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Structural studies on lipophorin, an insect lipoprotein.

J P Shapiro, P S Keim, J H Law

    The Journal of Biological Chemistry
    |March 25, 1984
    PubMed
    Summary

    Insect lipophorin, a high-density lipoprotein, was isolated and its apolipoproteins characterized. ApoLp-I and ApoLp-II exhibit distinct amino acid compositions and environmental exposures, crucial for understanding lipid transport in Manduca sexta.

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    Area of Science:

    • Biochemistry
    • Insect Physiology
    • Lipid Metabolism

    Background:

    • Lipophorin is a vital insect high-density lipoprotein.
    • It plays a key role in lipid transport within insect hemolymph.

    Purpose of the Study:

    • To isolate and characterize insect lipophorin from Manduca sexta.
    • To analyze the properties of its constituent apolipoproteins, apoLp-I and apoLp-II.

    Main Methods:

    • Rapid isolation of lipophorin using density gradient ultracentrifugation.
    • Dissociation and separation of apolipoproteins via guanidine HCl treatment and gel permeation chromatography.
    • Immunological characterization using electrophoretic blots and double immunodiffusion tests.

    Main Results:

    • Lipophorin was successfully isolated from larval Manduca sexta hemolymph.
    • Two apolipoproteins, apoLp-I (Mr = 245,000) and apoLp-II (Mr = 78,000), were identified and separated.
    • ApoLp-I and apoLp-II showed no immunological cross-reactivity and distinct amino acid compositions, particularly in tryptophan and cysteine content.
    • ApoLp-I appears more exposed to the aqueous environment than apoLp-II.

    Conclusions:

    • Insect lipophorin's apolipoproteins have distinct biochemical properties.
    • These differences likely influence their roles in lipid transport and lipophorin structure.
    • Findings provide insights into the molecular mechanisms of insect lipid transport.

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