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J. Biol. Chem., Vol. 275, Issue 30, 22631-22634, July 28, 2000

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ACCELERATED PUBLICATION
The 1,3-Galactosyltransferase 3GalT-V Is a Stage-specific Embryonic Antigen-3 (SSEA-3) Synthase^*

Dapeng Zhou, Timothy R. Henion^§, Firoze B. Jungalwala^§, Eric G. Berger, and Thierry Hennet^¶

From the Institute of Physiology, University of Zürich, Winterthurerstrasse 190, 8057 Zürich, Switzerland and the ^§ Eunice Kennedy Shriver Center, Waltham, Massachusetts 02452

Received for publication, April 18, 2000, and in revised form, May 29, 2000

	ABSTRACT

TOP ABSTRACT INTRODUCTION EXPERIMENTAL PROCEDURES RESULTS DISCUSSION REFERENCES

We have previously reported the molecular cloning of 1,3-galactosyltransferase-V (3GalT-V), which catalyzes the transfer of Gal to GlcNAc-based acceptors with a preference for the core3 O-linked glycan GlcNAc(1,3)GalNAc structure. Further characterization indicated that the recombinant 3GalT-V enzyme expressed in Sf9 insect cells also utilized the glycolipid Lc3Cer as an efficient acceptor. Surprisingly, we also found that 3GalT-V catalyzes the transfer of Gal to the terminal GalNAc unit of the globoside Gb4, thereby synthesizing the glycolipid Gb5, also known as the stage-specific embryonic antigen-3 (SSEA-3). The SSEA-3 synthase activity of 3GalT-V was confirmed in vivo by stable expression of the human 3GalT-V gene in F9 mouse teratocarcinoma cells, as detected with the monoclonal antibody MC-631 by flow cytometry analysis and immunostaining of extracted glycolipids. The biological relation between SSEA-3 formation and 3GalT-V was further documented by showing that F9 cells treated with the differentiation-inducing agent retinoic acid induced the expression of both the SSEA-3 epitope and the endogenous mouse 3GalT-V gene. This study represents the first example of a glycosyltransferase, which utilizes two kinds of sugar acceptor substrates without requiring any additional modifier molecule.

	INTRODUCTION

TOP ABSTRACT INTRODUCTION EXPERIMENTAL PROCEDURES RESULTS DISCUSSION REFERENCES

Glycosyltransferase enzymes mediate the synthesis of glycosylated structures by catalyzing the transfer of sugar units to various acceptor molecules utilizing nucleotide-activated sugars as donor substrates. In most cases, a single glycosyltransferase enables the transfer of one type of carbohydrate donor to one type of carbohydrate acceptor, although some exceptions have been reported. The lgtA glycosyltransferase from Neisseria meningitidis represents such an exception, as it can transfer two donors, GlcNAc and GalNAc, to Gal-based acceptors (1). Another notable exception is represented by the 1,4-galactosyltransferase-I enzyme, which is able to change its acceptor substrate specificity from GlcNAc to Glc by interacting with -lactalbumin (2, 3).

Previous work from this group and other laboratories has revealed a family of structurally related 1,3-glycosyltransferase enzymes (4-10). During the course of our investigation, we have found that one member of this family, the 1,3-galactosyltransferase (3GalT)¹-V enzyme that normally act on GlcNAc-based acceptors, can catalyze the transfer of galactose to GalNAc presented in the context of the Gb4 globoside structure. The resulting product, the Gb5 globoside, is also known as the stage-specific embryonic antigen (SSEA)-3 (11), which is found in the 4-8 cell stage mouse embryo as well as some adult tissues. We have established the SSEA-3 synthase activity of 3GalT-V both in vitro and in vivo in F9 mouse teratocarcinoma cells as a model system.

	EXPERIMENTAL PROCEDURES

TOP ABSTRACT INTRODUCTION EXPERIMENTAL PROCEDURES RESULTS DISCUSSION REFERENCES

Galactosyltransferase Assays-- The human 3GalT-V enzyme was expressed in Sf9 insect cells as a recombinant baculovirus as described previously (10). Enzyme assays with glycolipid acceptors were prepared with 10 µl of baculovirus-infected cell lysate in a 50-µl reaction volume containing 100 mM sodium cacodylate (pH 7.0), 10 mM MnCl₂, 10 mM CDP-choline, 0.4% Triton CF-54, 0.2 mM UDP-[¹⁴C]galactose (1 × 10⁵ cpm/nmol) and either 20 µg of Gb4 (Matreya, Pleasent Gap, PA) or 5 µg of Lc3Cer. Incubations were performed for 4 h at 37 °C, then stopped by the addition of 0.1 M potassium chloride/methanol:H₂O:chloroform (48:47:3), and lipid products purified by reverse phase extraction on Bond-Elut C₁₈ columns (Varian). Lipid residues dried under N₂ were reconstituted in chloroform:methanol (1:1) and spotted onto silica gel-60 high-performance TLC plates (E. Merck, Darmstadt, Germany) and developed with a solvent of chloroform:methanol:0.25% CaCl₂ (5:4:1). Radiolabeled products were visualized by autoradiography.

Transfection of F9 Teratocarcinoma Cells-- The mouse teratocarcinoma cell line F9 was obtained from ATCC (CRL-1720) and grown in Dulbecco's modified Eagle's medium with 10% fetal calf serum on tissue culture plates precoated with 0.1% gelatin (Sigma). The protein-coding region of the human 3GalT-V gene (10) was ligated into the BamHI and XhoI sites of the pcDNA3.1⁺ expression vector (Invitrogen). 5 µg of the resulting vector were introduced into F9 cells by LipofectAMINE (Life Technologies, Inc.)-mediated transfection. G418 (Life Technologies, Inc.) was added 24 h post-transfection at 600 µg/ml, and surviving cell clones were picked after 10 days.

Flow Cytometry-- The monoclonal antibody MC-631 (12) was purchased from the Developmental Studies Hybridoma Bank (Iowa City, IA). G418-resistant cells (5 × 10⁵) were first incubated with MC-631 diluted 1:100 for 15 min on ice. A fluorescein isothiocyanate-labeled rabbit anti-rat IgM antibody (Zymed Laboratories Inc., San Francisco, CA) diluted at 1:500 was used as secondary reagent. Labeled cells were analyzed in a FACScan flow cytometer (Becton Dickinson).

Glycolipid Analysis-- Glycolipids were extracted from NCCIT (ATCC, CRL-2073) and 3GalT-V expressing F9 cells as described previously (13). Lipids were separated into neutral and ganglioside species by fractionation on DEAE-Sephadex A-25 (Sigma). Immunostaining of extracted glycolipids was performed essentially as described previously (14). Briefly, glycolipid species were chromatographed on aluminum high-performance TLC plates (E. Merck) in a solvent system of chloroform:methanol:0.25% CaCl₂. Plates were fixed with 0.05% poly(isobutyl methacrylamate) in n-hexane and blocked with 5% bovine serum albumin prior to 4 °C incubation with 1:5 diluted MC-631 hybridoma supernatant. After washing and incubation with 1:400 diluted peroxidase-conjugated goat anti-mouse IgM (Roche Molecular Biochemicals), reactivity was visualized with 4-chloronapthol substrate (Sigma).

Retinoic Acid Treatment-- F9 cells were seeded at low density (5,000 cells/80-cm² dish) and treated with 10⁷ M all-trans-retinoic acid (Sigma) for 10 days. Cells were analyzed for SSEA-3 expression by flow cytometry as described above.

Cloning and Expression of the Mouse 3GalT-V Gene-- A 129/SvJ mouse genomic -library (Stratagene) was screened as described previously (4) using the human 3GalT-V gene as a probe. The genomic region, including the sequence encoding the catalytic domain of the 3GalT-V enzyme, was amplified by PCR with the primers 5'-CAGCATGAATTCTTTCAGAGAACTCC-3' and 5'-GCAAGAGGATCCCAGATCGTCACAAA-3' and subcloned into the pFLAG-CMV-1 vector (Sigma). The medium of COS-7 cells transiently transfected with the 3GalT-V vector was incubated with 20 µl of anti-FLAG M2-agarose beads (Sigma) for 2 h at 4 °C. After washing three times with phosphate-buffered saline, the beads were directly used for galactosyltransferase assays. For metabolic labeling, transfected cells were starved for 2 h in methionine-free Dulbecco's modified Eagle's medium, then incubated in the presence of 0.1 mCi of [³⁵S]methionine for 1 h. After replacement with complete medium, cells were further incubated for 4 h at 37 °C. After this time, the cell supernatant was collected and incubated with anti-FLAG M2-beads as described above.

Reverse Transcription (RT)-PCR-- Total RNA was extracted from F9 cells using the procedure of Chomczynski and Sacchi (15). RNA samples were digested with RNase-free DNase-I (Sigma) before RT-PCR. The mouse 3GalT-V RNA (5 µg) was reverse-transcribed using 1 unit of enhanced avian myeloblastosis virus reverse transcriptase (Sigma) and the primer 5'-AGTCCTGTTCTTTCGAGTTCTC-3'. Samples in a final volume of 20 µl were incubated for 2 h at 42 °C. PCR amplification was performed using 4 units of Taq polymerase (Sigma) with 10 µl of the RT reaction product and the primers 5'-CAAGGATGCCTACTTCAACCTG-3', 5'-CCAGGGAAGAAGGTCTGTTTGG-3' for 35 cycles at 95 °C for 45 s, 55 °C for 30 s, and 72 °C for 60 s. Using the same RT-PCR conditions, as an internal control the mouse GAPDH mRNA was reverse-transcribed with the primer 5'-CCCTGTTGCTGTAGCCGTATTC-3' and amplified with primers 5'-TTGGCATTGTGGAAGGGCTCAT-3' and 5'-CCCTGTTGCTGTAGCCGTATTC-3'. The human 3GalT-V RNA was detected in the NCCIT cell line (ATCC, CRL-2073) by RT-PCR with the RT primer 5'-GAAAGGATTTAGACTGTACATGC-3' and the PCR primers 5'-GAAAGGATTTAGACTGTACATGC-3' and 5'-GTGAATTCCTCTTTCTCTCTGCTG-3' using the same conditions as described above.

	RESULTS

TOP ABSTRACT INTRODUCTION EXPERIMENTAL PROCEDURES RESULTS DISCUSSION REFERENCES

During our investigation of the donor and acceptor substrate specificity of the 3GalT-V enzyme, we have found that this enzyme exhibited a preference for GlcNAc-based acceptors (10). However, when assaying glycolipid acceptors, the 3GalT-V enzyme showed activity toward the lacto-series glycolipid Lc3Cer and toward the globoside Gb4 (Fig. 1). The latter activity was surprising as the 3GalT-V enzyme displayed no activity toward the monosaccharide GalNAc(/-O-benzyl) acceptors (10). In addition, the Gb5 synthase activity of 3GalT-V did not require any modifier protein, since a FLAG-tagged soluble form of the 3GalT-V enzyme was capable of catalyzing the formation of Gb5 when affinity-purified on anti-FLAG M2-agarose beads (Fig. 2). By comparison, the 3GalT-I, -II, -III enzymes characterized previously (4, 5, 7) did not display any dual activity toward GlcNAc and GalNAc-based acceptors (data not shown).

View larger version (44K): [in this window] [in a new window]   Fig. 1.   SSEA-3 synthase activity of 3GalT-V in vitro. Lysate from Sf9 cells infected with recombinant 3GalT-V baculovirus or with a mock baculovirus were incubated with or without Gb4 glycolipid acceptors. The left panel shows the orcinol staining of the reaction products resolved on a thin-layer chromatography plate. The right panel shows an autoradiogram of the same plate. The migration of the standard glycolipids LacCer and Gb4 is indicated on the left.

View larger version (73K): [in this window] [in a new window]   Fig. 2.   Purification of the soluble tagged 3GalT-V enzyme. The supernatants of COS-7 cells transfected with a mock vector or with a FLAG-tagged soluble 3GalT-V construct were analyzed after 1-h labeling with [35S]methionine. Cell supernatant proteins bound to anti-FLAG M2-agarose beads were separated on SDS-polyacrylamide gel electrophoresis and autoradiographed. The results from two transfections (1) and (2) are shown. The arrow at the right indicates the expected size of the FLAG-tagged soluble 3GalT-V protein.

To establish whether the 3GalT-V enzyme is capable of catalyzing the synthesis of the Gb5 structure in vivo, we chose to overexpress the human 3GalT-V gene in F9 teratocarcinoma cells. This cell line is known to express the Gb4 globoside but lacks the Gb5 synthase activity (16). F9 cells stably expressing the human 3GalT-V gene were first analyzed for the presence of the Gb5 product by flow cytometry. As shown in Fig. 3A, F9 cells expressing the human 3GalT-V gene showed increased levels of the SSEA-3 epitope at their surface when compared with F9 cells transfected with a mock vector. For a comparison, the human teratocarcinoma cell line NCCIT showed a high level of SSEA-3 expression as reported earlier (16). Immunostaining of glycolipids extracted from 3GalT-V-transfected F9 cells also clearly indicated the synthesis of Gb5 structure in vivo (Fig. 3B). The globo-series ganglioside GL7, also termed SSEA-4, was also detected in the upper Folch fraction of the glycolipid extract in the transfected cells by immunostaining with MC-631 antibody (data not shown), thus indicating that the Gb5 product was further sialylated in F9 cells.

View larger version (36K): [in this window] [in a new window]   Fig. 3.   SSEA-3 biosynthesis in F9 cells overexpressing 3GalT-V. A, flow cytometry analysis of teratocarcinoma cells. The left panel shows NCCIT cells stained with the FITC-labeled rabbit anti-rat IgM secondary antibody alone (thin line) or with both primary anti-SSEA-3 MC-631 and secondary antibodies (thick line). On the right panel, wild-type F9 cells (thin line) and F9 cells overexpressing the 3GalT-V gene (thick line) were stained with primary MC-631 and secondary FITC-rabbit anti-rat IgM antibodies. B, neutral glycolipids extracted from NCCIT, F9 cells expressing a mock vector, and two sets of F9 cells expressing 3GalT-V (A/B) were resolved by thin-layer chromatography. The left panel shows the immunostaining of the plate with MC-631 antibody and the right panel the orcinol staining of the same extracts. The positions of the glycolipid standards are marked at the right.

The relation between 3GalT-V and the induction of SSEA-3 was further investigated in wild-type F9 cells. Treatment of F9 teratocarcinoma cells with retinoic acid is known to promote cell differentiation and to induce the expression of the SSEA-3 epitope (17) (Fig. 4A). To determine whether the increase in SSEA-3 levels is paralleled by the induction of 3GalT-V gene transcription, we first cloned and expressed the mouse 3GalT-V (GenBank^TM accession number AF254738). The mouse protein is 308 amino acid long and shows 71% identity to the human 3GalT-V at the amino acid level. The mouse 3GalT-V enzyme exhibited a galactosyltransferase activity when transiently expressed in COS-7 cells (data not shown). The presence of 3GalT-V mRNA in F9 cells was analyzed by RT-PCR. As shown in Fig. 4B, F9 cells treated with retinoic acid for 10 days were positive for 3GalT-V transcript, whereas untreated F9 cells remained negative. As a comparison, human 3GalT-V mRNA was also detected in NCCIT cells, which constitutively express SSEA-3 at their surface (see Fig. 3A). This experiment demonstrated that the expression of the 3GalT-V gene correlates with the induction of the SSEA-3 epitope.

View larger version (35K): [in this window] [in a new window]   Fig. 4.   SSEA-3 and 3GalT-V induction in differentiating F9 cells. A, flow cytometry analysis of MC-631-stained F9 cells treated for 10 days with 107 M retinoic acid (thick line, F9+RA) or with control solvent (thin line, F9-RA) B, detection of 3GalT-V transcripts in teratocarcinoma cells. The lanes represent the PCR products obtained from: cDNA of F9 cells treated with retinoic acid (lane 1), cDNA of F9 cells treated with solvent (lane 2), RNA of F9 cells treated with retinoic acid (lane 3), RNA of F9 cells treated with solvent (lane 4), and cDNA of NCCIT cells (lane 5). The bottom gel shows the detection of the GAPDH mRNA as a control in samples 1-4. The positions of the mouse 3GalT-V (435 bp) and the mouse GAPDH (468 bp) PCR fragments are marked at the left. The position of the human 3GalT-V (349 bp) PCR fragment is shown at the right.

	DISCUSSION

TOP ABSTRACT INTRODUCTION EXPERIMENTAL PROCEDURES RESULTS DISCUSSION REFERENCES

In the present study, we report a dual acceptor specificity for the 3GalT-V enzyme by establishing its ability to transfer Gal to the terminal GalNAc residue of Gb4 in addition to its activity toward GlcNAc-based acceptors (9, 10). This represents one of the few glycosyltransferases reported to date, which are capable of transferring a donor sugar molecule to different terminal monosaccharide acceptors. The best documented case is the 1,4-galactosyltransferase-I enzyme, which is able to use both GlcNAc and Glc as substrates (2, 3). However, whereas the 1,4-galactosyltransferase-I enzyme must interact with another modifier molecule, -lactalbumin, to switch the substrate specificity from GlcNAc to Glc, the 3GalT-V enzyme does not require any additional modifier to switch from one acceptor substrate to the other.

3GalT-V is the first member of the recently cloned 3GalT family that utilizes Gb4 as an acceptor. While the tissue distribution pattern of the SSEA-3 epitope and its biochemical nature have been characterized for many years, a distinct 3GalT enzyme with SSEA-3 synthase activity has yet to be cloned. It remains unclear whether 3GalT-V is the only enzyme that can perform this role in vivo. Also, it must be established whether the SSEA-3 synthase activities from human teratocarcinoma cells (18) and from mouse kidney (19) represent orthologous proteins.

The human and mouse 3GalT-V genes displayed differences in their tissue expression patterns. The human 3GalT-V gene was mainly expressed in small intestine, pancreas, and testis (10), and mouse 3GalT-V transcripts were mainly detected in brain and kidney but not in testis (data not shown). Noteworthy, expression of SSEA-3 has been reported to be confined to the kidneys in adult mice (20). However, it is difficult to relate the pattern of expression of the 3GalT-V gene with the distribution of SSEA-3 among tissues, since additional factors, such as the availability of the Gb4 acceptor, will also affect the presence or absence of the antigen on specific cell types.

The parallel induction of SSEA-3 and 3GalT-V expressions in F9 cells treated with retinoic acid supports the concept of a direct relation between both events. Nevertheless, we cannot exclude the existence of other 3GalT enzymes, which may participate to the formation of SSEA-3 in vivo. On the other hand, it is also possible that the SSEA-3 synthase activity indeed represents a second activity of the type-1 chain synthase 3GalT-V enzyme. In this case, the enzyme may function either way depending on the levels of the respective acceptor available in cells. The targeted inactivation of the mouse 3GalT-V gene will provide answers to this question and may represent a valuable model to address the biological functions associated to SSEA-3 during embryonic development.

	ACKNOWLEDGEMENTS

We thank Vincent Riglet and Dr. Martine Malissard for technical assistance and helpful suggestions. We are also grateful to Dr. Omanand Koul for providing the Gb5 standards and for his valuable technical advice.

	FOOTNOTES

^* This work was supported by the Swiss National Science Foundation Grant 31-58577.99 and by United States Public Health Service, National Institutes of Health Grants R01-NS24405 and PO1-HD05505.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EMBL Data Bank with accession number(s) AF254738.

Both authors contributed equally to this work.

^¶ To whom correspondence should be addressed: Institute of Physiology, Winterthurerstrasse 190, 8057 Zurich, Switzerland. Tel.: 41-1-635-5080; Fax: 41-1-635-6814; E-mail: thennet@access.unizh.ch.

Published, JBC Papers in Press, June 2, 2000, DOI 10.1074/jbc.C000263200

	ABBREVIATIONS

The abbreviations used are: 3GalT, 1,3-galactosyltransferase; SSEA, stage-specific embryonic antigen; RT, reverse transcription; PCR, polymerase chain reaction; Gb4, GalNAc(1,3)Gal(1,4)Gal(1,4)Glc-ceramide; Gb5, Gal(1,3)GalNAc(1,3)Gal(1,4)Gal(1,4)Glc-ceramide; GL7, Sia(2,3)Gal(1,3)GalNAc(1,3)Gal(1,4)Gal(1,4)Glc-ceramide; Lc3Cer, GlcNAc(1,3)Gal(1,4)Glc-ceramide; FITC, fluorescein isothiocyanate; GAPDH, glyceraldehyde-3-phosphate dehydrogenase; bp, base pair(s).

	REFERENCES

TOP ABSTRACT INTRODUCTION EXPERIMENTAL PROCEDURES RESULTS DISCUSSION REFERENCES

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This Article Abstract Full Text (PDF) All Versions of this Article: 275/30/22631    most recent C000263200v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Zhou, D. Articles by Hennet, T. Search for Related Content PubMed PubMed Citation Articles by Zhou, D. Articles by Hennet, T. Social Bookmarking                      What's this?