Lipoproteins serve a vital function as transport vehicles of lipophilic biomolecules. Lipoprotein metabolism is affected by the presence of specific apoproteins and the action of lipid transfer proteins. We will employ an insect model system to study plasma lipoprotein metabolism. We plan to continue our investigation of the major hemolymph lipoprotein, lipophorin, and the role of a lipid transfer protein and a specific apolipoprotein in its metabolism. The physical properties of Manduca sexta lipid transfer particle (LTP), which catalyzes net transfer of lipid mass between isolated lipoproteins in vitro, will be determined. Characterization of the apoprotein and lipid components of this very high density lipoprotein will be performed. The requirement of individual apoproteins and the lipid component of LTP for catalysis of lipid transfer will be determined. Antibodies directed against LTP will be used to investigate its role in the mechanism of hormone-induced net uptake and non-endocytotic delivery of lipoprotein-associated lipids to tissues in vitro and in vivo. In addition, the role of LTP in mediating lipid transfer processes involved in uptake and delivery of ingested lipids during larval life will be determined. LTP will also be used as a tool to modify the lipid content of lipoproteins in order to investigate the effect of particle lipid content on apolipophorin III binding to lipophorin. The ability of free apolipophorin III to exchange with lipoprotein- bound apolipophorin III will be assessed. These studies should greatly increase our understanding of lipoprotein metabolism in insects and also provide basic information regarding pathways of lipoprotein metabolism which involve non-endocytotic transfer of lipoprotein-associated lipids to cells and from cells to lipoprotein.

Agency
National Institute of Health (NIH)
Institute
National Heart, Lung, and Blood Institute (NHLBI)
Type
Research Project (R01)
Project #
2R01HL034786-04
Application #
3348127
Study Section
Tropical Medicine and Parasitology Study Section (TMP)
Project Start
1985-09-30
Project End
1993-09-29
Budget Start
1988-09-30
Budget End
1989-09-29
Support Year
4
Fiscal Year
1988
Total Cost
Indirect Cost
Name
University of Alberta
Department
Type
DUNS #
City
Edmonton
State
AB
Country
Canada
Zip Code
T6 2E1
Blacklock, B J; Ryan, R O (1994) Hemolymph lipid transport. Insect Biochem Mol Biol 24:855-73
Zhang, Y; Lewis, R N; McElhaney, R N et al. (1993) Calorimetric and spectroscopic studies of the interaction of Manduca sexta apolipophorin III with zwitterionic, anionic, and nonionic lipids. Biochemistry 32:3942-52
Ryan, R O; Oikawa, K; Kay, C M (1993) Conformational, thermodynamic, and stability properties of Manduca sexta apolipophorin III. J Biol Chem 268:1525-30
Singh, T K; Scraba, D G; Ryan, R O (1992) Conversion of human low density lipoprotein into a very low density lipoprotein-like particle in vitro. J Biol Chem 267:9275-80
Blacklock, B J; Smillie, M; Ryan, R O (1992) Insect lipid transfer particle can facilitate net vectorial lipid transfer via a carrier-mediated mechanism. J Biol Chem 267:14033-7
Wang, J; Liu, H; Sykes, B D et al. (1992) 31P-NMR study of the phospholipid moiety of lipophorin subspecies. Biochemistry 31:8706-12
Price, H M; Ryan, R O; Haunerland, N H (1992) Primary structure of locust flight muscle fatty acid binding protein. Arch Biochem Biophys 297:285-90
Singh, T K; Blacklock, B J; Wientzek, M et al. (1992) A turbidimetric assay of lipid transfer activity. Anal Biochem 206:137-41
Ryan, R O; Kay, C M; Oikawa, K et al. (1992) Effect of particle lipid content on the structure of insect lipophorins. J Lipid Res 33:55-63
Liu, H; Ryan, R O (1991) Role of lipid transfer particle in transformation of lipophorin in insect oocytes. Biochim Biophys Acta 1085:112-8

Showing the most recent 10 out of 26 publications