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J. Biol. Chem., Vol. 276, Issue 14, 11100-11112, April 6, 2001
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From the Biochemistry Laboratory, The Institute of Low Temperature
Science, Hokkaido University, Sapporo, Japan 060-0819
Pro-phenoloxidase (proPO) in insects is
implicated in the defense against microbes and wounding. The presence
of proPO in the cuticle was suggested more than 30 years ago, but it
has not been purified. The extract of cuticles of the silkworm,
Bombyx mori, was shown to contain two proPO isoforms
(F-type and S-type proPOs, which have slightly different mobilities in
polyacrylamide gel electrophoresis under nondenaturing conditions). The
two isoforms were purified to homogeneity. From hemolymph of the same
insect, two types of proPO with the same electrophoretic mobilities as those of cuticular isoforms were separated and were shown to be different at five amino acid residues in one of their subunits. The
isoforms in the hemolymph and cuticle were activated by a specific
activating enzyme. The resulting active phenoloxidases exhibited almost
the same substrate specificities and specific activities toward
o-diphenols. The substrate specificities and the
susceptibilities to inhibitors, including carbon monoxide, indicated
that the purified proPO isoforms were not zymogens of laccase-type
phenoloxidase. The proPO in hemolymph was shown to be transported to
the cuticle. This demonstration was corroborated by the failure to
detect proPO transcripts by Northern analysis of total RNA from
epidermal cells. In reversed-phase column chromatography, cuticular and
hemolymph proPOs gave distinct elution profiles, indicating that some
yet to be identified modification occurs in hemolymph proPO and results
in the formation of cuticular proPO. There was little transportation of
cuticular proPO to the cuticle when it was injected into the hemocoel.
The nature of the modification is described in the accompanying paper
(Asano, T., and Ashida, M. (2001) J. Biol. Chem. 276, 11113-11125).
Cuticular Pro-phenoloxidase of the Silkworm, Bombyx
mori
PURIFICATION AND DEMONSTRATION OF ITS TRANSPORT FROM
HEMOLYMPH*
*
This work was supported in part by Grants 09265201 and
06454023 from the Japan Ministry of Education, Science, Sports, and Culture.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed. Tel.:
81-11-706-6877; Fax: 81-11-706-7142; E-mail:
ashida@pop.lowtem.hokudai.ac.jp.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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