Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

A serum prolactin-binding protein: implications for growth hormone.

P S Dannies1

  • 1Dept of Pharmacology, Yale School of Medicine, New Haven, CT 06520-8066, USA.

Trends in Endocrinology and Metabolism: TEM
|November 10, 2001
PubMed
Summary

A newly identified serum protein, similar to the prolactin receptor's extracellular domain, may influence growth hormone binding. This research investigates its impact on growth hormone and prolactin biological activities.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Misfolded growth hormone causes fragmentation of the Golgi apparatus and disrupts endoplasmic reticulum-to-Golgi traffic.

Journal of cell science·2001
Same author

Concentrating hormones into secretory granules: layers of control.

Molecular and cellular endocrinology·2001
Same author

Acquisition of Lubrol insolubility, a common step for growth hormone and prolactin in the secretory pathway of neuroendocrine cells.

The Journal of biological chemistry·2000
Same author

Accumulation of synaptosomal-associated protein of 25 kDa (SNAP-25) and other proteins associated with the secretory pathway in GH4C1 cells upon treatment with estradiol, insulin, and epidermal growth factor.

Endocrinology·2000
Same author

Autosomal dominant growth hormone (GH) deficiency type II: the Del32-71-GH deletion mutant suppresses secretion of wild-type GH.

Endocrinology·2000
Same author

Protein folding and deficiencies caused by dominant-negative mutants of hormones.

Vitamins and hormones·2000

Area of Science:

  • Endocrinology
  • Molecular Biology
  • Protein Chemistry

Background:

  • Soluble forms of membrane receptors, including the prolactin receptor's extracellular domain, are found in circulation.
  • A serum protein exhibiting characteristics of the human prolactin receptor's extracellular domain has been identified.

Discussion:

  • The extracellular domain of the prolactin receptor is known to bind human growth hormone.
  • Investigating the effect of this serum protein on circulating growth hormone binding is crucial.
  • Assessing the extent of the serum protein's influence on the biological activities of growth hormone and prolactin is warranted.

Key Insights:

  • Identified a serum protein resembling the prolactin receptor's extracellular domain.
  • Poses the question of this protein's impact on growth hormone binding.

Related Experiment Videos

  • Raises the possibility of significant modulation of growth hormone and prolactin functions.

    • Outlook:

    • Further studies are needed to quantify the binding affinity and biological consequences.
    • Elucidating the precise role of this serum protein in endocrine regulation.
    • Potential therapeutic implications for growth hormone and prolactin related disorders.