Source:http://linkedlifedata.com/resource/pubmed/id/15475296
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
10
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pubmed:dateCreated |
2004-10-11
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pubmed:abstractText |
Apolipophorin-III (apoLp-III) is a hemolymph protein whose function is to facilitate lipid transport in an aqueous medium. Recently, apoLp-III in Galleria mellonella larvae was shown to play an unexpected role in insect immune activation. We identified the cDNA sequence of Hyphantria cunea apoLp-III by oligonucleotide-primed amplification, and 5'- and 3'-RACE PCR. Since H. cunea has an unusually low level of apoLp-III in the hemolymph, a recombinant apoLp-III was overexpressed using a baculovirus expression system to investigate its biological activity. Recombinant apoLp-III and/or Escherichia coli were injected into the hemocoel of last instar larvae, and the expression of antimicrobial peptide from fat body was determined by Northern blot. Injection of apoLp-III as well as E. coli induced slight up-regulation of its transcription rate in fat body, whereas the expression of antimicrobial peptide was dramatically induced by the injection of apoLp-III and E. coli. H. cunea hemocytes had apoLp-III in the granules and expressed its transcript, albeit at a much lower level than in the fat body. Upon bacterial injection, a subpopulation of hemocytes showed degranulation and degradation. Local discharge of apoLp-III from hemocytes caused by the injection of E. coli might be related to the immune response through an unknown mechanism.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Apolipoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Insect Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/apolipophorin III
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0965-1748
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
34
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1011-23
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:15475296-Amino Acid Sequence,
pubmed-meshheading:15475296-Animals,
pubmed-meshheading:15475296-Apolipoproteins,
pubmed-meshheading:15475296-Base Sequence,
pubmed-meshheading:15475296-DNA, Complementary,
pubmed-meshheading:15475296-Escherichia coli,
pubmed-meshheading:15475296-Genes, Insect,
pubmed-meshheading:15475296-Hemocytes,
pubmed-meshheading:15475296-Insect Proteins,
pubmed-meshheading:15475296-Microscopy, Immunoelectron,
pubmed-meshheading:15475296-Molecular Sequence Data,
pubmed-meshheading:15475296-Moths,
pubmed-meshheading:15475296-RNA, Messenger,
pubmed-meshheading:15475296-Recombinant Proteins
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pubmed:year |
2004
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pubmed:articleTitle |
Immune activation of apolipophorin-III and its distribution in hemocyte from Hyphantria cunea.
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pubmed:affiliation |
Division of Applied Life Science, Gyeongsang National University, Chinju 660 701, South Korea.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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