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At least 19 recordsLinked to original sources
PubMed1996

Glycodelin from seminal plasma is a differentially glycosylated form of contraceptive glycodelin-A.

Glycodelin-A is a human amniotic fluid-derived glycoprotein with contraceptive and immunosuppressive activities. An immunoreactive form of glycodelin was detected in seminal plasma over a decade ago, but definitive characterization of this glycoprotein was not pursued. We considered it unlikely that the seminal plasma of fertile men would contain an appreciable amount of contraceptive glycodelin-A. To address this issue we purified seminal plasma glycodelin (glycodelin-S) and performed comparative studies with glycodelin-A. Glycodelin-S behaved differently when compared with glycodelin-A during sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) and isoelectric focusing but identically after enzymatic deglycosylation. N-terminal sequencing of glycodelin-A and glycodelin-S gave identical results, and digestion with trypsin gave identical peptide fragments. The glycoproteins were also found to be indistinguishable from each other based upon immunological analyses. These results indicate that glycodelin-S and glycodelin-A have similar overall protein structure, suggesting the likelihood that these glycoproteins are differentially glycosylated forms of very similar proteins. This latter possibility is supported by lectin binding studies indicating that, unlike glycodelin-A, glycodelin-S does not manifest any affinity for lectins from Wisteria floribunda or Sambucus nigra. The results of sugar analysis and neuraminidase digestion also lead us to conclude that glycodelin-S and glycodelin-A are differentially glycosylated forms of similar proteins. Our evidence indicates that glycodelin-A mediated its biological activities via its unusual oligosaccharide sequences that are not associated with glycodelin-S. In lectin-immunoassay no appreciable amount of contraceptive glycodelin-A was found in the 22 seminal plasma samples studied.

Amidohydrolases↗
PubMed2000

Recombinant glycodelin carrying the same type of glycan structures as contraceptive glycodelin-A can be produced in human kidney 293 cells but not in chinese hamster ovary cells.

We have produced human recombinant glycodelin in human kidney 293 cells and in Chinese hamster ovary (CHO) cells. Structural analyses by lectin immunoassays and fast atom bombardment mass spectrometry showed that recombinant human glycodelin produced in CHO cells contains only typical CHO-type glycans and is devoid of any of the N, N'-diacetyllactosediamine (lacdiNAc)-based chains previously identified in glycodelin-A (GdA). By contrast, human kidney 293 cells produced recombinant glycodelin with the same type of carbohydrate structures as GdA. The presence of a beta1-->4-N-acetylgalactosaminyltransferase functioning in the synthesis of lacdiNAc-based glycans in human kidney 293 cells is concluded to be the cause of the occurrence of lacdiNAc-based glycans on glycodelin produced in these cells. Furthermore, human kidney 293 cells were found to be particularly suited for the production of recombinant glycodelin when they were cultured in high glucose media. Lowering the glucose concentration and the addition of glucosamine resulted in higher relative amounts of oligomannosidic-type glycans and complex glycans with truncated antennae. Human glycodelin is an attractive candidate for the development of a contraceptive agent, and this study gives valuable information for selecting the proper expression system and cell culture conditions for the production of a correctly glycosylated recombinant form.

Animals↗
PubMed1997

The role of relaxin in glycodelin secretion.

Glycodelin is a glycoprotein named for its unique carbohydrate structure. Glycodelin is produced by the secretory endometrium during the late luteal phase and returns to baseline during menses of the ensuing cycle, whereas in conceptive cycles it rapidly increases. Although progesterone and possibly estradiol are required for glycodelin production, they are not directly involved in the synthesis and release of this protein. Their role may be development of the endometrial secretory glandular elements, whereas other factors are required to initiate and maintain glycodelin secretion. The pattern of relaxin secretion during the luteal phase and early pregnancy is similar to that of glycodelin, but their profiles have not been determined simultaneously. To investigate the relationship of relaxin and glycodelin, two studies were conducted. In the first study, relaxin, glycodelin, and ovarian steroids were measured in daily serum samples from nonconceptive and conceptive natural cycles. Profiles of relaxin and glycodelin were closely associated, with the onset of relaxin preceding glycodelin secretion by 1-2 days in nonconceptive cycles, and the pregnancy-associated increases in each hormone differing by about 2 days. The second study tested the hypothesis that relaxin stimulates glycodelin secretion. Samples were obtained from patients injected with human relaxin for 28 days. In subjects demonstrating ovarian cyclicity, glycodelin secretion was elevated, but it was not detected in subjects without ovarian cyclicity or in placebo-treated control subjects. This study reveals a close temporal and quantitative relationship between relaxin and glycodelin profiles in the late luteal phase and early pregnancy. It also demonstrates that relaxin administration can stimulate glycodelin production from a developed endometrium. This is the first report of a nonsteroidal ovarian factor that controls glycodelin secretion, and these results suggest a function for relaxin during early pregnancy. Glycodelin is a potent inhibitor of sperm zona pellucida binding by virtue of its extensive carbohydrate structure, but it is normally at a nadir in the periovulatory period. The data demonstrate that relaxin can stimulate glycodelin secretion throughout the menstrual cycle, including the periovulatory period, when relaxin-induced glycodelin secretion could have a contraceptive effect.

Adolescent↗
PubMed2000

Implications in the management of pregnancy: II. Low levels of gene expression but enhanced uptake and accumulation of umbilical cord glycodelin.

OBJECTIVE: We recently reported the presence of glycodelin in the endothelial cells of human umbilical cord. The objective of the current study is to determine whether human umbilical cord endothelial cells synthesize glycodelin. DESIGN: Controlled clinical study. SETTING: Healthy women undergoing normal delivery at Grady Memorial Hospital, Atlanta, Georgia. PATIENT(S): Healthy women undergoing normal delivery. INTERVENTION(S): None. MAIN OUTCOME MEASURE(S): Human umbilical cord was collected after full-term delivery and total RNA from endothelial cells was isolated. Reverse-transcription polymerase chain reaction (RT-PCR) was performed by using primers from glycodelin sequence. Human umbilical cord endothelial cells at passage 3 were incubated with glycodelin-derived peptide or glycodelin-rich amniotic fluid. Immunocytochemical analysis was performed by using purified chicken anti-glycodelin peptide antibody to detect the accumulation of glycodelin in cells. RESULT(S): Little or no glycodelin message was detectable in the endothelial cells from human umbilical cord vein by RT-PCR and Southern blot analysis. However, these cells readily took up glycodelin protein and glycodelin-derived synthetic peptide from the medium. CONCLUSION(S): The presence and accumulation of glycodelin in the umbilical cord might indicate their potential role in the survival of fetal tissue in the maternal environment.

Blotting, Western↗
PubMed1998

Regulation of the glycosylated beta-lactoglobulin homolog, glycodelin [placental protein 14:(PP14)] in the baboon (Papio anubis) uterus.

In vitro studies indicate that glycodelin (PP14) synthesis by the human endometrium increases dramatically at the time of implantation and early pregnancy. It has been postulated that this protein may have an immunosuppressive function. Due to the limitations associated with in vivo studies in the human, this study was undertaken to study the regulation of the baboon glycodelin homolog in vivo during the menstrual cycle and early pregnancy. In nonpregnant baboons, between days 10-12 postovulation (n = 3) the mid and apical regions of the glandular epithelium showed a distinct punctate staining pattern, which increased between days 12-18 of pregnancy (n = 3). Between days 25-60 of pregnancy, staining intensity in the glandular epithelium decreased. The decrease was more apparent at the implantation site compared with the nonimplantation site. The immunostaining correlated with the synthesis of radiolabeled baboon glycodelin in explant culture. Northern blot analysis demonstrated two messenger RNA (mRNA) transcripts [1.0 and 1.7 kilobases (kb)] in the baboon uterus compared with a single 1.0-kb transcript in the human, and mRNA expression was consistent with protein localization and synthesis. The protein and mRNA expression was consistently higher in the deeper glands of the functionalis and basalis during early pregnancy. Because the increased expression of glycodelin in the baboon endometrium coincided with peak levels of CG, a simulated pregnant baboon model was used to confirm hormonal regulation. Exogenous human CG (hCG) followed by estrogen and progesterone treatment in intact and ovariectomized baboons up-regulated glycodelin expression between days 18-25 postovulation (n = 10). By day 32 postovulation (n = 3), glycodelin synthesis decreased. Estrogen and progesterone treatment in the absence of exogenous hCG did not result in an increase of glycodelin synthesis. Analysis of uterine flushings from hCG-treated animals revealed that a minimum of 7 days of hCG treatment was required for glycodelin to be detectable in the uterine lumen. These studies indicate that a posttranslationally modified glycodelin homolog is synthesized by the baboon uterus during early pregnancy and appears to be regulated directly by CG. This pattern of synthesis is comparable with that observed with in vitro studies in the human. Because glycodelin expression is associated with CG secretion, we suggest that this protein may have a functional role during implantation in the primate. Thus, the baboon may serve as a nonhuman primate model to elucidate the function of this protein in vivo.

Amino Acid Sequence↗
PubMed1996

Normal human ovary and ovarian tumors express glycodelin, a glycoprotein with immunosuppressive and contraceptive properties.

Glycodelin is a glycoprotein with potent immunosuppressive and contraceptive activities. It reacts with antibodies against placental protein 14, or progesterone-associated endometrial protein, and has a unique carbohydrate structure. Previous nomenclature is misleading, because glycodelin is neither synthesized in the placenta nor is it endometrium specific. No ovarian synthesis of glycodelin has been demonstrated. We present evidence for glycodelin synthesis in the human ovary and ovarian tumors. In follicular phase, immunoperoxidase staining of microwave-treated tissue sections employing affinity-purified polyclonal antibodies localized glycodelin to areas of stromal cell condensation in ovarian cortex, theca interna, and the granulosa. In luteal phase, cortical stroma was negative or only weakly positive, whereas glycodelin was present in theca interna of the corpus luteum and luteinized granulosa cells and also in corpus albicans and Leydig cells of the ovarian hilus. In situ hybridization gave negative results for glycodelin mRNA in normal ovary, whereas in ovarian tumors strong expression of both the glycodelin mRNA and the protein were found in benign and malignant serous cystadenomas, mucinous ovarian tumors being negative. We conclude that glycodelin is synthesized in human ovarian tumors, and its occurrence in normal human ovary may represent either synthesis or a site of glycodelin action.

Adult↗
PubMed1998

Epithelial expression of glycodelin in biphasic synovial sarcomas.

Glycodelin is a 28 kDa glycoprotein of the lipocalin family that was previously considered to be specific for the reproductive tract. Glycodelin is found in the secretory glandular epithelium of endometrium and in seminal vesicles. Given the cyclic differentiation of normal endometrial epithelium, we studied by immunohistochemistry a possible expression of glycodelin in other tissues displaying stroma-to-epithelium maturation. We report here that 11/11 biphasic synovial sarcomas expressed glycodelin in the cells exhibiting epithelial or glandular differentiation while the sarcomatous spindle cells remained negative. Glycodelin was also found in secreted material in the lumina of the gland-like structures. In only 1 of the 7 monophasic synovial sarcomas studied, focal glycodelin reactivity was seen in some flattened spindle cells. The expression of glycodelin in biphasic synovial sarcoma tissue was further verified by the demonstration of glycodelin mRNA by reverse transcriptase-polymerase chain reaction. Considering the monoclonal origin of synovial sarcomas, our findings raise the intriguing possibility that activation of expression of the glycodelin gene is involved in the molecular regulation of mesenchyme-to-epithelium differentiation.

Epithelium↗
PubMed1999

Expression of glycodelin in human breast and breast cancer.

Glycodelin is a 28 kDa glycoprotein with structural homology to beta-lactoglobulins, particularly expressed in steroid-responsive tissues of the female reproductive tract. We previously found that transfection of glycodelin cDNA into MCF-7 breast cancer cells induces differentiation into organized acinar epithelium and up-regulation of epithelial markers. In this study, we used immunohistochemistry, Northern blotting and reverse transcription-polymerase chain reaction (RT-PCR) analyses to study glycodelin expression in normal and in malignant breast tissues. The results were compared with the expression of estrogen (ER) and progesterone receptors (PR) and p53 tumor suppressor protein. Glycodelin was found in ductal and lobular epithelium of 6/6 normal breast tissues, 27/29 morphologically normal breast tissues from breast cancer patients, 6/6 benign lactating adenomas, 21/35 ductal carcinomas, 9/9 tubular carcinomas, 9/9 mucinous carcinomas, 3/3 mixed ductal/tubular carcinomas and 7/11 lobular carcinomas. In the latter, of particular interest was the presence of glycodelin in paranucleolar vacuoles of carcinoma cells. Northern blot analysis of fresh frozen tissues revealed the normal full length 0.9 kb mRNA of glycodelin in ductal breast carcinoma. Using RT-PCR analysis, glycodelin messenger ribonucleic acid was found in 13/13 ductal and in 3/3 tubular tumor tissues. We also detected a splicing variant lacking exon 4, which includes the nucleotide sequence encoding the potential N-glycosylation site at Asn-85. Our results demonstrate the synthesis of glycodelin in normal breast and breast cancer. In addition, we show that the paranuclear vacuole, characteristically present in lobular breast cancer cells, contains abundant amounts of glycodelin.

Adenoma↗
PubMedDate not supplied

Seminal plasma glycodelin and fertilization in vitro.

Endometrium-derived glycodelin-A inhibits sperm-egg binding, whereas differentially glycosylated seminal plasma glycodelin-S does not. The difference has been ascribed to the specific type of glycosylation of glycodelin-A. We studied whether the total glycodelin concentration or the relative glycodelin-A concentration in seminal plasma are related to the in vitro fertilization rate of oocytes. We found that total glycodelin levels were significantly higher in a quartile of men with the lowest in vitro fertilization rate compared with the remaining 3 quartiles combined (P = .01). However, for predicting low fertilization capacity of sperm, combining the glycodelin and sperm concentrations by logistic regression analysis did not significantly increase the information obtained from sperm concentration alone. We used specific lectin-immunoassays to determine whether increased glycodelin-A-type glycosylation in seminal plasma would be related to failure to fertilize. No difference was found between the groups with high fertilization and no fertilization in vitro. It is concluded that, although high seminal plasma total glycodelin level has a tendency of being associated with a lower fertilization rate, the difference has limited value to predict fertilization in vitro.

Blood Proteins↗
PubMed2000

Effects of progestins and relaxin on glycodelin gene expression in human endometrial cells.

OBJECTIVE: Glycodelin is an endometrial protein proposed to play an important role in embryonic implantation. We examined the effects of progestins and relaxin on glycodelin transcription, synthesis, and secretion. STUDY DESIGN: Northern blotting, metabolic labeling, and fluorography were used to assess glycodelin messenger ribonucleic acid and protein synthesis in endometrial tissue and cells. Luciferase reporter constructs transfected into endometrial adenocarcinoma cells (Ishikawa cells) were used to determine whether progestins or relaxin could activate the glycodelin gene promoter. RESULTS: Progestins but not relaxin stimulated glycodelin secretion in primary epithelial cell cultures. A 452-base pair fragment of the glycodelin gene promoter was activated 4.3 +/- 0.7 times normal by 10-nmol/L promegestone; however, addition of relaxin to the same construct repressed progestin-stimulate promoter activation by >30%. CONCLUSION: Glycodelin transcription, synthesis, and secretion by endometrial epithelial cells were stimulated by progestins. However, relaxin failed to stimulate production of this immunomodulatory protein and, in fact, repressed progestin-stimulated activation of the glycodelin gene promoter.

Endometrium↗
PubMed1999

Glycodelin and beta-lactoglobulin, lipocalins with a high structural similarity, differ in ligand binding properties.

Human glycodelin, a lipocalin with a high amino acid similarity to beta-lactoglobulins, appears as various glycoforms with different biological activities in endometrium (glycodelin-A) and seminal plasma (glycodelin-S). We found that the structures of these glycodelins and beta-lactoglobulin are similar. Despite this structural similarity, unlike beta-lactoglobulin, glycodelin-A binds neither retinoic acid nor retinol. It was impossible to detect any endogenous retinoids or steroids in any of the two purified glycodelins. Both their glycoforms share similar thermodynamic parameters of reversible denaturation suggesting that native folding of glycodelin-A and glycodelin-S is not influenced by the differences in glycosylation or by ligand binding.

Base Sequence↗
PubMed2000

Implications in the maintenance of pregnancy: I. Presence of immunoreactive glycodelin in human umbilical cord vein endothelial cells.

OBJECTIVE: We previously reported an antipeptide antibody to human glycodelin that recognizes glycodelin in amniotic fluid and epithelial glands of the endometrium. The objective of this study was to determine the presence of glycodelin in human umbilical cord. DESIGN: Controlled clinical study. SETTING: Healthy women undergoing normal delivery at Grady Memorial Hospital, Atlanta, Georgia. PATIENT(S): Healthy women undergoing normal delivery. INTERVENTION(S): None. MAIN OUTCOME MEASURE(S): Umbilical cord vein was isolated from the cord and used for immunohistochemical studies. Human umbilical cords and placentae were collected after full-term delivery. Cords were washed and fixed with formal sucrose. Decidua tissues and blood vessels from placentae were dissected out and fixed. Cryostat sections were immunostained with anti-glycodelin peptide antibody and anti-von Willebrand factor antibody. RESULT(S): Endothelial cells of human umbilical cord vein and artery were strongly immunostained with antiglycodelin antibody. Endothelial cells of the vein were more strongly stained than those of the artery. These cells were confirmed as endothelial cells by positive immunostaining with anti-von Willebrand factor. The epithelial cells outlining the cord were stained with antiglycodelin antibody but not with anti-von Willebrand factor antibody. CONCLUSION(S): This is the first study showing that immunoreactive glycodelin is present in endothelial cells of the umbilical cord. Glycodelin in the umbilical cord may have immunosuppressive or other, unknown functions affecting the physiology or pathophysiology of pregnancy. Whether umbilical vein endothelial cells synthesize glycodelin or serve as reservoir for glycodelin is currently under investigation.

Case-Control Studies↗
PubMed1997

Expression of glycodelin in MCF-7 breast cancer cells induces differentiation into organized acinar epithelium.

Glycodelin, a 28-kd human glycoprotein found in glandular epithelial cells of endometrium and seminal vesicle, was originally considered specific for the reproductive tract. Glycodelin has significant amino-acid sequence homology with beta-lactoglobulins from various species. We report herein the expression of glycodelin in normal and neoplastic glandular epithelia outside the reproductive tract including breast, sweat glands, parabronchial glands, hidradenoma, and pancreatic cystadenoma. The localization of glycodelin in highly differentiated acinar epithelia led us to investigate a possible role for glycodelin in epithelial organization. Transfection of glycodelin cDNA into MCF-7 breast cancer cells induced a dramatically altered growth behavior with formation of acinar configurations and an inability to grow in semisolid media because of apoptosis. The glycodelin-expressing cells also displayed strongly up-regulated expression of markers of organized epithelia, such as cytokeratins 8 and 18 as well as E-cadherin, and changes in intracellular distribution of beta-catenin. The rate of proliferation was also suppressed. These results show that, besides being a product of glandular epithelial cells, expression of glycodelin is accompanied by the acquisition of a phenotype of organized glandular epithelium.

Breast Neoplasms↗
PubMed1998

Promegestone (R5020) and mifepristone (RU486) both function as progestational agonists of human glycodelin gene expression in isolated human epithelial cells.

One of the most abundant protein products of human secretory endometrium is glycodelin, a glycoprotein previously referred to as PP14. Although the precise function of this protein is unknown, its unique glycosylation pattern is believed to affect immunomodulatory activity during human embryonic implantation and inhibition of sperm-egg binding after ovulation. Having confirmed the expression of glycodelin in secretory endometrial glands, we used purified endometrial epithelial cell cultures to demonstrate the hormonal regulation of glycodelin synthesis and secretion. The findings were corroborated by transiently transfecting glycodelin gene promoter-reporter constructs into human epithelioid HeLa and Ishikawa cells. Our results indicate that glycodelin protein production by endometrial epithelial cells is directly up-regulated 4- to 9-fold by progestins and antiprogestins in vitro. Transcriptional regulation of the glycodelin gene promoter expressed in HeLa cells is progesterone receptor-dependent. As observed in the primary endometrial cells, progestins and antiprogestins both act as agonists on the in vitro expression of this endometrial gene. Our findings provide insight into the regulation of this abundant endometrial protein and raise interesting questions about the physical nature of the interaction of agonist- and antagonist-bound progesterone receptors with the glycodelin gene promoter.

Drug Evaluation, Preclinical↗
PubMed1999

Glycodelin mRNA is expressed in the genital tract of male and female rats (Rattus norvegicus).

In the present study we demonstrate for the first time the expression of glycodelin mRNA in the female and male genital tracts of rats using non-radioactive in situ hybridisation. Glycodelin fragment 1 (+41 to +141) shares 100% homology with the human gene sequence. In the ovary, glycodelin mRNA was restricted to granulosa cells. In the uterus, glycodelin mRNA was expressed in all epithelial cells of the endometrium. In the male reproductive tract, glycodelin mRNA was distributed in all epithelial cells of the epididymis, the prostate and the seminal vesicle. However, in the testis, glycodelin mRNA was predominantly found in spermatogonia and in spermatocytes of the seminiferous epithelium. The expression in several reproductive organs of rats offers an excellent tool to study further the physiological role of glycodelin, which is so far thought to act as an immunosuppressive factor.

Animals↗
PubMed1998

Generation and characterization of a polyclonal antipeptide antibody to human glycodelin.

OBJECTIVE: To develop and characterize an antiglycodelin antibody using a 15-amino acid synthetic peptide as antigen, derived from the sequence of human glycodelin. DESIGN: We have developed a chicken antiglycodelin-derived peptide antibody and have characterized the antibody with the use of endometrial and ovarian cell lines. The antibody was also tested for its ability to detect glycodelin by ELISA assay, immunocytochemistry, and by Western blot. SETTING: Various cell lines, cell culture medium, and amniotic fluid were used in the experiments. PATIENT(S): Amniotic fluid was collected from pregnant patients in their first trimester of pregnancy. INTERVENTION(S): No intervention. MAIN OUTCOME MEASURE(S): Detection of glycodelin. RESULT(S): The cell lines RL95-2 (human endometrial carcinoma cells), OVCAR-3 (human ovarian adenocarcinoma cells), HeLa (human cervical epitheloid carcinoma cells), and EM42-D (human endometrial epithelial cells) reacted with the antibody, indicating the presence of glycodelin. A specific 45-kd protein representing glycodelin was detected by Western blot in the amniotic fluid. CONCLUSION(S): Antipeptide antibodies can be successfully used to detect and quantify the presence of glycodelin in cells and fluids.

Adenocarcinoma↗
PubMed1998

Glycodelins.

Glycodelins are 28 to 30-kD glycoproteins synthesized in various glands, notably those of the male and female reproductive organs. Depending on the site of origin, the same protein backbone is glycosylated in different ways, yielding glycodelins with different biological actions. Thus, human endometrium-derived glycodelin-A is temporally expressed in the latter half of the menstrual cycle, consists of unique sialylated and fucosylated lacdiNAc oligosaccharide sequences, and inhibits sperm-egg binding. By contrast, glycodelin-S from seminal vesicles has no such oligosaccharide sequences and no contraceptive activity. Glycodelin-A also has potent immunosuppressive properties, and its chemically modified forms inhibit transmission of HIV in vitro. Studies are reviewed suggesting that glycoforms dictate the function of human glycodelins, and that some of the oligosaccharide recognition sites present in the human gametes and immune cells have converged.

Alpha-Globulins↗
PubMed1995

Structural analysis of the oligosaccharides derived from glycodelin, a human glycoprotein with potent immunosuppressive and contraceptive activities.

Glycodelin, also known as placental protein 14 (PP14) or progesterone-associated endometrial protein (PAEP), is a human glycoprotein with potent immunosuppressive and contraceptive activities. In this paper we report the first characterization of glycodelin-derived oligosaccharides. Using strategies based upon fast atom bombardment and electrospray mass spectrometry we have established that glycodelin is glycosylated at Asn-28 and Asn-63. The Asn-28 site carries high mannose, hybrid and complex-type structures, whereas the second site is exclusively occupied by complex-type glycans. The major non-reducing epitopes in the complex-type glycans are: Gal beta 1-4GlcNAc (lacNAc), GalNAc beta 1-4GlcNAc (lacdiNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacdiNAc), Gal beta 1-4(Fuc alpha 1-3)GlcNAc (Lewisx), and GalNAc beta 1-4(Fuc alpha 1-3)GlcNAc (lacdiNAc analogue of Lewisx). It is possible that the oligosaccharides bearing sialylated lacNAc or lacdiNAc antennae may manifest immunosuppressive effects by specifically blocking adhesive and activation-related events mediated by CD22, the human B cell associated receptor. Oligosaccharides with fucosylated lacdiNAc antennae have previously been shown to potently block selectin-mediated adhesions and may perform the same function in glycodelin. The potent inhibitory effect of glycodelin on initial human sperm-zona pellucida binding is consistent with our previous suggestion that this cell adhesion event requires a selectin-like adhesion process. This result also raises the possibility that a convergence between immune and gamete recognition processes may have occurred in the types of carbohydrate ligands recognized in the human.

Amino Acid Sequence↗