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

Prolactin binding in rat Langerhans islets.

M Tesone, R M Oliveira-Filho, E H Charreau

    Journal of Receptor Research
    |January 1, 1980
    PubMed
    Summary

    Female rat islet cells possess specific binding sites for ovine prolactin (oPrl), primarily in membrane fractions. These sites are crucial for prolactin

    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

    Correction: Stat3 regulates ErbB-2 expression and co-opts ErbB-2 nuclear function to induce miR-21 expression, PDCD4 downregulation and breast cancer metastasis.

    Oncogene·2024
    Same author

    Correction: MiR-16 mediates trastuzumab and lapatinib response in ErbB-2-positive breast and gastric cancer via its novel targets CCNJ and FUBP1.

    Oncogene·2023
    Same author

    Correction: Targeting ErbB-2 nuclear localization and function inhibits breast cancer growth and overcomes trastuzumab resistance.

    Oncogene·2023
    Same author

    Gamma secretase inhibitor impairs epithelial-to-mesenchymal transition induced by TGF-β in ovarian tumor cell lines.

    Molecular and cellular endocrinology·2016
    Same author

    Sphingosine-1-phosphate restores endothelial barrier integrity in ovarian hyperstimulation syndrome.

    Molecular human reproduction·2016
    Same author

    Peripheral and Central Mechanisms Involved in the Hormonal Control of Male and Female Reproduction.

    Journal of neuroendocrinology·2016

    Area of Science:

    • Endocrinology
    • Cell Biology
    • Pancreatic Islet Research

    Background:

    • Prolactin (Prl) is a hormone with diverse physiological roles.
    • The endocrine pancreas, specifically Langerhans islets, plays a critical role in glucose homeostasis.
    • Investigating hormone-receptor interactions within islet cells is key to understanding pancreatic function.

    Purpose of the Study:

    • To investigate the presence and characteristics of prolactin binding sites on pancreatic islet cell membranes.
    • To determine the specificity and affinity of these potential prolactin receptors.
    • To explore the implications of prolactin-islet cell interaction in normal and diabetic states.

    Main Methods:

    • Preparation of membrane fractions from collagenase-dispersed Langerhans islets of Wistar rats.
    • Binding assays using 125I-labelled ovine prolactin (125I-oPrl).
    • Characterization of binding kinetics (saturation, time, temperature, displacement) and receptor properties (Scatchard analysis, enzymatic digestion).
    • Assessment of binding in islets from streptozotocin-induced diabetic rats.

    Main Results:

    • Specific binding sites for 125I-oPrl were identified in membrane preparations of female rat islets, with negligible binding in males.
    • Binding was saturable, time- and temperature-dependent, reaching equilibrium at 16h and 0°C.
    • The 12,000 g pellet contained over 80% of specific binding sites.
    • Prolactin binding was not displaced by other pituitary hormones (FSH, LH, GH).
    • Scatchard analysis indicated a single class of binding sites with a high affinity (Ka = 0.21 x 10(10)M-1).
    • Protein and phospholipid components were essential for receptor activity, as evidenced by reduced binding after trypsin or phospholipase C treatment.
    • A significant reduction in binding sites was observed in islets from streptozotocin-diabetic rats.

    Conclusions:

    • Langerhans islets of female rats possess specific, high-affinity membrane-bound receptors for prolactin.
    • These receptors are protein and phospholipid in nature and are localized predominantly in the 12,000 g fraction.
    • The reduced number of prolactin binding sites in diabetic rat islets suggests a potential role for prolactin in pancreatic islet function and its alteration in diabetes.
    • These findings support the hypothesis that prolactin may exert direct effects on the endocrine pancreas via specific membrane interactions.

    Related Experiment Videos