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Structure and structure-function relationships in glycoprotein hormones

J G Pierce, M R Faith, L C Giudice

    Ciba Foundation Symposium
    |January 1, 1976
    PubMed
    Summary
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    The tertiary structures of glycoprotein hormone subunits (TSH, LH, hCG, FSH) remain unclear. Studies on partial reduction reveal conserved disulfide bonds and similar tertiary structures among beta-subunits, aiding in understanding hormone function.

    Area of Science:

    • Biochemistry
    • Endocrinology
    • Protein Chemistry

    Background:

    • The structural relationships of thyrotropin (TSH), lutropin (LH), human choriogonadotropin (hCG), and follitropin (FSH) are established.
    • Each beta-subunit has six disulfide bonds, showing homology across these hormones.
    • Major questions persist regarding the tertiary structures of these subunits and their interactions.

    Purpose of the Study:

    • To investigate the tertiary structures of glycoprotein hormone alpha- and beta-subunits.
    • To identify disulfide bridges and understand subunit interactions in TSH, LH, hCG, and FSH.
    • To explore intermediates formed during partial reduction and their potential for reassembly.

    Main Methods:

    • Partial reduction of LH and TSH beta-subunits followed by cysteine labeling.

    Related Experiment Videos

  • Analysis of disulfide bond reduction patterns under various conditions.
  • Preliminary experiments on reoxidation and recombination of reduced alpha-subunits with native beta-subunits.

    • Main Results:

    • A single, conserved disulfide bond is preferentially reduced first in LH and TSH beta-subunits.
    • Chemical data suggest similar tertiary structures for different beta-subunits.
    • Reoxidized alpha-subunits can recombine with native beta-subunits to form biologically active TSH or LH.

    Conclusions:

    • Partial reduction provides insights into the conserved tertiary structures of glycoprotein hormone beta-subunits.
    • The alpha-subunit can be reoxidized and retain its ability to form active hormones with beta-subunits.
    • Further studies on chemical modifications and structural analysis are crucial for a complete understanding.