Hybrids from equine LH: alpha enhances, beta diminishes activity.
Abstract: LH hybrids were prepared by combining eLH alpha and eLH beta with the corresponding subunits of oLH, pLH and hCG. Recombinants were isolated by gel filtration and assessed by SDS-polyacrylamide gel electrophoresis under both dissociating and non-dissociating conditions. All combinations of subunits produced hybrid LH molecules. Hybrids prepared by combining eLH beta with oLH alpha, pLH alpha or hCG alpha were very inactive in rat radioligand and Leydig cell in vitro bioassays. Hybrids prepared with eLH alpha were very active in both assays. The greatest potentiating activity was observed when eLH alpha was combined with pLH beta. The resulting hybrid was 49 times as active as pLH in stimulating steroidogenesis by Leydig cells.
Publication Date: 1985-04-01 PubMed ID: 2581829DOI: 10.1016/0303-7207(85)90159-5Google Scholar: Lookup
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- Comparative Study
- Journal Article
- Research Support
- Non-U.S. Gov't
- Research Support
- U.S. Gov't
- P.H.S.
Summary
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The research article is focused on understanding the impacts of different hybrid combinations of the hormones eLH alpha and eLH beta with oLH, pLH and hCG on stimulating steroidogenesis by Leydig cells.
Experiment Methodology
- The researchers created LH hybrids by combining eLH alpha and eLH beta with the corresponding subunits of three different LH varieties: oLH, pLH, and hCG. LH stands for luteinizing hormone, a hormone produced by gonadotropic cells in the anterior pituitary gland. In this research, ‘eLH’ refers to LH from equine sources, ‘oLH’ is from ovine (sheep), ‘pLH’ is from porcine (pig), and ‘hCG’ is human chorionic gonadotropin (a hormone produced in the human placenta).
- Once these hybrids were produced, they were isolated using a technique called gel filtration. This method is commonly used to separate proteins, nucleic acids, and small molecules in solution based on their size and charge.
- SDS-polyacrylamide gel electrophoresis, a common method for separating proteins by their electrophoretic mobility, was then utilized to assess the recombinants under both conditions, where the proteins are broken up into their component subunits (dissociating), and where they are left intact (non-dissociating).
Research Findings
- The research revealed that all combinations of subunits resulted in the formation of hybrid LH molecules. However, it was found that the bioactivity of these hybrids varied extensively depending on the combination.
- Hybrids that were prepared by combining eLH beta with oLH alpha, pLH alpha or hCG alpha were found to be very inactive in rat radioligand and Leydig cell in vitro bioassays. These bioassays are tests performed outside of a living organism in a controlled environment, and are generally used to measure the potency or concentration of a compound.
- In contrast, hybrids prepared with eLH alpha were incredibly active in both types of assays. This suggests that the presence of eLH alpha in the hybrid could substantially enhance its biological activity.
- The greatest potentiating activity was seen when eLH alpha was combined with pLH beta. In this case, the potency of the hybrid was found to be 49 times as potent as regular pLH in stimulating steroidogenesis by Leydig cells.
In summary, the hybrid molecules formed by combining different subunits of luteinizing hormone exhibit contrasting levels of bioactivity. The hybrids involving eLH alpha, particularly in combination with pLH beta, appear to be the most potent in stimulating steroidogenesis in Leydig cells. This research could deepen our understanding of Gonadotropin hormone function and provide new insights for hormone treatment strategies.
Cite This Article
APA
Bousfield GR, Liu WK, Ward DN.
(1985).
Hybrids from equine LH: alpha enhances, beta diminishes activity.
Mol Cell Endocrinol, 40(1), 69-77.
https://doi.org/10.1016/0303-7207(85)90159-5 Publication
Researcher Affiliations
MeSH Terms
- Animals
- Biological Assay
- Cells, Cultured
- Chorionic Gonadotropin / pharmacology
- Chorionic Gonadotropin, beta Subunit, Human
- Glycoprotein Hormones, alpha Subunit
- Horses / metabolism
- Leydig Cells / drug effects
- Luteinizing Hormone / pharmacology
- Male
- Peptide Fragments / pharmacology
- Pituitary Hormones, Anterior / pharmacology
- Protein Multimerization
- Rats
- Sheep / metabolism
- Species Specificity
- Steroids / biosynthesis
- Swine / metabolism
Grant Funding
- AM-09801 / NIADDK NIH HHS
- HD-18210 / NICHD NIH HHS
Citations
This article has been cited 2 times.- Bousfield GR, Butnev VY, Butnev VY, Hiromasa Y, Harvey DJ, May JV. Hypo-glycosylated human follicle-stimulating hormone (hFSH(21/18)) is much more active in vitro than fully-glycosylated hFSH (hFSH(24)).. Mol Cell Endocrinol 2014 Feb 15;382(2):989-97.
- Campbell RK, Dean-Emig DM, Moyle WR. Conversion of human choriogonadotropin into a follitropin by protein engineering.. Proc Natl Acad Sci U S A 1991 Feb 1;88(3):760-4.
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