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Related Experiment Videos

Multiple interactions between pituitary hormones and the mannose receptor.

D Z Simpson1, P G Hitchen, E L Elmhirst

  • 1Glycobiology Institute, Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, U.K.

The Biochemical Journal
|October 8, 1999
PubMed
Summary

The macrophage mannose receptor binds pituitary hormones via its cysteine-rich domain, recognizing sulphated N-acetylgalactosamine (SO(4)-4GalNAc). Carbohydrate-recognition domains (CRDs) also contribute to hormone binding through interactions with other sugars.

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Area of Science:

  • Immunology
  • Endocrinology
  • Glycobiology

Background:

  • The macrophage mannose receptor (MMR) is crucial for innate immunity.
  • MMR also clears pituitary hormones by recognizing sulphated terminal N-acetylgalactosamine (SO(4)-4GalNAc) residues.
  • Previous research suggested the SO(4)-4GalNAc binding site is in the N-terminal cysteine-rich domain, separate from the C-type carbohydrate-recognition domains (CRDs).

Purpose of the Study:

  • To characterize the binding of natural pituitary hormones to different domains of the mannose receptor.
  • To investigate the role of the cysteine-rich domain and CRDs in hormone binding specificity.
  • To elucidate the molecular interactions involved in pituitary hormone clearance by MMR.

Main Methods:

  • Utilized soluble forms of the mannose receptor: full extracellular domain and a truncated form lacking the N-terminal cysteine-rich domain and fibronectin type II repeat.

Related Experiment Videos

  • Assessed high-affinity, saturable binding of lutropin and thyrotropin to both receptor forms.
  • Analyzed the influence of pH, ionic strength, SO(4)-4GalNAc, and mannose on binding interactions.

    • Main Results:

    • Both receptor forms exhibited high-affinity, saturable binding to lutropin and thyrotropin.
    • Full-length receptor binding was pH/ionic strength-dependent, inhibited by SO(4)-4GalNAc and partially by mannose.
    • Truncated receptor binding was also pH/ionic strength-dependent but inhibited by mannose, not SO(4)-4GalNAc.

    Conclusions:

    • The cysteine-rich domain of the mannose receptor possesses a specific SO(4)-4GalNAc binding site.
    • Interactions between other hormone sugars and the CRDs are also significant for pituitary hormone binding.
    • These findings refine our understanding of MMR's role in hormone clearance and innate immunity.