The expression of human apolipoprotein E in tobacco hornworm larvae ca
uses a dramatic change in the buoyant density of the insect's endogeno
us lipoproteins. Larvae without apoE have lipoproteins that are found
exclusively in the high-density range. Baculovirus-mediated apoE expre
ssion results in the conversion of approximately one-fourth of the end
ogenous lipoproteins to low-density species. This density conversion i
s progressive and parallels a similar change in apoE density distribut
ion. ApoE is secreted from the lipoprotein producing fat body tissue i
n a lipid-poor form, but readily associates with circulating insect li
poproteins in the hemolymph where the density conversion takes place.
Analysis of the buoyant lipoprotein particles indicates that they cont
ain apoE and insect apolipophorins I and II with few or no other prote
ins present. Immunoprecipitation of apolipophorins I and II results in
coprecipitation of apoE. This association is disrupted by detergent,
consistent with the three proteins sharing the same lipoprotein partic
les. The ability of apoE to influence buoyant lipoprotein formation in
an invertebrate system leads us to suggest that small apolipoproteins
such as apoE may play a role in buoyant lipoprotein production in mam
mals.