Lipoprotein-mediated lipid transport in insects: analogy to the mammalian lipid carrier system and novel concepts for the functioning of LDL receptor family members.
In all animals, lipoproteins are used to transport lipids through the aqueous circulation. Lipids are delivered to mammalian cells by two different mechanisms: via endocytic uptake of the complete lipoprotein particle mediated by members of the low density lipoprotein (LDL) receptor (LDLR) family, or by selective delivery of lipoprotein-carried lipids at the cell surface, such as lipid uptake following the action of a lipoprotein lipase. Although many structural elements of the lipid transport system of insects are similar to those of mammals, insect lipoprotein-mediated lipid transport was thought to apply only to the latter concept, since the single lipoprotein acts as a reusable lipid shuttle. However, the recent identification of lipoprotein receptors of the LDLR family in insects suggests that lipid transport in these animals may also adopt the first concept. Yet, the endocytic properties of the insect LDLR homologue appear to deviate from those of the mammalian LDLR family members, resulting in the recycling of endocytosed lipoprotein in a transferrin-like manner. This indicates that a hitherto unknown as well as unexpected function can be added to the plethora of functions of LDLR family members. Analysis of the molecular mechanism of the ligand-recycling function of the insect receptor provides also new insight into the possible functioning of the mammalian family members. In the last several years, mammalian and insect lipoprotein-mediated lipid transport systems have been reviewed separately with respect to functioning and lipid delivery. This review, in which new and important developments in the insect field with respect to our understanding of lipid delivery are discussed with a particular focus on the involvement of the LDLR homologue, aims at comparing the two systems, also from an evolutionary biological perspective, and proposes that the two systems are more similar than assumed previously.
Rodenburg
Kees W
KW
Department of Biochemical Physiology, Faculty of Biology and Institute of Biomembranes, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands. k.w.rodenburg@bio.uu.nl
Van der Horst
Dick J
DJ
D000595:Amino Acid Sequence; D000818:Animals; D001692:Biological Transport / Q000502:physiology; D006801:Humans; D007313:Insecta / Q000737:chemistry / Q000378:metabolism* / Q000502:physiology; D050356:Lipid Metabolism; D008074:Lipoproteins / Q000737:chemistry / Q000502:physiology*; D008969:Molecular Sequence Data; D011973:Receptors, LDL / Q000502:physiology*
D008074:Lipoproteins; D011973:Receptors, LDL