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Human hepatic lipase subunit structure determination

J S Hill1, R C Davis, D Yang

  • 1Lipid Research Laboratory, West Los Angeles VA Medical Center, Los Angeles, California 90073, USA.

The Journal of Biological Chemistry
|September 13, 1996
PubMed
Summary
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This study reveals that human hepatic lipase (HL) functions as a dimer. Two HL monomer subunits are necessary for its lipolytic activity, supporting a homodimeric structure crucial for physiological function.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Enzymology

Background:

  • Human hepatic lipase (HL) plays a key role in lipid metabolism.
  • Understanding the quaternary structure of HL is essential for elucidating its physiological function.

Purpose of the Study:

  • To characterize the subunit structure and determine the functional unit of human hepatic lipase (HL).
  • To investigate the molecular basis of HL's lipolytic activity.

Main Methods:

  • Recombinant human HL expressed in Chinese hamster ovary cells.
  • Purification of HL to milligram quantities.
  • Analysis using intensity light scattering, sedimentation equilibrium, and radiation inactivation techniques.

Main Results:

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  • Intensity light scattering indicated a polypeptide molecular mass of 107 kDa, consistent with an HL dimer.
  • Sedimentation equilibrium revealed a molecular mass of 121 kDa (including carbohydrates).
  • Radiation inactivation determined the functional target size to be 109 kDa and the structural unit size to be 63 kDa, indicating a dimeric structure is required for activity.

Conclusions:

  • Human hepatic lipase (HL) exists and functions as a homodimer.
  • Two HL monomer subunits are necessary for lipolytic activity.
  • A model for active dimeric HL is proposed with implications for its physiological role.