Purification and characterization of mouse decidual calcyclin: a novel stimulator of mouse placental lactogen-II secretion.

The effects of secretagogue(s) from mouse decidual tissue on the release of mouse placental lactogen-II (mPL-II) were studied. Decidual tissue was obtained from 10- and 11-day-pregnant mice. The tissue was homogenized, extracted, and the tissue extract was made 50% saturated with ammonium sulfate. Both the precipitate and supernatant were tested for their ability to stimulate mPL-II release from cultured trophoblasts. The supernatant contained an activity to stimulate the release of mPL-II. This activity was further purified using column chromatography. The purification resulted in isolation of a protein with a mol wt of 20 K as estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis under nonreducing conditions and 6 K under reducing conditions. Further characterization of this protein showed that it binds calcium and has an amino acid sequence that is highly homologous with calcyclin expressed in mouse embryonic fibroblast cells and with calcyclin from other species. This protein was designated mouse decidual calcyclin. Antiserum was raised against the purified decidual calcyclin for development of an RIA and for immunoblots. Western blots of various mouse tissue extracts and mouse serum from different physiological stages showed that the concentration of calcyclin was highest in decidual tissue. Detectable levels were found in extracts from trophoblast, lung, and stomach, but the concentrations in these tissues were about 100 times lower than in decidua. Decidual calcyclin was not detectable in mouse serum. Cultured decidual cells released calcyclin into the medium. On average, this release was about 7.8 ng/micrograms DNA.24 h. The rate of release did not change significantly during 4 days of culture. The ratio of calcyclin in cells per calcyclin released during 24 h averaged 2.3 and did not change significantly during the culture period. The purified decidual calcyclin stimulated the release of mPL-II from cultured trophoblasts in a dose-dependent manner at concentrations from 0.01 to 1 microgram/ml. The maximum stimulation averaged about 1.5 times above control. It is concluded that decidual calcyclin may be of physiological importance for the regulation of mPL-II secretion.

[1]  L. Murphy,et al.  Identification of a serum-inducible messenger RNA (5B10) as the mouse homologue of calcyclin: tissue distribution and expression in metastatic, ras-transformed NIH 3T3 cells. , 1990, Cell growth & differentiation : the molecular biology journal of the American Association for Cancer Research.

[2]  C. Heizmann,et al.  Calcium-binding protein from mouse Ehrlich ascites-tumour cells is homologous to human calcyclin. , 1989, The Biochemical journal.

[3]  P. Chomczyński,et al.  Cloning and characterization of mouse growth hormone-releasing hormone (GRH) complementary DNA: increased GRH messenger RNA levels in the growth hormone-deficient lit/lit mouse. , 1989, Molecular endocrinology.

[4]  K. Christy,et al.  Modifications for SDS-PAGE of proteins. , 1989, BioTechniques.

[5]  C. Kordon,et al.  LHRH-like immunoreactivity in the human placenta is not identical to LHRH , 1989 .

[6]  K. Yoshinaga,et al.  Immunoreactive growth hormone-releasing hormone in rat placenta. , 1988, Endocrinology.

[7]  L. Murphy,et al.  Cloning and characterization of a cDNA encoding a highly conserved, putative calcium binding protein, identified by an anti-prolactin receptor antiserum. , 1988, The Journal of biological chemistry.

[8]  Z. Hochberg,et al.  Two pathways of placental lactogen secretion by cultured human trophoblast. , 1988, Biochemical medicine and metabolic biology.

[9]  D. Hilt,et al.  The S 100 protein family , 1988 .

[10]  F. Talamantes,et al.  Development of a placental cell culture system for studying the control of mouse placental lactogen II secretion. , 1987, Placenta.

[11]  J. Kuźnicki,et al.  Purification and properties of a novel Ca2+-binding protein (10.5 kDa) from Ehrlich-ascites-tumour cells. , 1987, The Biochemical journal.

[12]  F. Talamantes,et al.  Purification and partial characterization of two prolactin-like glycoprotein hormone complexes from the midpregnant mouse conceptus. , 1987, Endocrinology.

[13]  J. Bahr,et al.  Secretion of a gonadotrophin-releasing hormone- (GnRH-)like factor by the rabbit fetal placenta in vitro. , 1987, Placenta.

[14]  F. Talamantes,et al.  In vitro kinetics of synthesis and release of mouse placental lactogen. , 1986, Endocrinology.

[15]  L. Kaczmarek,et al.  Molecular cloning of the cDNA for a growth factor-inducible gene with strong homology to S-100, a calcium-binding protein. , 1986, The Journal of biological chemistry.

[16]  M. Harper,et al.  GnRH effects on placental hormones during gestation. III. Prostaglandin E, prostaglandin F, and 13,14-dihydro-15-keto-prostaglandin F. , 1986, Biology of reproduction.

[17]  F. Talamantes,et al.  The effect of hypophysectomy on serum placental lactogen and progesterone in the mouse. , 1986, Endocrinology.

[18]  T. Siler-Khodr,et al.  Gonadotropin-releasing hormone effects on placental hormones during gestation: I. Alpha-human chorionic gonadotropin, human chorionic gonadotropin and human chorionic somatomammotropin. , 1986, Biology of reproduction.

[19]  D. Sarkar.  Gonadotropin-releasing hormone-like immunoreactivity in rat placenta. , 1986, Neuroendocrinology.

[20]  N. Ling,et al.  Immunoreactive and biologically active growth hormone-releasing factor in the rat placenta. , 1985, Endocrinology.

[21]  F. Suzuki,et al.  Inhibition of adipose S-100 protein release by insulin. , 1985, Biochimica et biophysica acta.

[22]  F. Talamantes,et al.  Placental lactogen secretion in the mouse: in vitro responses and ovarian and hormonal influences. , 1985, The Journal of experimental zoology.

[23]  F. Suzuki,et al.  Hormonal Regulation of Adipose S‐100 Protein Release , 1984, Journal of neurochemistry.

[24]  R. Baserga,et al.  Cell-cycle-specific cDNAs from mammalian cells temperature sensitive for growth. , 1984, Proceedings of the National Academy of Sciences of the United States of America.

[25]  B. Moore,et al.  Proteins of the Brain Extracellular Fluid: Evidence for Release of S‐100 Protein , 1984, Journal of neurochemistry.

[26]  H. Friesen,et al.  Ovariectomy leads to a rapid increase in rat placental lactogen secretion. , 1984, Endocrinology.

[27]  H. Friesen,et al.  Ovarian factors inhibit and fetal factors stimulate the secretion of rat placental lactogen. , 1984, Endocrinology.

[28]  S. Handwerger,et al.  Inhibition of decidual prolactin release by a decidual peptide. , 1983, The Journal of clinical endocrinology and metabolism.

[29]  F. Suzuki,et al.  Increase in S-100 protein levels in blood plasma by epinephrine. , 1983, Journal of biochemistry.

[30]  H. Nogami,et al.  Novel clonal strains from adult rat anterior pituitary producing S-100 protein , 1983, Nature.

[31]  S. Handwerger,et al.  Stimulation of the synthesis and release of decidual prolactin by a placental polypeptide. , 1983, Endocrinology.

[32]  J. Heikkila,et al.  Synthesis of S100 Protein on Free and Membrane‐Bound Polysomes of the Rabbit Brain , 1983, Journal of neurochemistry.

[33]  F. Talamantes,et al.  The development and characterization of a homologous radioimmunoassay for mouse placental lactogen. , 1982, Endocrinology.

[34]  F. Talamantes,et al.  Isolation, purification, and characterization of mouse placental lactogen. , 1982, Proceedings of the National Academy of Sciences of the United States of America.

[35]  R. Wollmann,et al.  S-100 protein in human chondrocytes , 1982, Nature.

[36]  F. Suzuki,et al.  Peripheral distribution of nervous system-specific S-100 protein in rat. , 1982, Journal of biochemistry.

[37]  J. Sykes,et al.  Iodination of proteins, glycoproteins, and peptides using a solid-phase oxidizing agent, 1,3,4,6-tetrachloro-3α, 6α-diphenyl glycoluril (Iodogen) , 1981 .

[38]  S. Handwerger,et al.  Human placental lactogen release in vitro: paradoxical effects of calcium. , 1981, The American journal of physiology.

[39]  H. Towbin,et al.  Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. , 1979, Proceedings of the National Academy of Sciences of the United States of America.

[40]  R. Donato.  FURTHER STUDIES ON THE SPECIFIC INTERACTION OF S‐100 PROTEIN WITH SYNAPTOSOMAL PARTICULATES 1 , 1976, Journal of neurochemistry.

[41]  M. M. Bradford.  A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. , 1976, Analytical biochemistry.

[42]  F. Michetti,et al.  Soluble and membrane-bound S-100 protein in cerebral cortex synaptosomes Properties of the S-100 receptor , 1975, Brain Research.

[43]  R. Hinegardner,et al.  An improved fluorometric assay for DNA. , 1971, Analytical biochemistry.

[44]  U. K. Laemmli,et al.  Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4 , 1970, Nature.

[45]  B. Moore.  A soluble protein characteristic of the nervous system. , 1965, Biochemical and biophysical research communications.