ARTICLE

Presence of H Type 3/4 Chains of ABO Histo-blood Group System in Serous Cells of Human Submandibular Gland and Regulation of Their Expression by the Secretor Gene (FUT2)

Correspondence to: Hiroshi Kimura, Dept. of Forensic Medicine, Kurume Univ. School of Medicine, Kurume 830-0011, Japan.

	Summary

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We have investigated by immunochemistry the distribution of H Type 3/4 chains of the ABO histo-blood group system in human submandibular gland using a monoclonal anti-H MBr1 antibody specific for H Type 3/4 chains, and have found the expression of H Type 3/4 chains was mainly in the serous cells. Serous cells from secretors were stained by MBr1 but not by anti-A and anti-B antibodies, whereas serous cells from nonsecretors exhibited a negative reaction with MBr1. Mucous cells were not stained by MBr1. Only a few striated duct cells showed a weak reaction with anti-H MBr1. These results suggested that the H Type 3/4 chains were distributed predominantly in the serous cells of the human submandibular gland and that secretor Type (1,2)fucosyltransferase (Se enzyme) controlled the synthesis of H Type 3/4 chains in vivo. Saliva also contained H Type 3/4 chains, which were controlled by the secretor gene (FUT2). The differences in the distributions of H Type 1, H Type 2, and H Type 3/4 chains of the ABO histo blood group system in the submandibular gland are discussed. (J Histochem Cytochem 47:889–894, 1999)

Key Words: ABO, MBr1, H type 3 chain, H type 4 chain, secretor gene (FUT2), submandibular gland

	Introduction

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Because carbohydrate chains are the ABO histo- blood group determinants, their expression is under control of the genes that encode specific glycosyltransferases (Oriol et al. 1986 ). The epitope of the H antigen, the precursor of A, B, Le^Y, and Le^b antigens of ABO and Lewis histo-blood groups, is carried by at least four different types of internal carbohydrate backbone (Type 1, Galß1-3GlcNAcß1-R; Type 2, Galß1-4GlcNAcß1-R; Type 3, Galß1-3GalNAc1-R; Type 4, Galß1-3GalNAcß1-R) (Clausen and Hakomori 1989 ). However, much less is known about the distribution and the amount of each type of chain of the ABO antigens in tissues. We have previously measured the H Type 1 and H Type 2 substances in human saliva using synthetic oligosaccharides as the standard substances and found that the concentration of H Type 2 chain in saliva was about 5–10% that of H Type 1 chain (Wang et al. 1994 ). We have also immunohistochemically determined the differences in distribution of H Type 1 and H Type 2 antigens in human submandibular gland using specific monoclonal antibodies (MAbs) (Liu et al. 1998 ), in which we demonstrated the distribution of H Type 1 chain in mucous cells and in duct cells and of H Type 2 chain in duct cells and in vascular endothelial cells. However, no H Type 1 and no H Type 2 chains were demonstrated in the serous cells of the submandibular gland, despite the presence in the serous cells of Ulex europaeus I (UEA-I)-positive substances that appeared to be regulated by the secretor gene.

In this study, we used MAb anti-H MBr1, which is defined as a breast cancer-associated antigen and is specific for H Type 3/4 antigens (Menard et al. 1983 ; Bremer et al. 1984 ; Kannagi et al. 1984 ; Clausen et al. 1986a , Clausen et al. 1986b ; Adobati et al. 1997 ), to examine the distribution of H Type 3/4 chains in cell types of the human submandibular gland through an immunohistochemical method, and have demonstrated that the H Type 3/4 chains were expressed mainly in the serous cells, with their expression dependent on the secretor status.

	Materials and Methods

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The ABO histo-blood group phenotypes of tissue donors were determined on red blood cells using the conventional hemagglutination method with mouse MAbs (Kokusai; Kobe, Japan) against histo-blood group antigens A and B (Liu et al. 1996 ). In addition, the Se genotypes of tissue donors were determined by PCR after extraction of DNA from frozen salivary glands, as described previously (Koda et al. 1996 ).

Two anti-H MAbs, MBr1 and 1E3, were used in the present study. MAb MBr1, specific for H Type 3/4 structures (Fuc1-2Galß1-3GalNAc-) (Bremer et al. 1984 ; Clausen et al. 1986a , Clausen et al. 1986b ; Adobati et al. 1997 ), was a kind gift from Dr. Maria I. Colnaghi (Division of Experimental Oncology E, National Institute for Cancer Research; Milan, Italy). Anti-H MAb 1E3 was a kind gift from Drs. Ken Furukawa and Shin Yazawa (Department of Legal Medicine, Gunma University School of Medicine). The anti-H 1E3 has been demonstrated to be reactive with H Type 1–H Type 4 oligosaccharides and to be reactive with Fuc1-2Galß disaccharide, using a series of synthetic oligosaccharides (Nakajima et al. 1993 ), but to be reactive predominantly with the H Type 1 and H Type 2 antigens in situ in the submandibular gland, as shown in our previous study (Liu et al. 1998 ).

Submandibular glands from individuals with different ABO histo-blood groups were obtained from autopsy cases (five secretors and four nonsecretors from O blood group individuals and four secretors from A and four secretors from B blood group individuals). Deparaffinized sections of 10% formalin-fixed, paraffin-embedded submandibular glands were immunostained using the streptavidin–biotin complex immunoperoxidase method as described previously (Liu et al. 1998 ). The primary MAbs, anti-H MBr1, anti-H 1E3, anti-A, or anti-B, diluted 500 times in PBST (0.01 M phosphate buffer, pH 7.4, 0.15 M NaCl, and 0.5% Tween 20), were reacted at 4C overnight in a moist chamber.

A dot ELISA was carried out as described previously (Liu et al. 1996 , Liu et al. 1998 ). Briefly, boiled human saliva samples were diluted in twofold serial dilution, and 1 µl of each of the diluted samples was dotted onto a nitrocellulose membrane. After quenching intrinsic peroxidase activity with 3% H₂O₂, the nitrocellulose membrane was blocked with 0.05% Tween 20 in 0.9% NaCl. Then the antigenicity was detected using MAb MBr1 or 1E3 (both diluted 200 times), followed by peroxidase-conjugated goat anti-mouse IgM (Cappel; West Chester, PA) and 4-chloro-1-naphthol for color development.

To examine whether the H Type 3/4 antigens were synthesized by the H enzyme or the Se enzyme, the wild-type allele of the FUT1 for H enzyme or the FUT2 for Se enzyme was subcloned into a mammalian expression vector pRc/CMV (Invitrogen; San Diego, CA) (pRc/CMV-H or pRc/CMV-Se), as described previously (Koda et al. 1996 , Koda et al. 1997 ). The plasmid (pRc/CMV-H or pRc/CMV-Se) was transfected into COS7 cells by a DEAE–dextran method (Gonzalez and Joly 1995 ). After 48 hr of culture, the expression of H antigens on cells was examined using anti-H MBr1 or anti-H 1E3 and fluorescein-labeled anti-mouse IgM (Koda et al. 1993 ).

	Results

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The murine MAb MBr1, raised against the human breast cancer cell line MCF-7, recognized a saccharide epitope on human breast, ovary, and lung carcinomas (Mariani-Costantini et al. 1984a , Mariani-Costantini et al. 1984b ; Martignone et al. 1993 ; Perrone et al. 1993 ). This antigen was originally identified as a globo series glycosphingolipid with an H-like determinant at its terminus (Fuc1-2Galß1-3GalNAcß1-3Gal1-4Galß1-4Glcß1-Cer) in MCF-7 cells (Bremer et al. 1984 ). Later, it was shown that MBr1 recognized the trisaccharide sequence (Fuc1-2Galß1-3GalNAc, H Type 3/4) on glycolipids and on glycoproteins, irrespective of the anomeric structure of the internal GalNAc residue (Clausen et al. 1986a , Clausen et al. 1986b ). Recently, Adobati et al. 1997 demonstrated that MBr1 was more specific for Fuc1-2Galß1-3GalNAcß1 (H Type 4 chain).

Previous studies have revealed the presence of Type 3 chain-based ABH antigens in saliva and ovarian cyst fluids (Donald 1981 ) and in seminal plasma (Hanischi et al. 1986 ) after isolation and chemical characterization. In dot ELISA, anti-H MBr1 reacted with human saliva from secretor individuals but not with saliva from nonsecretors (Figure 1). This finding indicated that human saliva contained H Type 3/4 chains and that their secretion was dependent on the secretor status.

View larger version (38K): [in this window] [in a new window]   Figure 1. Reaction of saliva with anti-H MBr1 and anti-H 1E3 on dot ELISA. The saliva from secretor individuals showed a positive reaction with anti-H MBr1 (B) and anti-H 1E3 (A), but that from nonsecretors showed a negative reaction with each antibody. Numbers at top indicate dilutions of saliva samples.

Next, we immunohistochemically investigated the human submandibular gland using anti-H MBr1 and anti-H 1E3 (Figure 2). Serous cells and some serous demilune cells from secretor donors, but not from nonsecretor donors, were stained intensely by anti-H MBr1, irrespective of ABO phenotypes (Figure 2A and Figure 3A). These results suggested that the production of H Type 3/4 antigens in serous cells of human submandibular glands was under the control of the Se gene. In contrast, mucous acini, vascular endothelia, and erythrocytes showed no reaction with anti-H MBr1, although these cells showed a good reaction with anti-H 1E3 (Figure 2), anti-A (Figure 3), or anti-B (not shown) in tissues from corresponding ABO group individuals. Positive staining by MBr1 was observed in the luminal surface and luminal contents of many striated ducts, but only a few epithelial cells (less than 1%) of striated ducts showed a weak reaction with MBr1. Staining by 1E3 appeared to localize on basolateral plasma membranes of striated duct cells, and this mode of distribution obviously differed from that in mucous cells (Figure 2B and Figure 2D). Epithelial cells of interlobular ducts demonstrated a negative reaction with MBr1 (not shown). In the submandibular gland of A secretors, we also observed a strong reaction with anti-A in mucous acini (Figure 3) and a weak reaction in some ducts, but no reaction in serous acini despite the strong staining by anti-H MBr1 in serous cells, suggesting the expression of the ABO gene in mucous cells and duct cells but not in serous cells. It appeared that all serous cells from the A secretors showed a positive reaction with MBr1 (Figure 3A), whereas only a portion of serous cells from the O secretors reacted with the antibody (Figure 2A). The difference in staining of serous cells between A and O secretors was due to individual variation. All results are summarized in Table 1.

View larger version (109K): [in this window] [in a new window]   Figure 2. Serial sections of submandibular gland from an O secretor stained by anti-H MBr1 (A) or by anti-H 1E3 (B), and those from an O nonsecretor stained by MBr1 (C) or by 1E3 (D). The strong staining of serous acini (double arrows) by MBr1, but not by 1E3, was dependent on secretor status. Mucous acini (arrows) from a secretor reacted with 1E3 but not with MBr1. The majority of striated duct cells (arrowheads) were not labeled by MBr1, whereas luminal surface and luminal contents showed a positive reaction with MBr1. Striated duct cells were well stained by anti-H 1E3. Bar = 50 µm.

View larger version (132K): [in this window] [in a new window]   Figure 3. Immunohistochemical staining of the submandibular gland from an A secretor by anti-H MBr1 (A) and by anti-A (B). Serous acini (double arrows) were strongly stained by anti-H MBr1 but not by anti-A. Mucous acini (arrows) were stained by anti-A but not by anti-H MBr1. The apical surfaces of striated ducts (arrowheads) were labeled by anti-H MBr1. Anti-A showed a strong reaction with apical surface and basal membranes of striated ducts. Bar = 50 µm.

COS7 cells transfected by the H gene (FUT1) or the Se gene (FUT2) showed strong fluorescence with both anti-H MBr1 and 1E3 (not shown), suggesting that both (1,2)fucosyltransferases (H enzyme and Se enzyme) can fucosylate a precursor of Type 3 or Type 4 to form H Type 3 chain or H Type 4 chain in vitro, consistent with a previous report (Henry et al. 1996 ).

	Discussion

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In this study we examined immunohistochemically the location of H Type 3/4 antigens in cell types in the human submandibular gland using anti-H MBr1, and we identified cell types expressing H Type 3/4 chains as serous cells. Our results extended previous observations (Ito et al. 1989 ; Cossu et al. 1990 ; Cossu and Lantini 1996 ), which implied the presence of the H antigen in serous cells of human submandibular gland by lectin histochemical and immunoelectron microscopic methods. From our previous and present studies, we have now clearly identified cell types expressing H Type 1, H Type 2, and H Type 3/4: H Type 1 in mucous cells and duct cells, H Type 2 in duct cells, and H Type 3/4 in the serous cells of the submandibular gland (Table 2) (Liu et al. 1998 ). The expression of H Type 1 in mucous cells and of H Type 3/4 in serous cells was regulated by the Se enzyme in vivo. However, the H enzyme also can form H Type 3/4 antigens, as demonstrated by the positive reaction with MBr1 on COS7 cells after transfection of the H gene (FUT1).

The H Type 3 has been found in ovarian cyst fluid and saliva (Donald 1981 ) and in erythrocytes (Clausen et al. 1986a ) from individuals with blood group A. The H Type 3 glycosphingolipid (a precursor of repetitive A) (Fuc1-2Galß1-3GalNAc1-3[Fuc1-2]Galß1-4GlcNAcß1-3Galß1-4GlcNAc-Cer) was constructed by adding a Gal residue and then a Fuc residue sequentially to the terminal GalNAc of the A Type 2 structure. Alternatively, the formation of the H Type 3 chain needs both the H Type 2 chain as a precursor and the activity of A glycosyltransferase. The other Type 3 chain-based H antigen is a fucosylated T antigen (Fuc1-2Galß1-3GalNAc1-O-Ser/Thr), which has been found in the mucosa of the stomach and colon (Macartney 1986 ; Nakayama et al. 1987 ; Okada et al. 1994 ). Using peanut agglutinin (PNA) and glycosidase digestion, Ito et al. 1989 concluded that O-linked Type 3 chain-based H antigen (Fuc1-2Galß1- 3GalNAc1-O-Ser/Thr) was produced in serous cells and that its fucosylation was under the control of the Se gene in human submandibular glands. Okada et al. 1994 also demonstrated the expression of the Thomsen–Friedenreich antigen (T antigen) (Galß1-3GalNAc-O-Ser/Thr) and fucosylated T antigen (H Type 3) in human gastric surface epithelial cells and the dependency of its fucosylation on the Se gene, using anti-H MBr1 and PNA as probes. However, the specificity of PNA has been questioned because of different distributions of PNA-positive and anti-T-positive substances before and after neuraminidase treatment and different reactivities of PNA and anti-T antibody after galactose oxidation (Macartney 1986 ; Nakayama et al. 1987 ). Ito et al. 1989 reported that PNA-reactive substances were not accumulated in serous cells of the submandibular gland from nonsecretors.

In this study we have demonstrated that reactivity of anti-H MBr1 was found in the serous cells of the submandibular gland from O individuals, and that anti-A- and anti-H MBr1-positive substances were present in different cell types of the submandibular gland from A individuals, suggesting that an MBr1-reactive substance appeared to be not a precursor of repetitive A (H Type 3 glycosphingolipid). Moreover, no A, B, or H Type 2 antigens were detected in serous acini (Figure 3) (Laden et al. 1984 ; Ito et al. 1989 ; Liu et al. 1998 ). The H Type 4 chain isolated from the human O erythrocytes (Kannagi et al. 1984 ) and from the human mammary carcinoma cell line MCF-7 (Bremer et al. 1984 ) was originally identified as the antigen defined by anti-H MBr1. Recently, Adobati et al. 1997 examined the specificity of MBr1 and demonstrated that the terminal tetrasaccharide of globo-H (Fuc1-2Galß1-3GalNAcß1-3Gal1-R) is the MBr1-defined epitope and that the terminal fucose is essential for MBr1 recognition. However, because anti-H MBr1 cannot discriminate H Type 3 from H Type 4, it is not known whether MBr1-reactive material in serous cells is H Type 3, H Type 4, or both. Because the A type 4 antigen was isolated from human kidney (Breimer and Jovall 1985 ; Holgersson et al. 1992 ), it would be of interest to examine the kidney immunohistochemically using anti-H MBr1.

It is known that the UEA-I-positive substances, which are regulated by the Se gene, are present in the serous cells of human submandibular gland (Ito et al. 1989 ; Liu et al. 1998 ). Here, we have demonstrated the presence of H Type 3/4 chains in the serous cells and the dependency of their expression on the Se gene. However, Mollicone et al. 1996 and Baldus et al. 1996 examined the specificity of UEA-I using synthetic oligosaccharides and demonstrated no reaction of UEA-I with H Type 3 and H Type 4 chains. Therefore, the characteristics of UEA-I-positive substance(s) in serous cells still remain unclear.

	Acknowledgments

Supported by grants-in-aid for Scientific Research from the Ministry of Education, Science, Culture and Sports of Japan.

We are grateful to Drs Ken Furukawa and Shin Yazawa (Department of Legal Medicine, Gunma University School of Medicine) and to Dr Maria I. Colnaghi (Division of Experimental Oncology E, National Institute for Cancer Research, Milan) for the kind gifts of MAb anti-H 1E3 and anti-H MBr1, respectively. We thank Mr Shigeo Kamimura and Ms Yasuko Noguchi for making serial thin sections.

Received for publication September 8, 1998; accepted January 12, 1999.

	Literature Cited

Top Summary Introduction Materials and Methods Results Discussion Literature Cited

Adobati E, Panza L, Russo G, Colnaghi MI, Canevari S (1997) In vitro mimicry of CaMBr1 tumor-associated antigen by synthetic oligosaccharides. Glycobiology 7:173-178[Abstract/Free Full Text]

Baldus SE, Thiele J, Park Y-O, Hanisch FG, Bara J, Fischer R (1996) Characterization of the binding specificity of Anguilla anguilla agglutinin (AAA) in comparison to Ulex europaeus agglutinin I (UEA-I). Glycoconjugate J 13:585-590[Medline]

Breimer ME, Jovall PA (1985) Structural characterization of a blood group A heptaglycosylceramide with globo-series structure. The major glycolipid based blood group A antigen of human kidney. FEBS Lett 179:165-172[Medline]

Bremer EG, Levery SB, Sonnino S, Ghidoni R, Canevari S, Kannagi R, Hakomori S (1984) Characterization of a glycosphingolipid antigen defined by the monoclonal antibody MBr1 expressed in normal and neoplastic epithelial cells of human mammary gland. J Biol Chem 259:14773-14777[Abstract/Free Full Text]

Clausen H, Hakomori S (1989) ABH and related histo-blood group antigens; immunochemical differences in carrier isotypes and their distribution. Vox Sang 56:1-20[Medline]

Clausen H, Holmes E, Hakomori S (1986a) Novel blood group H glycolipid antigens exclusively expressed in blood group A and AB erythrocytes (type 3 chain H). II. Differential conversion of different H substrates by A₁ and A₂ enzymes, and type 3 chain H expression in relation to secretor status. J Biol Chem 261:1388-1392[Abstract/Free Full Text]

Clausen H, Levery SB, Kannagi R, Hakomori S (1986b) Novel blood group H glycolipid antigens exclusively expressed in blood group A and AB erythrocytes (type 3 chain H). I. Isolation and chemical characterization. J Biol Chem 261:1380-1387[Abstract/Free Full Text]

Cossu M, Lantini MS (1996) Ultrastructural localization of blood group antigens in human salivary glands. Eur J Morphol 34:191-195[Medline]

Cossu M, Riva A, Lantini MS (1990) Subcellular localization of blood group substances ABH in human salivary glands. J Histochem Cytochem 38:1165-1172[Abstract]

Donald ASR (1981) A-active trisaccharide isolated from A₁ and A₂ blood-group-specific glycoproteins. Eur J Biochem 120:243-249[Medline]

Gonzalez AL, Joly E (1995) A simple procedure to increase efficiency of DEAE-dextran transfection of COS cells. Trends Genet 11:216-217[Medline]

Hanischi FG, Egge H, Peter–Katalinic J, Uhlenbruck G (1986) Structure of neutral oligosaccharides derived from mucus glycoproteins of human seminal plasma. Eur J Biochem 155:239-247[Medline]

Henry S, Mollicone R, Fernandez P, Samuelsson B, Oriol R, Larson G (1996) Molecular basis for erythrocyte Le(a+b+) and salivary ABH partial-secretor phenotypes: expression of a FUT2 secretor allele with an A-T mutation at nucleotide 385 correlates with reduced (1,2)fucosyltransferase activity. Glycoconjugate J 13:985-993[Medline]

Holgersson J, Bäcker AE, Breimer ME, Gustavsson ML, Jovall PA, Karlsson H, Pimlott W, Samuelsson BE (1992) The blood group B type-4 heptaglycosylceramide is a minor blood group B structure in human B kidneys in contrast to the corresponding A type-4 compound in A kidneys. Structural and in vitro biosynthetic studies. Biochim Biophys Acta 1180:33-43[Medline]

Ito N, Nishi K, Nakajima M, Okamura Y, Hirota T (1989) Histochemical analysis of the chemical structure of blood group-related carbohydrate chains in serous cells of human submandibular glands using lectin staining and glycosidase digestion. J Histochem Cytochem 37:1115-1124[Abstract]

Kannagi R, Levery SB, Hakomori S (1984) Blood group H antigen with globo-series structure. Isolation and characterization from human blood group O erythrocytes. FEBS Lett 175:397-401[Medline]

Koda Y, Kimura H, Mekada E (1993) Analysis of Lewis fucosyltransferase genes from the human gastric mucosa of Lewis-positive and -negative individuals. Blood 82:2915-2919[Abstract/Free Full Text]

Koda Y, Soejima M, Johnson PH, Smart E, Kimura H (1997) Missense mutation of FUT1 and deletion of FUT2 are responsible for Indian Bombay phenotype of ABO blood group system. Biochem Biophys Res Commun 238:21-25[Medline]

Koda Y, Soejima M, Liu Y-H, Kimura H (1996) Molecular basis for secretor type (1,2)-fucosyltransferase gene deficiency in a Japanese population: a fusion gene generated by unequal crossover responsible for the enzyme deficiency. Am J Hum Genet 59:343-350[Medline]

Laden SA, Schulte BA, Spicer SS (1984) Histochemical evaluation of secretory glycoproteins in human salivary glands with lectin–horseradish peroxidase conjugates. J Histochem Cytochem 32:965-972[Abstract]

Liu Y-H, Akiyama K, Jia J-T, Kimura H (1996) Characterization of a monoclonal antibody specific for H type 2 structure of ABO blood group, and its use for measuring H type 2 on human red blood cells. J Clin Lab Anal 10:144-148[Medline]

Liu Y-H, Fujitani N, Koda Y, Kimura H (1998) Distribution of H type 1 and of H type 2 antigens of ABO blood group in different cells of human submandibular gland. J Histochem Cytochem 46:69-76[Abstract/Free Full Text]

Macartney JC (1986) Lectin histochemistry of galactose and N-acetyl-galactosamine glycoconjugates in normal gastric mucosa and gastric cancer and the relationship with ABO and secretor status. J Pathol 150:135-144[Medline]

Mariani–Costantini R, Barbanti P, Colnaghi MI, Menard S, Clemente C, Rilke F (1984a) Reactivity of a monoclonal antibody with tissues and tumors from human breast. Immunohistochemical localization of a new antigen and clinico-pathologic correlations. Am J Pathol 115:47-56[Abstract]

Mariani–Costantini R, Colnaghi MI, Leoni F, Menard S, Cerasoli S, Rilke F (1984b) Immunohistochemical reactivity of a monoclonal antibody prepared against human breast carcinoma. Virchows Arch [Pathol Anat] 402:389-404

Martignone S, Menard S, Bedini A, Paccagnella A, Fasolato S, Veggian R, Colnaghi MI (1993) Study of the expression and function of the tumor-associated antigen CaMBr1 in small cell lung carcinomas. Eur J Cancer 29A:2020-2025

Menard S, Tagliabue E, Canevari S, Fossati G, Colnaghi MI (1983) Generation of monoclonal antibodies reacting with normal and cancer cells of human breast. Cancer Res 43:1295-1300[Abstract/Free Full Text]

Mollicone R, Cailleau A, Imberty A, Gane P, Perez S, Oriol R (1996) Recognition of the blood group H type 2 trisaccharide epitope by 28 monoclonal antibodies and three lectins. Glycoconjugate J 13:263-271[Medline]

Nakajima T, Yazawa S, Miyazaki S, Furukawa K (1993) Immunochemical characterization of anti-H monoclonal antibodies obtained from a mouse immunized with human saliva. J Immunol Methods 159:261-267[Medline]

Nakayama J, Ota M, Honda T, Katsuyama T (1987) Histochemical demonstration of sugar residues by lectin and immunocytochemical techniques for blood group antigens in human colon. Histochem J 19:454-464[Medline]

Okada Y, Sotozono MA, Sakai N, Yonei T, Nakanishi S, Tsuji T (1994) Fucosylated Thomsen–Friedenreich antigen in -anomeric configuration in human gastric surface epithelia: an allogeneic carbohydrate antigen possibly controlled by the Se gene. J Histochem Cytochem 42:371-376[Abstract]

Oriol R, Le Pendu J, Mollicone R (1986) Genetics of ABO, H, Lewis, X and related antigens. Vox Sang 51:161-171[Medline]

Perrone F, Menard S, Canevari S, Calabrese M, Boracchi P, Bufalino R, Testori S, Baldini M, Colnaghi MI (1993) Prognostic significance of the CaMBr1 antigen on breast carcinoma: relevance of the type of recognised glycoconjugate. Eur J Cancer 29A:2113-2117

Wang B-J, Akiyama K, Jia J-T, Kimura H (1994) Measuring H type 1 and H type 2 antigens in human saliva by immunoassay using artificial antigens as standard substances. Forensic Sci Int 67:1-8[Medline]

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