Abstract:
:Lipid transfer particle (LTP) is present in hemolymph of the tobacco hornworm Manduca sexta. Biosynthesis of LTP, occurrence in hemolymph, and the role of LTP-apoproteins in the lipid transfer reaction were investigated using antibodies specific for LTP or for each of the apoproteins. In vitro protein synthesis followed by immunoprecipitation demonstrated that LTP is synthesized by the fat body and secreted into the medium. In contrast to apolipophorin III, an exchangeable apoprotein of lipophorin (the major lipid transport protein in hemolymph), apoLTP-III could not be detected free in hemolymph. LTP concentrations in the hemolymph were measured by a sandwich ELISA using a mouse monoclonal antibody against apoLTP-III as capturing antibody and rabbit polyclonal antibody against apoLTP-I as detecting antibody. LTP concentration increased during the late fifth instar larval stage, followed by a decrease in the wandering stage. Subsequently, LTP concentrations were strongly increased in hemolymph of adult moths. The role of the three apoproteins of LTP in the lipid transfer reaction was analyzed using apoprotein-specific antibodies. All three, apoLTP-I, -II, and -III, appeared to be important for lipid transfer activity, as shown by inhibition of lipid transfer by antibodies specific for each of the three apoproteins.
journal_name
Arch Insect Biochem Physioljournal_title
Archives of insect biochemistry and physiologyauthors
Van Heusden MC,Yepiz-Plascencia GM,Walker AM,Law JHdoi
10.1002/(SICI)1520-6327(1996)31:1<39::AID-ARCH3>3.subject
Has Abstractpub_date
1996-01-01 00:00:00pages
39-51issue
1eissn
0739-4462issn
1520-6327pii
10.1002/(SICI)1520-6327(1996)31:1<39::AID-ARCH3>3.journal_volume
31pub_type
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