Binding of placental lactogen and growth hormone to fetal sheep fibroblasts

John Fowlkes, Michael Freemark

Research output: Contribution to journalArticlepeer-review

10 Scopus citations


Growth hormone (GH) regulates growth and development in the postnatal period but lacks somatotropic activity in the fetus. In contrast, the placental hormone placental lactogen (PL) stimulates amino acid transport, DNA synthesis, and somatomedin production in isolated fetal tissues, suggesting that PL may function as a “fetal GH.” To elucidate the mechanisms by which PL exerts GH-like effects in fetal tissues, we examined the binding of PL, GH, and prolactin to cultured skin fibroblasts obtained from midgestational fetal lambs. Ovine fetal fibroblasts bound radiolabeled ovine PL (oPL) specifically and with high affinity (EC50 0.20 nM). In competitive displacement assays using125I-oPL as the radioligand, the potency of unlabeled oPL was eight to 12 times greater than that of ovine GH and1000 times greater than that of ovine prolactin. Covalent cross-linking of125I-oPL (22 kD) to ovine fetal fibroblasts revealed a specific hormone-receptor complex with an apparent Mr of 130 000, suggesting that the high affinity oPL binding site has a molecular mass of approximately 108 kD. The specific bindings of radiolabeled ovine GH (0.6% per 250 fig protein) and ovine prolactin (0.04% per 250 μg protein) were only1/15 and ‘/ho that of radiolabeled oPL (9.1% per 250 μg protein), and no specific cross-linking of125I-ovine GH or125I-ovine prolactin to ovine fetal fibroblasts was detected. These findings demonstrate preferential binding of PL by isolated fetal sheep fibroblasts in culture, providing a cellular mechanism whereby PL may exert growth-promoting effects in the fetus.

Original languageEnglish
Pages (from-to)200-203
Number of pages4
JournalPediatric Research
Issue number2
StatePublished - Aug 1992

ASJC Scopus subject areas

  • Pediatrics, Perinatology, and Child Health


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