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PROGESTERONE BINDING AND METABOLISM IN HUMAN FETAL MEMBRANES *

At term lysosomes are perturbed allowing phospholopase A2 activity which results in hydrolysis of glycerophospholipids and the release of free aranchidonic acids may be converted to prostaglandin or prostaglandin-like substances which may diffuse to the myometrium to inhibit ATP-dependent calcium ions by the sarcoplasmic reticulum and thereby initiate myometrial contractions of human labor. It is suggested that the lysosomes are perturbed by an increase in progesterone-binding substance causing progesterone withdrawal in the fetal membranes which decrease enzymes that metabolize progesterone. The progesterone withdrawal alone or with estrogen stimulation perturbs the lysosomes. Another suggestion is that progesterone-binding substance in the chorion laeve or protein-progesterone complex may perturb fetal membrane lysosomes. In either case a unique protein with high progesterone affinity appears in the fetal membranes before the onset of parturition.