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At least 325 records · Page 18Linked to original sources
PubMed1989

Monoclonal antibodies to human secretory "pregnancy-associated endometrial alpha 1-globulin," an insulin-like growth factor binding protein: characterization and use in radioimmunoassay, Western blots, and immunohistochemistry.

Monoclonal antibodies were raised against pregnancy-associated endometrial alpha 1-globulin (alpha 1-PEG), a 32 KD insulin-like growth factor binding protein (IGF-BP), which represents a major secretory product of the human decidualized endometrium during pregnancy. This class of IGF-BP has been implicated in the modulation of action, inhibitory and stimulatory, of insulin-like growth factors. Immunization with the protein purified from pregnancy endometrium resulted after myeloma fusion in the isolation of six hybridoma clones and the antibodies produced were characterized. The Ka of the antibodies ranged between 4.75 x 10(9) M-1 and 0.7 x 10(8) M-1. In Western blots all monoclonal antibodies reacted with purified protein of molecular weight 32 KD and specifically detected this IGF-BP species in culture medium and cytosolic extracts of pregnancy endometrium and amniotic fluid. The monoclonal antibodies appear to define three epitope-bearing regions as evidenced by their reactivity to polypeptide fragments of the protein. After synthesis and secretion by tissue explants in vitro the protein is susceptible to cleavage into fragments possessing different monoclonal antibody-defined reactivity. Employing immunohistochemical techniques the protein was principally localized to decidual cells in tissue sections of pregnancy endometrium and solely to these cells after enzymic digestion of the tissue. The implications of these results are discussed with respect to potential role of IGF-BP in the action of IGF upon the IGF-1 receptor-bearing populations, including lymphocytes and trophoblast cells, D in the decidua.

Antibodies, Monoclonal↗
PubMed1991

Suppression by human placental protein 14 of natural killer cell activity.

Human decidua of early pregnancy contains considerable numbers of CD3-CD56+ natural killer (NK) cells. In this study, two major protein products of the decidua, placental protein 14 (PP14) and placental protein 12 (PP12), were tested for the ability to regulate human NK cell activity. In vitro overnight exposure to PP14 of blood lymphocytes or purified large granular lymphocytes (LGL) resulted in suppression of cytotoxicity against K562 target cells in a 4-h 51Cr release assay. The NK inhibition was dependent on concentrations of PP14, being detectable at 5 micrograms/ml and reaching maximum at 50 micrograms/ml. Manifestation of PP14-induced NK suppression required 18-h contact with NK cells. The suppression of NK activity by PP14 was not abolished by indomethacin. In a target binding assay the number of PP14-treated LGL binding to K562 was comparable to that of untreated ones. By contrast with PP14, PP12 produced no effects on NK cells. These results indicate that PP14 suppresses the function of NK cells, which might be involved in prevention of maternal immune rejection of fetus at the fetomaternal interface.

Cells, Cultured↗
PubMed2006

Human endometrial cytodifferentiation by histone deacetylase inhibitors.

Abstract Human uterine endometrium repeats proliferation, differentiation (decidualization) and tissue breakdown during the menstrual period. Appropriate secretion of ovarian steroid hormones regulates these sequential endometrial remodeling cycles. While progesterone replacement therapy is adopted for endometrial dysfunction of differentiation, including recurrent impairment of implantation, no obvious effective results are obtained. Histone reversible acetylation, regulated by histone acetyltransferases and histone deacetylases plays a pivotal role in gene transcription. Although, in cells cultured with histone deacetylase inhibitors (HDACI), the expression of only about 2% of expressed genes is changed twofold or more compared with untreated control cells. Numerous previous works have demonstrated that HDACI affect cell proliferation/apoptosis in a variety of types of cells. To date, several HDACI are in phase I or phase II clinical trials as anticancer drugs. However, no reports have been found that HDACI is useful for transdifferentiation in human endometrium. Recently, we reported that HDACI could induce the expression of differentiation marker proteins, morphological change and functional cytodifferentiation in both human endometrial stromal and epithelial cells. In this review, we summarize the effect of HDACI against the human endometrial cytodifferentiation, indicating the possibility that HDACI can be used not only as an anticancer drug, but also as a transdifferentiation reagent, based on a new strategy.

Acetylation↗
PubMed1991

Molecular cloning of complementary DNAs for two human endometrial proteins and cellular localization of their messenger RNAs.

Insulin-like growth factor binding protein-1 (IGFBP-1) and a human beta-lactoglobulin homologue (beta LG/PP14) are two major secretory proteins of the human endometrium. The genes coding for these two proteins are expressed in separate types of the endometrial cells, with the IGFBP-1 gene being expressed in the stromal and the beta LG/PP14 gene in the glandular epithelial cells. Although the biological reasons for the presence and expression of IGFBP-1 and beta LG/PP14 in human endometrial cells remain to be elucidated, the fact that these gene products are expressed in different endometrial cell types provides a unique opportunity to employ them as markers in studies on epithelial-to-stromal cell communication in the endometrium. The primary structures of these proteins have been deduced from their cloned cDNAs. beta LG/PP14 is highly homologous to all known beta-lactoglobulins from various species. For example, horse beta-lactoglobulin I monomer exhibits a 53% protein sequence identity with beta LG/PP14; they have the same number of amino acid residues, and their three-dimensional structures are predicted to be similar. This latter conclusion is inferred from the fact that the four cysteinyl residues that are responsible for the formation of intramolecular bridges in beta-lactoglobulins are spatially conserved in beta LG/PP14. The human protein is encoded by a 900-base pair-long mRNA that is expressed in the glandular epithelial cells of the endometrium in a cyclic manner; in addition, it is found in the mucosal epithelial cells of the fallopian tubes. Several lines of circumstantial evidence suggest that the expression of the beta LG/PP14 gene is regulated by progesterone; however, whether this regulation is elicited by the progesterone receptor at the transcriptional level has not so far been demonstrated. The IGFBP-1 protein sequence contains 259 amino acid residues, with the propeptide possessing a 25-amino acid-long signal peptide. The NH2-terminal sequence of this and other IGFBPs is very cysteine-rich, suggesting the possibility that this domain is involved in the binding of IGF-I and IGF-II ligands. A PEST region, a sequence that is found in proteins with short intracellular half-lives, is included in the middle half of the IGFBP-1 polypeptide. Among the IGFBPs, IGFBP-1 appears to be the only one with a PEST sequence. The carboxy-terminal end of IGFBP-1 contains an Arg-Gly-Asp tripeptide that is also found in IGFBP-2 and may function as a cell attachment recognition signal in these proteins.(ABSTRACT TRUNCATED AT 400 WORDS)

Amino Acid Sequence↗
PubMed2001

Glycoprotein structure determination by mass spectrometry.

The human genome encodes 30,000 to 40,000 proteins, and a major challenge is to understand how posttranslational events, such as glycosylation, affect the activities and functions of these proteins in health and disease. Glycosylated proteins are ubiquitous components of extracellular matrices and cellular surfaces where their oligosaccharide moieties are implicated in a wide range of cell-cell and cell-matrix recognition events. The power of ultrahigh-sensitivity mass spectrometric strategies for defining the primary structures of highly complex mixtures of glycoprotein glycoforms is set to revolutionize structural glycobiology in the coming postgenomic era.

Animals↗
PubMed1990

Protein factor of fertility in malignancies.

Serum levels of the protein factor of fertility (PFF) were measured by immunoenzymatic assay with a sensitivity of 4 ng/ml. The normal concentration of PFF was within 8-20 ng/ml in males and 20-40 ng/ml in females. Elevated levels of PFF--from 50 to 400 ng/ml--were found in patients with ovarian tumors (19%), cancer of the uterine body (25%) and tumors of the uterine cervix (37%).

Animals↗
PubMed1991

Comparative study of enzyme-linked immunosorbent assay and radioimmunoassay techniques in determining serum placental protein 14 levels in gynecologic patients.

A comparative analysis of radioimmunoassay (RIA) and enzyme-linked immunosorbent assay (ELISA) techniques in determining placental protein 14 (PP14) levels in gynecologic patients was performed. Serum PP14 levels were assessed in the patients in the last period of gestation, during menopause and in healthy nonpregnant controls. The possible discrepancy in PP14 levels was also examined in gynecologic patients with benign and malignant tumors. Both RIA and ELISA techniques proved to be sufficiently sensitive to measure PP14 concentration.

Enzyme-Linked Immunosorbent Assay↗
PubMed1992

Serous ovarian cyst fluids contain high levels of endometrial placental protein 14.

This paper reports the detection and characterization of endometrial placental protein 14 (PP14) in human ovarian cyst fluids. PP14 from ovarian cyst fluid has the same molecular size as PP14 purified from human amniotic fluid. No clear difference was found in the PP14 concentrations between benign, borderline and malignant cyst fluids, but serous ovarian cyst fluids had significantly higher PP14 concentrations (median 253.3 micrograms/l) than mucinous cyst fluids (median 17.5 micrograms/l).

Adult↗
PubMed2001

A rheostatic mechanism for T-cell inhibition based on elevation of activation thresholds.

The activation of discrete T-cell responses depends on the triggering of individualized threshold numbers of T-cell receptors (TCRs). The results of this study indicate that the lipocalin placental protein 14 (PP14), a T-cell inhibitor produced by cells of the reproductive and hematopoietic systems, mediates its anti-inflammatory activity by elevating the T-cell activation threshold, thereby rendering T cells less sensitive to stimulation. Significantly, the data demonstrate hierarchical sensitivity of selected cytokine responses to PP14-mediated inhibition, with the hierarchy reflecting their respective activation thresholds. These findings suggest a novel paradigm for immunoinhibition wherein negative regulators can finely tune, rather than inactivate, T-cell responses, and thereby skew the cytokine output of immunologic responses.

Amniotic Fluid↗
PubMed1986

Secretory endometrium synthesizes placental protein 14.

Saline extracts of human nonpregnant endometrium were found to contain placental protein 14 (PP14). The tissue PP14 content was highest in the late secretory phase (median, 7.7 mg/g protein; n = 14), whereas proliferative endometrium (n = 8) was either PP14 negative or showed a low PP14 content (median, 0.15 mg/g protein). By immunoperoxidase staining, PP14 was localized in the glandular epithelial cells of endometrium. In tissue culture, secretory endometrium released more PP14 than proliferative endometrium, and cycloheximide markedly decreased this release. Synthesis of PP14 by secretory endometrium was demonstrated by incorporation of [35S]methionine into immunoprecipitable PP14. These results show that PP14 is synthesized and secreted by the nonpregnant endometrium.

Culture Techniques↗
PubMed1987

Amino acid sequence homology between human placental protein 14 and beta-lactoglobulins from various species.

The primary structure of 22 N-terminal amino acid residues of placental protein 14 was determined by automated Edman degradation with a gas-phase sequencer. This protein, isolated from the human placenta and its membranes, was considered pure as evidenced by a single N-terminal amino acid sequence M D I P Q T K Q D L E L P K L A G T W H S M. It shows significant sequence homology with horse, bovine, buffalo, sheep and goat beta-lactoglobulins. We found 13 identities out of 22 possible matches with horse beta-lactoglobulin. beta-lactoglobulins from several animal species have been found to bind retinol. Among the identical residues there is one tryptophan at position 19 which is conserved in beta-lactoglobulins and is also found in the human retinol-binding protein at the corresponding position. These data suggest a common origin of PP14 and beta-lactoglobulins.

Amino Acid Sequence↗
PubMed1988

N-terminal amino acid sequence of human pregnancy-associated endometrial alpha 1-globulin, an endometrial insulin-like growth factor (IGF) binding protein--evidence for two small molecular weight IGF binding proteins.

We have previously demonstrated that quantitatively the major secretory protein of the human endometrium from the latter half of the first trimester of pregnancy, pregnancy-associated endometrial alpha 1-globulin (alpha 1-PEG), is a small mol wt insulin-like growth factor binding protein (IGF BP) and is detected at high levels in amniotic fluid. N-terminal amino acid sequences have been determined for this protein purified from both these sources and a single N-terminal amino acid sequence Ala Pro Trp Gln Cys Ala Pro Cys Ser Ala Glu Lys Leu Ala Leu Pro Pro was obtained. The first ten residues are identical to those previously reported for the small mol wt IGF BP isolated from amniotic fluid and HEPG2 culture medium. However it was different to that reported for the IGF BP isolated from term placenta, placental protein 12 (PP12), a protein previously suggested to originate in the endometrium. These data suggest that at least two distinct forms of the small mol wt IGF BP exist and supports the hypothesis that the amniotic fluid form originates from the pregnancy endometrium.

Amino Acid Sequence↗
PubMed1996

Analysis of differential gene regulation in adequate versus inadequate secretory-phase endometrial complementary deoxyribonucleic acid populations from the rhesus monkey.

The ability to create artificial menstrual cycles in the rhesus monkey provides a model for studies on the regulation of genes and gene networks by estradiol or progesterone (P) in the primate endometrium. This model allowed us to create both a normal level of secretory phase P or an inadequate level of secretory phase P, i.e. endometria that cannot support implantation. The objective of our present study focused on PCR analyses of genes for several factors that are believed to be important in the proper maturation of the endometrium. Complementary DNA (cDNA) populations were prepared from endometria harvested on day 13 (peak E level), days 21-23 of an adequate secretory phase (PcDNA) and days 21-23 of an inadequate secretory phase (IcDNA). Although placental protein 14, leukemia inhibitory factor and 17-beta hydroxysteroid dehydrogenase displayed highly upregulated levels in PcDNA (P-activated genes), there was little or no up-regulation in IcDNA. Transforming growth factor-beta 2 and its receptor and insulin growth factor-I and its receptor were up-regulated in PcDNA, whereas little or no expression was observed in IcDNA. Regulators of the cell cycle and transcription, such as retinoblastoma, c-fos, and c-jun genes, were also greatly underexpressed in IcDNA compared with PcDNA. Interestingly, one gene that we studied, keratinocyte growth factor, that was up-regulated by P (peak E levels vs. PcDNA) was more highly expressed in IcDNA. This latter result suggests that low levels of circulating P are sufficient for expression of this gene, whereas high sustained P levels result in an autologous down-regulation. These data show that the regulation of genes that may play pivotal roles in endometrial maturation are differentially expressed in IcDNA vs. PcDNA and may, in part, characterize improper endometrial maturation.

17-Hydroxysteroid Dehydrogenases↗