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Related Experiment Video

Updated: May 17, 2026

Sampling Human Indigenous Saliva Peptidome Using a Lollipop-Like Ultrafiltration Probe: Simplify and Enhance Peptide Detection for Clinical Mass Spectrometry
08:37

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Characterization of Δ7/11, a functional prolactin-binding protein.

J M Fleming1, E Ginsburg, C W McAndrew

  • 1Mammary Biology and Tumorigenesis Laboratory, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892, USA. jodie.fleming@nccu.edu

Journal of Molecular Endocrinology
|October 11, 2012
PubMed
Summary
This summary is machine-generated.

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This study identifies a novel prolactin receptor (PrlR) splice variant, Δ7/11, that binds prolactin. This interaction inhibits prolactin-driven breast cell proliferation and alters cell cycle regulation.

Area of Science:

  • Endocrinology
  • Molecular Biology
  • Cancer Research

Background:

  • Prolactin is vital for mammary gland development and influences tumor progression.
  • Soluble prolactin receptor (PrlR) isoforms act as prolactin-binding proteins, modulating prolactin availability.
  • The specific role of the Δ7/11 PrlR splice variant in prolactin interaction and cellular function remains uncharacterized.

Purpose of the Study:

  • To investigate the direct interaction between prolactin and the Δ7/11 PrlR splice variant.
  • To elucidate the biochemical properties and functional consequences of this interaction on breast epithelial cells.

Main Methods:

  • Proximity ligation assay and immunoprecipitation to confirm prolactin-Δ7/11 binding.
  • Biochemical analysis of Δ7/11 glycosylation, cellular localization, and secretion.

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Published on: July 5, 2021

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Last Updated: May 17, 2026

Sampling Human Indigenous Saliva Peptidome Using a Lollipop-Like Ultrafiltration Probe: Simplify and Enhance Peptide Detection for Clinical Mass Spectrometry
08:37

Sampling Human Indigenous Saliva Peptidome Using a Lollipop-Like Ultrafiltration Probe: Simplify and Enhance Peptide Detection for Clinical Mass Spectrometry

Published on: August 7, 2012

Direct Detection of Isolevuglandins in Tissues Using a D11 scFv-Alkaline Phosphatase Fusion Protein and Immunofluorescence
06:33

Direct Detection of Isolevuglandins in Tissues Using a D11 scFv-Alkaline Phosphatase Fusion Protein and Immunofluorescence

Published on: July 5, 2021

  • Analysis of Δ7/11 expression in human serum, milk, and breast tumor tissues.
  • Functional assays assessing the impact of Δ7/11 on prolactin-induced cell proliferation and cell cycle arrest.

    • Main Results:

    • Δ7/11 directly binds prolactin.
    • Δ7/11 is heavily glycosylated, influencing its localization and secretion.
    • Low levels of Δ7/11 were found in serum, but not human milk; detected in some breast tumors without correlation to demographics.
    • Δ7/11 inhibits prolactin-induced breast cell proliferation and modifies prolactin's effect on cell cycle arrest/senescence.

    Conclusions:

    • Δ7/11 represents a novel prolactin-binding protein.
    • This variant acts as a regulatory mechanism for prolactin bioavailability and signaling.
    • Δ7/11's inhibitory effects on proliferation and cell cycle modulation offer new insights into prolactin's role in breast health and disease.