Glycodelin-S in Human Seminal Plasma Reduces Cholesterol Efflux andInhibits Capacitation ofSpermatozoa

Chiu, Philip C.N.; Chung, Man-Kin; Tsang, H.Y.; Koistinen, Riitta; Koistinen, Hannu; Seppälä, Markku; Lee, Ckf; Yeung, William S.B.

doi:10.1074/jbc.m504103200

Cited by 79 publications

(70 citation statements)

References 50 publications

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“…Its glycans are unusually rich in fucose. The differences in carbohydrate moieties may explain the inability of glycodelin-S to bind to sperm FUT, and is consistent with the observation that the binding sites of glycodelin-S are different from other glycodelin isoforms (Chiu et al, 2005). However, glycodelin-F competes with glycodelin-A for binding to spermatozoa.…”

Section: Discussionsupporting

confidence: 72%

“…The bound glycodelin was eluted with 0.1% trifluoroacetic acid and dialysed against 100 mM sodium phosphate buffer (pH 7.2). Glycodelin-S was further purified by anionexchange chromatography (Chiu et al, 2005). The concentrations of the purified glycodelin isoforms were determined with a Bio-Rad Protein Assay Kit (Bio-Rad, Hercules, CA, USA).…”

Section: Purification Of Glycodelin Isoformsmentioning

confidence: 99%

“…The fallopian tube also expresses glycodelin in a hormone-dependent manner . Glycodelin-S maintains the spermatozoa in an uncapacitated state before their migration into the uterine cavity (Chiu et al, 2005), and glycodelin-F prevents premature progesterone-induced acrosome reaction (Chiu et al, 2003b).…”

Section: Introductionmentioning

confidence: 99%

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Glycodelin-A interacts with fucosyltransferase on human sperm plasma membrane to inhibit spermatozoa-zona pellucida binding

Chiu

Chung

Koistinen

et al. 2007

Journal of Cell Science

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Journal of Cell Science 34 suggest that the glycodelin receptor(s) and zona pellucida glycoprotein receptor(s) are closely related. The objectives of this study were to identify the receptor of glycodelin-A in human spermatozoa and to characterize its interaction with human zona pellucida. Results Fucosyltransferase 5 (FUT5) is a sperm surface glycodelin-A binding proteinThe results of identification of glycodelin-A-bound sperm surface protein(s) are shown in Figs 1, 2. Sulfosuccinimidyl-2-[6-(biotinamido)-2-(p-azidobenzamido)-hexanoamido]ethyl-1,3Ј-dithioproionate (Sulfo-SBED)-conjugated glycodelin-A was covalently bound to spermatozoa after photoactivation.Treatment of the glycodelin-A-sperm surface protein complexes with dithiothreitol (DTT; reducing conditions) resulted in reduction of the azo linkage and transfer of the biotin label from glycodelin-A to the sperm proteins. Thus, biotinylated glycodelin-A (Fig. 1A,B, lane 1) showed a single biotin band with molecular size ~30 kDa under non-reducing conditions, which was lost after DTT treatment (Fig. 1A,B, lane 2). One major biotinylated complex with size ~93 kDa appeared after incubation of glycodelin-A (Fig. 1A,B, lane 3) with the sperm extract. Treatment with DTT revealed a major biotinlabeled complex of size~65 kDa (Fig. 1A,B, lane 4). Some minor bands of smaller sizes were also seen. By contrast, glycodelin-A did not interact with fibroblasts and nonspecifically bound glycodelin-A was removed by washing of the cells after incubation. This is evidenced by the absence of a band in sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE; Fig. 1A,B, lane 6). Deglycosylated glycodelin-A did not interact with human spermatozoa (data not shown).Mass-spectrometry (MS) analysis of the tryptic digests and a database search identified the ~65 kDa glycodelin-A bound protein as FUT5 (Table 1). The six peptide sequences showed >90% match to the MS spectra and confirmed the protein identity at high confidence level. Two of the identified peptides, SFSWALAFCK and TELVAWAVSNWKPDSAR, were unique to FUT5 among fucosyltransferase 3 (FUT3), FUT5 and fucosyltransferase 6 (FUT6). The identity of the protein was confirmed by western blot analysis using the anti-FUT5 antibody, N-18 (Fig. 1C). The immunoreactivity was associated with bands of sizes ~93 and ~65 kDa, corresponding to the glycodelin-A-FUT complex in non-reducing conditions (Fig. 1C, lane 3) and FUT in reducing conditions (Fig. 1C, lane 4), respectively. Presence of FUT protein in human spermatozoaRecombinant FUT proteins were expressed in inclusion bodies and constituted for approximately 50% of the total protein of the transformed Escherichia coli. The yield of soluble protein was approximately 30-66 mg/l of culture. The expected sizes of recombinant FUT3, FUT5 and FUT6 are 51, 58 and 61 kDa, respectively. These recombinant FUTs were used to determine the specificities of the anti-FUT antibodies against different regions of the enzymes.Owing to the high sequence similarity (~90%) at the Cterminals, th...

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Section: Discussionsupporting

confidence: 72%

Section: Purification Of Glycodelin Isoformsmentioning

confidence: 99%

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Glycodelin-A interacts with fucosyltransferase on human sperm plasma membrane to inhibit spermatozoa-zona pellucida binding

Chiu

Chung

Koistinen

et al. 2007

Journal of Cell Science

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“…Glycodelin binding to ejaculated spermatozoa is positively correlated with sperm morphology (67). Glycodelin-S binds on the sperm head, thereby inhibiting cholesterol efflux and capacitation of the spermatozoa (52). Glycodelin-S is removed from spermatozoa as they migrate through the uterine cervix to reach the oocyte in the fallopian tube.…”

Section: Fertilisationmentioning

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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“…The percentage of sperm acrosome reaction was evaluated using a previously published methodological protocol (Chiu et al, 2005).…”

Section: Serum Hormone Measurement and Sperm Analysismentioning

confidence: 99%

Myoinositol improves sperm parameters and serum reproductive hormones in patients with idiopathic infertility: a prospective double-blind randomized placebo-controlled study

et al. 2015

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SUMMARYMale infertility is a multifactorial disorder that affects a significant percentage of couples. Its etiology and pathogenesis remain elusive in about one-third of the cases; this is referred to as idiopathic infertility. Inositols mediate the sperm processes involved into oocyte fertilization, such as penetration of the ovum cumulus oophorus, binding with the zona pellucida and the acrosome reaction. The aim of this double-blind, randomized, placebo-controlled trial was to evaluate the efficacy and safety of myoinositol (the most abundant form of inositols present in nature) treatment in men with idiopathic infertility. To accomplish this, we evaluated the effects of myoinositol on sperm parameters and reproductive hormones at baseline and after 3 months of treatment in men with idiopathic infertility. No adverse reaction was observed. Myoinositol significantly increased the percentage of acrosome-reacted spermatozoa, sperm concentration, and total count and progressive motility compared to placebo. In addition, myoinositol rebalanced serum luteinizing hormone, follicle-stimulating hormone, and inhibin B concentrations. The clinical improvement of idiopathic infertile patients should encourage myoinositol use for the treatment of this disorder, even though its detailed mechanisms at the testicular level remain still unclear.

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Glycodelin-S in Human Seminal Plasma Reduces Cholesterol Efflux andInhibits Capacitation ofSpermatozoa

Cited by 79 publications

References 50 publications

Glycodelin-A interacts with fucosyltransferase on human sperm plasma membrane to inhibit spermatozoa-zona pellucida binding

Glycodelin-A interacts with fucosyltransferase on human sperm plasma membrane to inhibit spermatozoa-zona pellucida binding

Glycodelin in reproductive endocrinology and hormone-related cancer

Myoinositol improves sperm parameters and serum reproductive hormones in patients with idiopathic infertility: a prospective double-blind randomized placebo-controlled study

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