Farnsworth R L, Talamantes F
Department of Biology, University of California, Santa Cruz, California 95064, USA.
Biol Reprod. 1998 Sep;59(3):546-52. doi: 10.1095/biolreprod59.3.546.
Placental lactogens are protein hormones produced by the placentas of many mammals. These hormones have diverse reproductive functions and are structurally similar to the pituitary hormones growth hormone and prolactin. Isolated decidual cells were previously shown to release a protein that stimulates mouse placental lactogen (mPL)-II release from mouse trophoblast cells in culture. Partial amino acid sequence data suggested that this protein shared sequence identity with mouse calcyclin. In the present study the sequence identity of this protein was determined by sequencing reverse transcription-polymerase chain reaction (RT-PCR) products. The sequence matched that of mouse calcyclin. The distribution of calcyclin message was determined in the conceptus by in situ hybridization, and a gestational profile of calcyclin mRNA was determined by Northern blot analysis. Calcyclin was localized primarily to cells that exhibited a uterine natural killer cell morphology within the decidua and to glycogen cells of the labyrinth and junctional zone. Although calcyclin was detectable by RT-PCR in midterm placentas, isolated trophoblast cells in culture did not contain detectable quantities of calcyclin by RT-PCR. Calcyclin stimulated secretion of mPL-II from isolated trophoblast cells in vitro but did not affect mPL-I secretion.
