.ibmb.2010.08.007

subject

Has Abstract

pub_date

2010-12-01 00:00:00

pages

873-82

issue

12

eissn

0965-1748

issn

1879-0240

pii

S0965-1748(10)00198-0

journal_volume

40

pub_type

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