Placental protein 14 and progestagen-dependent endometrial protein are immunologically indistinguishable

Julkunen, Mervi; Raikar, R.S.; Joshi, Shree; Bohn, H.; Seppålå, M

doi:10.1093/oxfordjournals.humrep.a136349

Cited by 70 publications

(22 citation statements)

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“…In addition, immunological and/or sequence similarity has been reported for PP14, a2-pregnancyassociated endometrial globulin (11) and progesteronedependent endometrial protein (12). The gene sequence of glycodelin has been documented (13), and the Human Genome Organization has registered PAEP as the official symbol of the glycodelin gene (9).…”

Section: Introductionmentioning

confidence: 99%

Glycodelin in reproductive endocrinology and hormone-related cancer

Seppälä¹,

Koistinen²,

Koistinen

et al. 2009

European Journal of Endocrinology

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Glycodelin is an endocrine-regulated glycoprotein that has significant effects on immune cells, apoptosis, reproduction, cell adhesion, differentiation and cancer. In reproduction, glycodelin contributes to capacitation and immunoprotection of spermatozoa, and it modulates sperm-oocyte binding, acrosome reaction and implantation. In endocrine-related cancer, the differentiation inducing effects of glycodelin are accompanied by growth restriction of malignant cells, decreased expression of oncogenes, increased expression of tumour suppressor genes and morphological reversion of the malignant phenotype. This review features these properties and clinical connections, highlighting the role of glycosylation in biological actions.

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Section: Introductionmentioning

confidence: 99%

Glycodelin in reproductive endocrinology and hormone-related cancer

Seppälä¹,

Koistinen²,

Koistinen

et al. 2009

European Journal of Endocrinology

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“…We have utilized the hemizona assay system to determine the potential inhibitory effects of different glycoconjugates on human gamete binding (4 -6). We recently showed that PP14 (human placental protein 14) (7); also referred to as PAEP (progesterone-associated endometrial protein) (8)) inhibits human sperm-zona pellucida binding under hemizona assay conditions in an immediate and dose-dependent fashion (9). This glycoprotein also suppresses responses by a variety of different immune effector cell types (10 -13).…”

mentioning

confidence: 99%

Gender-specific Glycosylation of Human Glycodelin Affects Its Contraceptive Activity

Morris

Dell

Easton

et al. 1996

Journal of Biological Chemistry

141

136

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We have recently demonstrated that a human amniotic fluid-derived glycoprotein, glycodelin-A (GdA; previously known as PP14 or PAEP), potently inhibits gamete binding in an established sperm-egg binding system and expresses immunosuppressive activities directed against a variety of different immune cell types. GdA has high mannose-, hybrid-, and complex-type biantennary oligosaccharides including structures with fucosylated or sialylated N,N-diacetyllactosediamine (GalNAc␤1-4GlcNAc) sequences, which are rare in other human glycoproteins. We now report the characterization of glycodelin-S (GdS). This is a human seminal plasma glycoprotein that is immunologically indistinguishable from GdA, but unlike the latter, does not inhibit human sperm-zona pellucida binding under hemizona assay conditions. Analysis of the N-glycans of GdS by mass spectrometry revealed that all glycoforms of GdS are different from those of GdA. GdS glycans are unusually fucose-rich, and the major complex-type structures are biantennary glycans with Lewis x (Gal␤1-4(Fuc␣1-3)GlcNAc) and Lewis y (Fuc␣1-2Gal␤1-4 (Fuc␣1-3)GlcNAc) antennae. It is probable that these highly fucosylated epitopes contribute to the immunosuppressive activity of human seminal plasma and to the low immunogenicity of sperm. This study provides the first evidence for gender-specific glycosylation that may serve to regulate key processes involved in human reproduction.

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“…Comparative studies performed in different laboratories revealed the immunochemical identity of PP14 isolated in our laboratory with chorionic a2-microglobulin (CAG-2) of Petrunin et al [44] as well as with progestagen-dependent endometrial protein (PEP) of Joshi et al and endometrial protein 15 (EP 15) of Bell et al and alpha uterine protein (AUP) of Suttcliffe [2,3,12,33,48].…”

Section: Pp8mentioning

confidence: 64%

Immunochemically detected placental proteins and their biological functions

Bohn

Winckler

Grundmann

1991

Arch Gynecol Obstet

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During the last 20 years a systematic search for proteins occurring in human term placenta (afterbirth) has been performed in our laboratory. As a result more than 30 soluble placental proteins and at least 20 different solubilized antigens apparently derived from the placental membranes have been identified by immunochemical methods in extracts from human term placentas. Most of these proteins have already been isolated to purity and characterized by their physicochemical parameters. Specific antisera to these proteins were obtained by immunizing animals with the corresponding purified proteins. They were used detect and localize these antigens by immunochemical methods in the placenta and in other human tissues. Sensitive immunochemical assays have been developed to exactly quantitate the new proteins in body fluids and to find out the diagnostic significance of measurement of these proteins in pregnant women and in patients with tumors and other diseases. Another aim was to elucidate the biological functions of our immunochemically detected proteins. The results obtained thus far are reported.

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Placental protein 14 and progestagen-dependent endometrial protein are immunologically indistinguishable

Cited by 70 publications

References 0 publications

Glycodelin in reproductive endocrinology and hormone-related cancer

Glycodelin in reproductive endocrinology and hormone-related cancer

Gender-specific Glycosylation of Human Glycodelin Affects Its Contraceptive Activity

Immunochemically detected placental proteins and their biological functions

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