Prostaglandin F2alpha specific binding in equine corpora lutea.
Abstract: Preliminary studies indicate the presence of PGF2alpha specific binding sites in membrane fractions prepared from equine corpora lutea. The equilibrium binding data indicate an apparent dissociation constant of 3.2 X 10(-9)M and the concentration of binding sites of -0.1 pmoles/mg membrane protein. Competition of several natural prostaglandins for equine luteal PGF2alpha specific binding sites indicates specificity for the 9alpha-hydroxyl moiety and the 5,6-cis doublebond. Significant increases in relative binding affinities were demonstrated for PGF2alpha analogs with a phenyl ring introduced at carbons 16 or 17. Specific PGF2alpha binding was demonstrated in corpora lutea collected at known stages of the estrous cycle. There was no pattern in these values based on the stage of the cycle. While specific 3H-PGE1 binding could be demonstrated, no high affinity sites could be quantitated. 3H-PGE1 binding appeared unaffected by changes in temperature or time of incubation, whereas PGF2alpha specific binding was significantly modified by both these factors.
Publication Date: 1977-03-01 PubMed ID: 557809DOI: 10.1016/0090-6980(77)90032-6Google Scholar: Lookup
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- Journal Article
Summary
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This study primarily investigates the presence of Prostaglandin F2alpha (PGF2alpha) specific binding sites in equine corpora lutea and how this binding is impacted by various factors and conditions. Prostaglandins play an essential role in the reproductive physiology of mammals.
Prostaglandin F2alpha Binding Sites
- The research pre-emptively shows the existence of specific PGF2alpha binding sites in the membrane sections prepared from the equine corpora lutea, a temporary endocrine gland in mammals’ ovaries.
- The calculated dissociation constant, reflecting binding affinity, is 3.2 X 10(-9)M, demonstrating a high affinity between the PGF2alpha and its receptor.
- The concentration of these specific binding sites is about -0.1 picomoles per milligram of membrane protein.
- The competition of varied natural prostaglandins for these specific binding sites exhibits specificity for the 9alpha-hydroxyl entity and the 5,6-cis double bond.
- The binding affinities considerably increase for PGF2alpha analogs when a phenyl ring gets introduced at carbon positions 16 or 17.
- PGF2alpha specific binding is detected in corpora lutea collected at known stages of the estrous cycle, reflecting differing hormone levels depending on the stage of the reproductive cycle.
- However, no specific pattern relating to the cycle stage and binding values is indicated. This suggests that the stage of the reproductive cycle may not significantly affect the binding ability of PGF2alpha to its receptor.
- Specific binding of another prostaglandin, 3H-PGE1, could also be demonstrated, but no high affinity sites could be quantified for this prostaglandin, indicating a lower binding affinity compared to PGF2alpha.
- 3H-PGE1 binding seems to be unaffected by alterations in temperature or incubation time. However, PGF2alpha specific binding significantly modifies according to changes in these factors, suggesting that the binding of PGF2alpha to its receptor is temperature and time-sensitive.
Competition and Specificity
Effects of Estrous Cycle and Temperature
Cite This Article
APA
Kimball FA, Wyngarden LJ.
(1977).
Prostaglandin F2alpha specific binding in equine corpora lutea.
Prostaglandins, 13(3), 553-564.
https://doi.org/10.1016/0090-6980(77)90032-6 Publication
Researcher Affiliations
MeSH Terms
- Animals
- Binding Sites
- Binding, Competitive
- Cell Membrane / metabolism
- Corpus Luteum / metabolism
- Estrus
- Female
- Horses
- Pregnancy
- Prostaglandins F / metabolism
- Temperature
Citations
This article has been cited 1 times.- Segabinazzi LGTM, Roberts BN, Peterson EW, Ambrosia R, Bergfelt D, Samper J, French H, Gilbert RO. Early Pregnancy in Jennies in the Caribbean: Corpus Luteum Development and Progesterone Production, Uterine and Embryo Dynamics, Conceptus Growth and Maturation. Animals (Basel) 2022 Jan 6;12(2).
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