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Circulatory lipid transport: lipoprotein assembly and function from an evolutionary perspective.

Dick J Van der Horst1, Sigrid D Roosendaal, Kees W Rodenburg

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Molecular and Cellular Biochemistry
|January 9, 2009
PubMed
Summary

Lipid transport in animals uses large lipid transfer proteins (LLTPs). Insect high-density lipophorin (HDLp) recycles lipids, unlike mammalian low-density lipoprotein (LDL), showcasing evolutionary adaptations in lipid carriers.

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Area of Science:

  • Evolutionary biology
  • Biochemistry
  • Comparative physiology

Background:

  • Circulatory transport of neutral lipids in animals relies on large lipid transfer proteins (LLTPs), including apolipoprotein B (apoB) in mammals and apolipophorin II/I (apoLp-II/I) in insects.
  • These proteins are crucial for assembling lipoproteins, acquiring lipids via microsomal triglyceride transfer protein (MTP), and binding them through amphipathic structures.

Purpose of the Study:

  • To compare the evolution, structure, and function of lipid transport systems in mammals and insects.
  • To elucidate the unique lipid delivery and recycling mechanisms of insect high-density lipophorin (HDLp) compared to mammalian low-density lipoprotein (LDL).

Main Methods:

  • Comparative analysis of LLTP superfamily members across different animal species.
  • Characterization of insect apoLp-II/I processing and its role in HDLp formation.
  • Investigation of HDLp-lipophorin receptor (LpR) interactions, including binding affinities and dissociation properties at varying pH and ionic conditions.
  • Analysis of mutant and hybrid receptors to define ligand-receptor binding interactions.

Main Results:

  • Insect apoLp-II/I is cleaved by furin, forming two apolipoproteins in HDLp, distinct from mammalian apoB.
  • Insect HDLp functions as a reusable lipid shuttle, capable of reloading lipids, unlike mammalian LDL which undergoes lysosomal degradation after uptake.
  • The HDLp-LpR complex exhibits remarkable stability, resisting dissociation at endosomal pH and EDTA treatment, suggesting a mechanism for lipoprotein recycling.
  • Specific binding interactions between the HDLp ligand and the ligand-binding domain of LpR were characterized.

Conclusions:

  • Lipid transport systems in mammals and insects show significant structural and functional adaptations shaped by evolution.
  • The recycling mechanism of insect HDLp, facilitated by a stable HDLp-LpR complex, represents a key evolutionary divergence from mammalian lipoprotein metabolism.
  • Understanding these differences provides insights into the diverse strategies animals employ for lipid homeostasis.