Direct demonstration of intrinsic follicle-stimulating hormone receptor-binding activity in acid-treated equine luteinizing hormone.
Abstract: After dissociating equine gonadotropins as a function of time at pH 3, we examined them by radioligand assay and sodium dodecyl sulfate polyacrylamide gel electrophoresis under nondissociating conditions (low, 0.1% SDS). Equine follicle-stimulating hormone (FSH) rapidly lost its receptor-binding activity, and low SDS-polyacrylamide gels demonstrated dissociation into subunits. Maximum dissociation occurred after 20-30 min of pH 3 incubation. Equine luteinizing hormone (LH), however, retained most biologic activity and was largely intact after 72 h of pH 3 incubation. Dose-response curves of acid-treated equine LH and FSH and intact equine LH and FSH were compared in five types of radioligand receptor assays. LH and FSH receptor-binding activities of equine LH were unaffected by pH 3. Equine LH showed 19- and 32-times more activity in the rat testis FSH assay than it did in chicken or horse FSH assays, respectively, directly demonstrating the intrinsic FSH receptor-binding activity of equine LH and the relative lack of specificity for these hormone preparations of the rat FSH receptor. Acid-treated 95% of its biologic activity in FSH assays. In LH assays, the slight (0.2%) activity of equine FSH was relatively unaffected by acid treatment, suggesting that contamination by equine LH accounts for this activity.
Publication Date: 1986-03-14 PubMed ID: 3004606DOI: 10.1016/0167-4889(86)90248-xGoogle Scholar: Lookup
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- 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 focuses on the effects of acid-treatment on the follicle-stimulating hormone receptor-binding activity of equine luteinizing hormone. It was found that equine luteinizing hormone retains these binding abilities even after being subjected to acidic conditions, providing insights into its intrinsic activity and potential specificity for certain receptor assays.
Experiments and Methods
- The scientists studied equine gonadotropins as they were dissociated over time in an acidic environment (pH 3).
- The process of dissociation was followed using techniques like radioligand assay and sodium dodecyl sulfate polyacrylamide gel electrophoresis under conditions that discourage further dissociation.
- The hormones under investigation were equine follicle-stimulating hormone (FSH) and equine luteinizing hormone (LH).
Findings
- Equine FSH quickly lost its ability to bind with receptor after it was exposed to the acidic environment. The dose-response curves also exhibited significant difference in equine FSH’s receptor-binding activity pre- and post acid treatment.
- Equine LH, on the other hand, showed a surprising resilience to the acidic conditions. It retained most of its biological activity even after 72 hours of incubation in the acidic medium.
- The LH and FSH receptor-binding activity of equine LH remained unaffected, indicating a certain robustness in how equine LH interacts with receptors, regardless of the environmental conditions.
Comparative Analysis
- When comparing the dose-response curves of acid-treated equine LH and FSH with their integral counterparts, the researchers found significant differences in their receptor-binding activities.
- In rat testis FSH assay, equine LH showed activity 19 and 32 times greater than its activity in assays using chicken or horse FSH respectively. This shows the intrinsic FSH receptor-binding activity of equine LH. It also implies that the rat FSH receptor has relative lack of specificity for these horse hormone.
Additional Observations
- While 95% of equine FSH lost its biological activity in FSH assays post acid treatment, its relatively insignificant activity (0.2%) in LH assays remained largely unaffected. This led to the suggestion that this remaining activity might be due to contamination by equine LH.
Cite This Article
APA
Bousfield GR, Ward DN.
(1986).
Direct demonstration of intrinsic follicle-stimulating hormone receptor-binding activity in acid-treated equine luteinizing hormone.
Biochim Biophys Acta, 885(3), 327-334.
https://doi.org/10.1016/0167-4889(86)90248-x Publication
Researcher Affiliations
MeSH Terms
- Animals
- Chickens
- Electrophoresis, Polyacrylamide Gel
- Follicle Stimulating Hormone / analysis
- Follicle Stimulating Hormone / metabolism
- Horses / metabolism
- Hydrogen-Ion Concentration
- Luteinizing Hormone / analysis
- Male
- Radioligand Assay
- Rats
- Receptors, Cell Surface / metabolism
- Receptors, FSH
- Testis
Grant Funding
- AM09801 / NIADDK NIH HHS
- HD18210 / NICHD NIH HHS
Citations
This article has been cited 2 times.- Cahoreau C, Klett D, Combarnous Y. Structure-function relationships of glycoprotein hormones and their subunits' ancestors. Front Endocrinol (Lausanne) 2015;6:26.
- Gordon WL, Bousfield GR, Ward DN. Comparative binding of FSH to chicken and rat testis. J Endocrinol Invest 1989 Jun;12(6):383-92.
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