Expression of glycodelin in human breast and breast cancer

Kämäräinen, Meerit; Halttunen, Mervi; Koistinen, Riitta; Boguslawsky, Kristina von; Smitten, Karl von; Andersson, Leif C.; Seppälä, Markku

doi:10.1002/(sici)1097-0215(19991210)83:6<738::aid-ijc7>3.0.co;2-f

Cited by 38 publications

(20 citation statements)

References 19 publications

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“…PP14 is expressed in maternal reproductive tracts and is highly abundant during early pregnancy, constituting up to 10% of total decidual protein in the first trimester, and occurs in remarkably high concentrations in amniotic fluid (AF) during the first half of pregnancy (125 mg/L; of decidual origin) (11,12). Significant concentrations of PP14 are also present in tumors of reproductive organs (13,14), in plasma during early pregnancy (12), and in male seminal fluid (15). Interestingly, decidual NK cells were shown to express PP14 (16), and in turn PP14 has been shown to suppress NK function (17).…”

Section: N Aive Cd4mentioning

confidence: 99%

Differential Regulation of Th1/Th2 Cytokine Responses by Placental Protein 14

Mishan-Eisenberg¹,

Borovsky²,

Weber

et al. 2004

The Journal of Immunology

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The potency of TCR signaling during primary CD4+ T cell activation influences initial cytokine expression patterns and subsequent polarization toward either Th1 or Th2 subsets. In this study, we demonstrate that the T cell inhibitor placental protein 14 (PP14; glycodelin) preferentially inhibits Th1 cytokine responses and chemokine expression when present during ex vivo priming of CD4+ T cells. PP14 synergizes with exogenously added IL-4 in skewing T cell responses. Significantly, PP14 impairs the down-regulation of GATA-3 transcriptional regulator expression that normally accompanies T cell activation, which is a prerequisite for Th1 development. Taken together, these data document for the first time the ability of PP14 to skew Th responses.

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Section: N Aive Cd4mentioning

confidence: 99%

Differential Regulation of Th1/Th2 Cytokine Responses by Placental Protein 14

Mishan-Eisenberg¹,

Borovsky²,

Weber

et al. 2004

The Journal of Immunology

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“…We believe these findings imply that the cell specific expression of glycodelin is due to specific factors in both the pathway by which progesterone is able to activate the glycodelin gene, absent in both COS-1 and T47D cells, as well as the components responsible for increased glycodelin expression in response to HDAC inhibition, absent in the COS-1 cells but not in the T47D cells. This may account for the previous observation that glycodelin is expressed in the human mammary gland but it is not regulated by progesterone (Kamarainen et al 1999). It has been shown in a number of other genes that HDAC may interact with Sp1 which in turn is bound to the Sp1 element (reviewed in Li et al 2004).…”

Section: Discussionmentioning

confidence: 89%

Histone deacetylase inhibition and progesterone act synergistically to stimulate baboon glycodelin gene expression

Jaffe

Ferguson-Gottschall²,

Gao³

et al. 2007

Journal of Molecular Endocrinology

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During the late luteal phase of the menstrual cycle and early pregnancy, the major secretory product of the uterine glandular epithelial cells in humans and non-human primates is glycodelin. Previous studies using Ishikawa cells, a human endometrial cell line, have shown that a chimeric plasmid containing the baboon glycodelin promoter responds to progestins but the response is modest compared with the induction of glycodelin seen in vivo and in gene array analysis. A recent report indicating that the histone deacetylase inhibitor trichostatin A (TSA) promoted glycodelin expression prompted us to examine its mechanism of action. In Ishikawa cells transfected with the baboon glycodelin promoter, TSA and the synthetic progestin medroxyprogesterone acetate both stimulated expression of the reporter and the combined treatment produced a synergistic effect. The effect of TSA and progestin was absent when the same promoter constructs were transfected into COS-1 cells, a kidney cell line, and a TSA effect but no progestin effect was observed in T47D cells, a mammary cell line. Through deletion analysis, the TSA action was localized to the K67/K52 region of the baboon glycodelin promoter, a region which contains the proximal Sp1 site. Deletions of this same region had no effect on progestin responsiveness. Our findings indicate that at least two regions of the glycodelin promoter are important for the normal induction of glycodelin expression. Non-target cells may lack factors which act on the response elements resulting in the restriction of expression to the appropriate target tissue.

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“…Recently, an alternative splice variant of Gd mRNA was demonstrated in human breast cancer tissue (Kamarainen et al 1999). Should this mRNA variant be translated, the ELISA for identiWcation of Lewis-type oligosaccharide structures and TF antigen on Gd A (GdA) and ascites Gd.…”

Section: Discussionmentioning

confidence: 99%

“…Should this mRNA variant be translated, the ELISA for identiWcation of Lewis-type oligosaccharide structures and TF antigen on Gd A (GdA) and ascites Gd. We identiWed signiWcant lower expression of SLeX expression in ascites Gd compared to GdA marked by an asterisk, signiWcant lower expression of SLea ascites Gd compared to GdA marked by two asterisks and signiWcantly elevated expression of the TF antigen marked by three asterisks resulting protein lacks one of the potential glycosylation sites at Asn-85 and two cysteinyl residues at 119 and 160 (Kamarainen et al 1999), which would eventually lead to diVerent folding of the protein.…”

Section: Discussionmentioning

confidence: 99%

“…The same set of antibodies was used to determine GdA expression in breast cancer cells (Kamarainen et al 1999). Using a polyclonal antibody against a synthetic Gd peptide sequence on endometrial, ovarian and cervical cancer, an elevated Gd expression in ovarian and endometrial cancer tissue has been demonstrated and further conWrmed by RT-PCR analysis .…”

Section: Introductionmentioning

confidence: 99%

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Immunohistochemistry, glycosylation and immunosuppression of glycodelin in human ovarian cancer

Jeschke

Mylonas

Kunert‐Keil

et al. 2008

Histochem Cell Biol

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Glycodelins (Gds) are glycoproteins with a gender specific glycosylation. Glycodelin A (GdA) is primarily produced in endometrial and decidual tissue and secreted to amniotic fluid. Glycodelins were also identified in several cancer types, including serous ovarian cancer. Gds act as a T-cell inhibitor and are involved in inactivation of human monocytes. With a Gd peptide antibody, derived from a 15 amino acid sequence of human Gd and in situ hybridization experiments, the expression of Gd in serous, mucinous, endometrioid and clear cell ovarian tumors was identified. In contrast to former investigations with antibodies against GdA, a positive immunohistochemical reaction for Gd was observed in all forms of epithelium ovarian cancer. These results were confirmed with in situ hybridization. In addition, Gd is expressed in granulose cell tumors, a non-epithelial form of ovarian cancer. Furthermore, Gd was purified from ascites fluid of ovarian cancer patients. Ascites Gd showed significant differences in its structure of sialyl Lewis-type oligosaccharides compared to GdA. Additionally, ascites Gd inhibits IL-2 stimulated proliferation of peripheral blood leucocytes and inhibits adhesion of SLe(X)-positive cells to E-selectin. Therefore, Gd could act as an inhibitor of lymphocyte activation and/or adhesion in ovarian cancer.

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Expression of glycodelin in human breast and breast cancer

Cited by 38 publications

References 19 publications

Differential Regulation of Th1/Th2 Cytokine Responses by Placental Protein 14

Differential Regulation of Th1/Th2 Cytokine Responses by Placental Protein 14

Histone deacetylase inhibition and progesterone act synergistically to stimulate baboon glycodelin gene expression

Immunohistochemistry, glycosylation and immunosuppression of glycodelin in human ovarian cancer

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