Lipopolysaccharide-lipophorin complex formation in insect hemolymph: a common pathway of lipopolysaccharide detoxification both in insects and in mammals

ISSN:
0965-1748
Keywords:
Antibacterial protein ; Cecropin ; Endotoxin ; Insect immunity
Source:
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
Topics:
Biology
Type of Medium:
Electronic Resource
URL:
_version_ 1798292140579618816
autor Kato, Y.
Motoi, Y.
Taniai, K.
Kadono-Okuda, K.
Yamamoto, M.
Higashino, Y.
Shimabukuro, M.
Chowdhury, S.
Xu, J.
Hiramatsu, M.
Sugiyama, M.
Yamakawa, M.
autorsonst Kato, Y.
Motoi, Y.
Taniai, K.
Kadono-Okuda, K.
Yamamoto, M.
Higashino, Y.
Shimabukuro, M.
Chowdhury, S.
Xu, J.
Hiramatsu, M.
Sugiyama, M.
Yamakawa, M.
book_url http://linkinghub.elsevier.com/retrieve/pii/0965-1748(94)90090-6
datenlieferant nat_lic_papers
fussnote The formation of the lipophorin-lipopolysaccharide (LPS) complex in Bombyx mori hemolymph and its role in LPS detoxification were explored. LPS, an antibacterial protein inducer in insects, was injected into B. mori larvae. Analytical density gradient ultracentrifugation revealed that after injection the LPS peak shifts to a zone of lower density with time. The shifted peak was identified as the lipophorin-LPS complex. This complex formation was also achieved in an in vitro mixture of cell-free hemolymph and LPS at 25^oC but not at 1^oC. The lipophorin-LPS complex had a significantly lower capacity to elicit the mRNA of cecropin B, an antibacterial protein. The biological activity of reextracted LPS from the complex was slightly reduced in the Limulus test and no structural modification was observed in sodium dodecylsulfate-polyacrylamide gel electrophoresis (SDS-PAGE). These results suggested that the formation of lipophorin-LPS strikingly reduces the cecropin inducibility of LPS without any structural change in LPS. Similar serum lipoprotein-LPS complex formation and reduction of biological activities of LPS were also observed in mammals. We, therefore, suggest that the formation of the serum lipoprotein-LPS complex is a common pathway to inactive LPS both in insects and in mammals.
hauptsatz hsatz_simple
identnr NLZ187431442
issn 0965-1748
journal_name Insect Biochemistry and Molecular Biology
materialart 1
package_name Elsevier
publikationsort Amsterdam
publisher Elsevier
reference 24 (1994), S. 547-555
schlagwort Antibacterial protein
Cecropin
Endotoxin
Insect immunity
search_space articles
shingle_author_1 Kato, Y.
Motoi, Y.
Taniai, K.
Kadono-Okuda, K.
Yamamoto, M.
Higashino, Y.
Shimabukuro, M.
Chowdhury, S.
Xu, J.
Hiramatsu, M.
Sugiyama, M.
Yamakawa, M.
shingle_author_2 Kato, Y.
Motoi, Y.
Taniai, K.
Kadono-Okuda, K.
Yamamoto, M.
Higashino, Y.
Shimabukuro, M.
Chowdhury, S.
Xu, J.
Hiramatsu, M.
Sugiyama, M.
Yamakawa, M.
shingle_author_3 Kato, Y.
Motoi, Y.
Taniai, K.
Kadono-Okuda, K.
Yamamoto, M.
Higashino, Y.
Shimabukuro, M.
Chowdhury, S.
Xu, J.
Hiramatsu, M.
Sugiyama, M.
Yamakawa, M.
shingle_author_4 Kato, Y.
Motoi, Y.
Taniai, K.
Kadono-Okuda, K.
Yamamoto, M.
Higashino, Y.
Shimabukuro, M.
Chowdhury, S.
Xu, J.
Hiramatsu, M.
Sugiyama, M.
Yamakawa, M.
shingle_catch_all_1 Kato, Y.
Motoi, Y.
Taniai, K.
Kadono-Okuda, K.
Yamamoto, M.
Higashino, Y.
Shimabukuro, M.
Chowdhury, S.
Xu, J.
Hiramatsu, M.
Sugiyama, M.
Yamakawa, M.
Lipopolysaccharide-lipophorin complex formation in insect hemolymph: a common pathway of lipopolysaccharide detoxification both in insects and in mammals
Antibacterial protein
Cecropin
Endotoxin
Insect immunity
Antibacterial protein
Cecropin
Endotoxin
Insect immunity
0965-1748
09651748
Elsevier
shingle_catch_all_2 Kato, Y.
Motoi, Y.
Taniai, K.
Kadono-Okuda, K.
Yamamoto, M.
Higashino, Y.
Shimabukuro, M.
Chowdhury, S.
Xu, J.
Hiramatsu, M.
Sugiyama, M.
Yamakawa, M.
Lipopolysaccharide-lipophorin complex formation in insect hemolymph: a common pathway of lipopolysaccharide detoxification both in insects and in mammals
Antibacterial protein
Cecropin
Endotoxin
Insect immunity
Antibacterial protein
Cecropin
Endotoxin
Insect immunity
0965-1748
09651748
Elsevier
shingle_catch_all_3 Kato, Y.
Motoi, Y.
Taniai, K.
Kadono-Okuda, K.
Yamamoto, M.
Higashino, Y.
Shimabukuro, M.
Chowdhury, S.
Xu, J.
Hiramatsu, M.
Sugiyama, M.
Yamakawa, M.
Lipopolysaccharide-lipophorin complex formation in insect hemolymph: a common pathway of lipopolysaccharide detoxification both in insects and in mammals
Antibacterial protein
Cecropin
Endotoxin
Insect immunity
Antibacterial protein
Cecropin
Endotoxin
Insect immunity
0965-1748
09651748
Elsevier
shingle_catch_all_4 Kato, Y.
Motoi, Y.
Taniai, K.
Kadono-Okuda, K.
Yamamoto, M.
Higashino, Y.
Shimabukuro, M.
Chowdhury, S.
Xu, J.
Hiramatsu, M.
Sugiyama, M.
Yamakawa, M.
Lipopolysaccharide-lipophorin complex formation in insect hemolymph: a common pathway of lipopolysaccharide detoxification both in insects and in mammals
Antibacterial protein
Cecropin
Endotoxin
Insect immunity
Antibacterial protein
Cecropin
Endotoxin
Insect immunity
0965-1748
09651748
Elsevier
shingle_title_1 Lipopolysaccharide-lipophorin complex formation in insect hemolymph: a common pathway of lipopolysaccharide detoxification both in insects and in mammals
shingle_title_2 Lipopolysaccharide-lipophorin complex formation in insect hemolymph: a common pathway of lipopolysaccharide detoxification both in insects and in mammals
shingle_title_3 Lipopolysaccharide-lipophorin complex formation in insect hemolymph: a common pathway of lipopolysaccharide detoxification both in insects and in mammals
shingle_title_4 Lipopolysaccharide-lipophorin complex formation in insect hemolymph: a common pathway of lipopolysaccharide detoxification both in insects and in mammals
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source_archive Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
timestamp 2024-05-06T08:43:47.169Z
titel Lipopolysaccharide-lipophorin complex formation in insect hemolymph: a common pathway of lipopolysaccharide detoxification both in insects and in mammals
titel_suche Lipopolysaccharide-lipophorin complex formation in insect hemolymph: a common pathway of lipopolysaccharide detoxification both in insects and in mammals
The formation of the lipophorin-lipopolysaccharide (LPS) complex in Bombyx mori hemolymph and its role in LPS detoxification were explored. LPS, an antibacterial protein inducer in insects, was injected into B. mori larvae. Analytical density gradient ultracentrifugation revealed that after injection the LPS peak shifts to a zone of lower density with time. The shifted peak was identified as the lipophorin-LPS complex. This complex formation was also achieved in an in vitro mixture of cell-free hemolymph and LPS at 25^oC but not at 1^oC. The lipophorin-LPS complex had a significantly lower capacity to elicit the mRNA of cecropin B, an antibacterial protein. The biological activity of reextracted LPS from the complex was slightly reduced in the Limulus test and no structural modification was observed in sodium dodecylsulfate-polyacrylamide gel electrophoresis (SDS-PAGE). These results suggested that the formation of lipophorin-LPS strikingly reduces the cecropin inducibility of LPS without any structural change in LPS. Similar serum lipoprotein-LPS complex formation and reduction of biological activities of LPS were also observed in mammals. We, therefore, suggest that the formation of the serum lipoprotein-LPS complex is a common pathway to inactive LPS both in insects and in mammals.
topic W
uid nat_lic_papers_NLZ187431442