Abstract
[3H]PAF binding parameters (affinity constants and binding capacities) were estimated for endometrial membranes obtained on days 3 (when the morulae first enter the gravid uterus), 4, 5 and on day 6, about 22 h before the blastocyst becomes irremovably attached to the endometrium. The two-site receptor system which characterized the binding on a large proportion of purified membranes from days 3 (60%) and 6 (75%) had the following parameters: day 3, K(d)1 (nM) 0.15 ± 0.04, B(max)1 (pmol/mg protein) 0.04 ± 0.01; K(d)2 (nM) 17.60 ± 6.40, B(max)2 (pmol/mg protein) 2.92 ± 0.91 (n = 6), and day 6, K(d)1 (nM) 0.33 ± 0.06, B(max)1 (pmol/mg protein) 0.11 ± 0.02; K(d)2 (nM) 7.42 ± 1.02, B(max)2 (pmol/mg protein) 1.75 ± 0.31 (n = 3). The remaining membranes, including all preparations of days 4 and 5, exhibited only one class of binding sites which were unlike the putative type 1 PAF receptor. The most significant observations were the apparent pregnancy-associated changes in the parameters of the PAF binding sites. However, regardless of the type of PAF binding exhibited, all the binding sites bound GTP. [3H]PAF dissociation from bound complexes was biphasic at 25°C. The rate constants were k-1, 0.27 ± 0.09 min-1 and k-2, 3.45 ± 1.19 x 10-3 min-1, for the rapid and slow dissociating components, respectively. In view of the inability to resolve the experimental data from days 4 and 5 into multiple sites, and of the occurrence of receptor interconversions on days 3 and 6, it is postulated that there may be cell membrane macromolecular reorganization/remodeling of proteins and cytoskeleton as a result of the arrival of blastocyst in the uterus and/or the dynamic interplay of local uterine PAF and the hormonal milieux during the peri-implantation period of pregnancy.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 271-288 |
| Number of pages | 18 |
| Journal | Journal of Lipid Mediators |
| Volume | 5 |
| Issue number | 3 |
| State | Published - 1992 |
ASJC Scopus subject areas
- Immunology
- Pharmacology
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