In 1861, Ito and Higashi discovered in human placentae a biological active protein which had prolactin like activity with a pigeon crop sac assay. In 1962, Josimovich and MacLaren, using an immunodiffusion gel technique, demonstrated that the serum of pregnant women contained a lactogenic protein which had immunologically partial identity with pituitary growth hormone. They named this protein, “human placental lactogen (HPL).”
Kaplan and Grumbach isolated this protein also and have suggested “chorionic growth hormone prolactin (CGP)” as its name.
In this paper the first term or HPL (Human Chorionic Somatomammotropin) will be used as the name of this protein. Several investigators have studied the chemical and biological character, and dynamic behavior of HPL during pregnancy. But the specific biological character of this protein has not yet been clarified.
It is the purpose of this paper to report the studies on the systematic anrd detailed analysis of biological charactesitics of this protein hormone.
HPL was extracted by modified Friesen's method from term placentae and was purified by gel filtration, ion exchange cellulose chromatography and DEAE-Sephadex A50 chromatography. The purified HPL (HPL-Kobe) developed a single band by 7% polyacrylamide disc electrophoresis and its molecular weight was about 20,000. The immunological character of this HPL showed evidence of partial identity with human growth hormone but antigenicity was not identical with human chorionic gonadotropin. It showed no cross-reaction with prolactin and human sera.
Crude HPL mobilized the FFA and blood glucose in serum in vivo and in the incubation medium in vitro and it also promoted the increase of glucose and insulin, and accelerated the activitities of hormone sensitive lipase (HSL) and lipoprotein lipase (LPL) in epididymal fat pads of rats of Wistar strain.
The biological character was also studied for its lipolytic action on rat epididymal fat pad in vitro. The addition of epinephrine (10 μg per ml), caffeine (0.01 M per ml), cyclic 3', 5' AMP (Iml per ml) or single HPL (30 μg per ml) to the incubation medium released nearly equal amounts of FFA. But combination of HPL (30 μg per ml and 3 μg per ml) with caffeine (0.01 M per ml) gave an enhanced release of FFA and activated HSL and LPL also. When adrenergic blockers (Dibenamine 3 μg per ml and Inderal 30 μg per ml) were added in combination with HPL, HSL and LPL activities were markedly lowered, but release of FFA was not so remarkably influenced. In this experiment with castrated male rats injected with estrogen 1 μg per 100 g body weight for 4 days or progesterone 1 mg per loog body weight for 4 days, the release of FFA was more remarkably accelerated by HPL administration in progesterone sensitized fat pad in vitro but estrogen had no influence. Injection of reserpine (100 μg per 100 g) had no effect on the release of FFA. When pregnant rats were injected with HPL, FFA, insulin and glucose markedly promoted to increase in the maternal blood and at the same time FFA in fetal blood increased significantly, and insulin and glucose remained the same. The above-mentioned findings indicate that HPL acts on maternal tissue to abtive adenyl cyclase and accelerate lipolysis via cyclic AMP.
From these experimental results, the auther may be able to conclude that human placental lactogen is a very important endocrine factor which influences the metabolism of fat and carbohydrate in the “feto-placental maternal system, ” especially promotes the fetal growth via peculiar changes of maternal metabolism during pregnancy.
View full abstract