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Squirrel monkey corticosteroid-binding globulin: primary structure and comparison with the human protein

G L Hammond1, C L Smith, P Lähteenmäki

  • 1Department of Obstetrics and Gynecology, University of Western Ontario, London, Canada.

Endocrinology
|February 1, 1994
PubMed
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Squirrel monkey corticosteroid-binding globulin (CBG) forms dimers and has low glucocorticoid affinity. Recombinant squirrel monkey CBG produced in CHO cells confirmed these properties, with dimerization influenced by an additional threonine residue but not low steroid binding.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Primate Genetics

Background:

  • Corticosteroid-binding globulin (CBG) plays a crucial role in regulating glucocorticoid bioavailability.
  • Squirrel monkey CBG exhibits unique dimerization and low steroid-binding affinity compared to human CBG.
  • Understanding structural and functional differences in CBG is vital for comprehending steroid hormone regulation.

Purpose of the Study:

  • To characterize the molecular properties of squirrel monkey corticosteroid-binding globulin (CBG).
  • To investigate the structural basis for squirrel monkey CBG's dimerization and low glucocorticoid affinity.
  • To compare squirrel monkey CBG with human CBG using recombinant expression systems.

Main Methods:

  • Analysis of squirrel monkey CBG cDNAs to determine amino acid sequence and identify conserved domains.

Related Experiment Videos

  • Expression of cDNAs for human and squirrel monkey CBGs in Chinese hamster ovary (CHO) cells.
  • Comparison of physico-chemical properties, including dimerization and steroid-binding affinity, of natural and recombinant CBG proteins.
  • Site-directed mutagenesis to assess the role of specific amino acid residues (e.g., threonine at position 144) in CBG properties.

    • Main Results:

    • Squirrel monkey CBG precursor is 406 amino acids, with the mature form comprising 384 amino acids.
    • Recombinant squirrel monkey CBG produced in CHO cells forms dimers and exhibits low cortisol-binding affinity (5-8 fold lower than human CBG).
    • An additional threonine residue at position 144 in squirrel monkey CBG contributes to dimerization but not low steroid-binding affinity.

    Conclusions:

    • Squirrel monkey CBG naturally circulates as a dimer with significantly lower glucocorticoid affinity than human CBG.
    • Recombinant expression in CHO cells successfully recapitulates the dimeric structure and low steroid-binding affinity of squirrel monkey CBG.
    • The additional threonine residue is implicated in squirrel monkey CBG's dimerization propensity, highlighting specific structural adaptations influencing its function.