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Related Experiment Videos

Prolactin isoforms secreted by human prolactinomas.

T Hoffmann1, G Gunz, T Brue

  • 1Laboratoire de Neuroendocrinologie Expérimentale, INSERM U 297, Marseille, France.

Hormone Research
|January 1, 1992
PubMed
Summary

Human prolactinoma cells secrete a major nonglycosylated prolactin (NG-hPRL) variant. This NG-hPRL form exhibits higher immunoreactivity and bioactivity compared to glycosylated prolactin (G-hPRL) isoforms.

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Area of Science:

  • Endocrinology
  • Molecular Biology
  • Biochemistry

Background:

  • Prolactinomas are pituitary tumors that secrete prolactin (PRL).
  • Understanding PRL isoforms is crucial for diagnosing and treating these tumors.
  • Heterogeneity in PRL structure can affect its biological function.

Purpose of the Study:

  • To purify and characterize human prolactin (hPRL) isoforms from prolactinoma cells.
  • To compare the immunoreactivity and bioactivity of different hPRL variants.
  • To identify the predominant hPRL isoform secreted by prolactinomas.

Main Methods:

  • Gel filtration chromatography for initial purification.
  • Lectin affinity chromatography to separate glycosylated and nonglycosylated forms.

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  • Gel electrophoresis to analyze molecular weight and identify isoforms.
  • Endoglycosidase treatment to assess carbohydrate chain heterogeneity.

    • Main Results:

    • Nonglycosylated hPRL (NG-hPRL) was the major secreted form.
    • Three glycosylated hPRL (G-hPRL) isoforms (G1-, G2-, G3-hPRL) were identified, differing in carbohydrate chains.
    • NG-hPRL demonstrated significantly higher immunoreactivity (68% less) and bioactivity (50% less) compared to G-hPRL forms.
    • NG-hPRL had an apparent molecular weight of 23,000 (M(r)), while G-hPRL forms had a molecular weight of 25,000 (M(r)).

    Conclusions:

    • The primary prolactin variant secreted by prolactinomas is the nonglycosylated form.
    • Glycosylation of hPRL leads to reduced immunoreactivity and bioactivity.
    • These findings contribute to understanding prolactin heterogeneity in disease states.