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Three-dimensional structures of gonadotropins

J W Lustbader1, S Pollak, L Lobel

  • 1Columbia University, College of Physicians and Surgeons, New York 10032, USA.

Molecular and Cellular Endocrinology
|December 20, 1996
PubMed
Summary
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Researchers developed a novel isotope-labeling medium for Chinese hamster ovary cells, enabling structural determination of biologically active human chorionic gonadotropin (hCG) and other glycoproteins.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Glycoprotein Research

Background:

  • Secreted proteins, including human chorionic gonadotropin (hCG), are often glycosylated, posing challenges for structural determination via crystallography due to carbohydrate heterogeneity.
  • Chemical deglycosylation (e.g., HF treatment) yields non-biologically active hCG with altered subunit interactions, necessitating methods to study the native, active hormone.

Purpose of the Study:

  • To develop a method for determining the structure of biologically active, glycosylated hCG and its subunits in solution.
  • To overcome limitations of crystallographic studies for heterogeneous glycoproteins.

Main Methods:

  • Development of a universal, nonradioactive isotope-labeling medium enriched in carbon-13 (13C) and nitrogen-15 (15N).
  • Expression of uniformly labeled hCG in Chinese hamster ovary (CHO) cells.

Related Experiment Videos

  • Biochemical, immunochemical, and biological activity comparisons of recombinant hCG with urinary hCG.
  • Mass spectrometry and preliminary NMR structural analysis of labeled hCG.

    • Main Results:

    • Uniform isotope labeling (over 90% incorporation) of recombinant hCG and its subunits was achieved using the developed medium.
    • Isotopically labeled hCG and its subunits were biochemically, immunochemically, and biologically indistinguishable from native urinary hCG.
    • Preliminary NMR data confirmed uniform labeling sufficient for structural studies.

    Conclusions:

    • The developed 13C and 15N-enriched labeling medium is a technological advancement enabling structural determination of biologically active glycoproteins, including hCG.
    • This method facilitates the study of other challenging glycoproteins unsuitable for crystallographic analysis.