Protein Synthesis and Secretion in Human Decidua of Early Pregnancy1

Abstract

Proteins synthesized and secreted by first trimester decidua in primary culture were identified. Explants were cultured for 24 h, in RPMI-1640 or Dulbecco's Modified Eagles Medium containing the radioactive amino acid 35S-methionine or 3H-proline. Electron microscopy of explants before and after 24 h of culture demonstrated the relative purity of the decidua, maintenance of cell integrity, and ultrastructural features indicative of active protein synthesis and secretion. Proteins synthesized and secreted by the explants into the medium were analyzed by fluorography of one-dimensional polyacrylamide gels in the presence of sodium dodecyl sulfate. By comparison of radiolabeled proteins from four women, eight 35S-methionine-labeled bands of 78, 70, 60, 50, 43, 34, 25, and 23 kDa were identified as common decidual peptides. A comparison of autoradiographs of the medium from decidual cultures to decidual cell homogenates showed that seven of these peptides were enriched in the culture medium. When labeled peptides from fibroblast cultures were compared to labeled proteins from decidual cultures each of the common decidual peptides (except the 70 kDa protein) occurred only in the decidual culture medium. Comparison of 3H-proline and 35S-methionine-labeled decidual proteins revealed that the 78, 70, 60, 50, and 34 kDa proteins were of similar fluorographic intensity when labeled with the two different amino acids. The 43, 25, and 23 kDa proteins appeared to contain more methionine, and proteins at 36, 20, 13, and 12 kDa were proline-rich, but contained less methionine. The seven decidual explant-specific, 35S-methionine-labeled secreted proteins were concentrated and purified by preparative gel electrophoresis, and antisera were generated to four of the putative decidual secretory proteins.

Ultrastructural alterations in human decidua in miscarriages compared to normal pregnancy decidua

“…However, we did not observe any apoptotic or necrotic cell in normal decidua. Kisalus et al (26) reported that, in addition to similar structural findings of decidua cell, they did not detect any cell death signs, such as pyknosis, karyorrhexis or mitochondrial degeneration, in normal human decidua explants. In the miscarriage group, besides normal decidual cells, most of the decidual cell shape changed to fusiform and shriveled cytoplasm with spindle‐shaped nuclei and unclear nucleoli.…”

Rheumatoid Factor-Associated High-Molecular-Weight Complexes in the Menstrual and Amniotic Fluids

“…Assuming that some of the functions of the decidua might be mediated by secretory proteins, studies have been directed toward the comprehensive identification of such proteins [2][3][4][5][6]. We have reported previously the identification and immunopurification of two novel human decidua-associated secretory glycopro teins named hDP200 and hDP71 [7,8].…”

Immunohistological distribution of the secretory endometrial protein, ‘pregnancy-associated endometrial α2-globulin’, a glycosylated β-lactoglobulin homologue, in the human fetus and adult employing monoclonal antibodies

“…Recent studies of the identification and characterization of major secretory proteins of the endometrium and decidua (Strinden and Shapiro, 1983;Bell et al, 1985aBell et al, ,b, 1986aHeffiier et al, 1986;Kisalus et al, 1987) promise to yield insights into the function of this tissue and to provide clinically useful markers to assess and monitor its function during the menstrual cycle and pregnancy (Joshi, 1983;Bell, 1986aBell, , 1988aSeppala et al, 1988). One such protein, endometrial protein 15 or pregnancyassociated endometrial a 2 -globulin (a 2 -PEG), was identified as the quantitatively major secretory soluble protein product of the endometrium during the second half of the luteal phase of the menstrual cycle and early first trimester of pregnancy (Bell, 1986a;Bell et al, 1985aBell et al, ,b, 1986a.…”