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Growth hormones. 1. Polymorphism (minireview).

J Charrier1, J Martal

  • 1Station de Physiologie Animale, I.N.R.A., Montpellier, France.

Reproduction, Nutrition, Developpement
|January 1, 1988
PubMed
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Human growth hormone (GH) exists as diverse molecular variants, including mass and charge variations. These GH variants, along with binding proteins, influence hormone activity and half-life.

Area of Science:

  • Endocrinology
  • Molecular Biology
  • Biochemistry

Background:

  • Pituitary growth hormone (GH) is not a single entity but a collection of molecular variants.
  • The 22 K variant is the predominant form, serving as a reference for other GH forms.
  • GH variants exhibit polymorphism, differing in molecular weight and electrophoretic mobility.

Purpose of the Study:

  • To explore the polymorphism of human growth hormone (GH).
  • To classify and describe various GH variants, including mass and charge variants.
  • To discuss less understood GH forms and their implications.

Main Methods:

  • Classification of GH variants based on molecular weight (mass variants) and electrophoretic mobility (charge variants).
  • Discussion of bioinactive and bioactive GH forms.

Related Experiment Videos

  • Consideration of the SV-hGH-2 variant and its potential role in human placental growth hormone (hPGH) synthesis.

    • Main Results:

    • GH variants are broadly categorized into mass variants (aggregated and non-aggregated) and charge variants.
    • Bioinactive GH (detected by RIA but lacking activity) and bioactive GH (lacking immunoreactivity) represent distinct entities.
    • The SV-hGH-2 variant may function as an isohormone and is potentially involved in hPGH synthesis, which takes over from pituitary GH during pregnancy.
    • GH molecules bind to carrier proteins, forming a reservoir and extending the hormone's biological half-life.

    Conclusions:

    • Human GH exhibits significant molecular polymorphism, impacting its biological activity.
    • Understanding GH variants is crucial for comprehending hormone function and regulation.
    • The interplay between GH variants, hPGH, and binding proteins highlights the complexity of GH physiology.