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CRITICAL REVIEWS IN ORAL BIOLOGY & MEDICINE |
Department of Oral Diagnostics, School of Dentistry, University of Copenhagen, Nørre Alle 20, DK-2200 Copenhagen N, Denmark;
* corresponding author, ed{at}odont.ku.dk
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ABSTRACT |
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 TOP ABSTRACT INTRODUCTIONABO BLOOD-GROUP ANTIGENSFUTURE RESEARCHREFERENCES |
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KEY WORDS: oral cancer • ABO blood-group antigens • carbohydrate antigens • oral precancer
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INTRODUCTION |
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TOPABSTRACTINTRODUCTIONABO BLOOD-GROUP ANTIGENSFUTURE RESEARCHREFERENCES |
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Cell-surface carbohydrates are built up in a stepwise fashion when monosaccharides are tranferred from their sugar nucleotide derivatives to appropriate acceptors. Each particular type of transfer is catalyzed by a unique specific glycosyltransferase. Thus, a missing or changed enzyme will block further synthesis of the carbohydrate structure, which will remain as a precursor structure. Additionally, the appearance of new enzymes that either compete for common substrate or lead to elongation of previously terminated structures will result in alteration in the carbohydrate that is finally expressed (Fukuda et al., 1999; Fukuda, 2002; Fuster et al., 2003).
In tumors, changes in glycosylation are found in both glycolipids and glycoproteins (Hakomori, 1999; Le Pendu et al., 2001). Most studies have dealt with alteration of carbohydrates at the cell surface. However, several recent studies have shown that altered glycosylation plays a major role in most aspects of the malignant phenotype, including signal transduction and apoptosis. These studies have recently been reviewed (Hakomori, 2002; Hakomori and Handa, 2002).
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ABO BLOOD-GROUP ANTIGENS |
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TOPABSTRACTINTRODUCTIONABO BLOOD-GROUP ANTIGENSFUTURE RESEARCHREFERENCES |
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Two carbohydrate antigens, A and B antigens, and their antibodies constitute the ABO system (Watkins, 1966). In recent years, the molecular basis for the ABO system has been described in detail (Yamamoto et al., 1990; Clausen et al., 1994; Yamamoto, 2000). The A and B functional alleles of the ABO genetic locus encode the A transferase (glycosyltransferase 
1,3-GalNAc-transferase) and the B transferase (1,3Gal-transferase), respectively. The A transferase transfers a GalNAc residue from UDP-GalNAc to the precursor H substrate, producing A antigens as defined by the trisaccharide determinant structure GlNAc-1,3 (Fuc1-2)GalNAcß1-R (Fig. 1
). Similarly, the B transferase catalyzes the transfer of Gal from UDPGal to the H substrate, producing B antigens (Fig. 1). The phenotypic differences between A and B are thus due to the subtle differences in substrate specificity of the A and B glycosyltransferases. Phenotype O is characterized by the absence of A and B transferase and, most likely, by the presence of an inert protein encoded by the O allele, leaving the H structure unchanged. The synthesis of the H structure is controlled by 2 fusosyltransferases coded for by 2 distinct genes, Fut1 and Fut2 (Koda et al., 1997a,b; Oriol et al., 2000). Fut1 controls the expression of H on erythrocytes, endothelium, and epithelial cell membranes, whereas Fut2 is responsible for H in saliva and other secretions, but also on some epithelial cell membranes (Oriol et al., 2000). Secretors are defined as individuals that secrete blood-group antigen H or A/B in saliva. The Fut2 gene is absent in 20% of the Western population, resulting in the absence of ABH antigens in saliva. Secretors were classically designated as SeSe or Sese, and non-secretors as sese (Hartmann, 1941; Watkins, 1966; Rouquier et al., 1995; Oriol et al., 2000).
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) (Yamamoto et al., 1990). Genetic analyses by such restriction enzymes have been used to detect cancer-associated genetic changes in carcinoma cells (Yamamoto et al., 1990; Orlow et al., 1998).
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Cancer and Precancer
Reduction or complete loss of antigen expression has been reported in carcinomas of the oral cavity, lung, stomach, colon, larynx, ovary, prostate, bladder, and breast (Le Pendu et al., 2001). Loss of blood-group antigen expression may also be seen in potentially malignant lesions of the gastric mucosa, prostate, cervical mucosa, epithelial hyperplasia of the breast, and oral mucosa (Le Pendu et al., 2001). Loss of A and B antigens is often correlated with an increased H antigen expression in endometria, prostate, breast, and oral carcinomas, whereas it is accompanied by an increase in Ley expression in lung and ovary carcinomas. The presence of H and Ley in the tumors indicates that loss of A or B antigens is the result of a blocked synthesis (Fig. 2
) (Dabelsteen et al., 1983; Bryne et al., 1991; Le Pendu et al., 2001).
Immunohistochemical studies of oral squamous cell carcinomas have shown loss of expression of A or B antigens in more than 80% of cases, all of which showed concomitant loss of A/B transferase (Figs. 3A, 3B, 3C) (Gao et al., 2004a,b). Studies of potentially malignant lesions have shown loss of A/B antigen in most lesions with epithelial dysplasia and in half of the lesions clinically classified as leukoplakias but without histological evidence of epithelial dysplasia (Dabelsteen et al., 1975; Gao et al., 2004a). As mentioned above, in the normal oral cavity, keratinized epithelium in the palate or gingiva shows little or no expression of A or B blood-group antigen (Dabelsteen et al., 1991). Since a change from a non-keratinized to a keratinized differentiation pattern is a characteristic of many oral carcinomas and potentially malignant lesions, the lack of expression of blood-group antigens in such lesions could be due to a change in differentiation pattern of the epithelium (Dabelsteen et al., 1975). However, it has been demonstrated that half of the leukoplakias that developed in buccal mucosa show expression of A antigen, even though they histologically appear as keratinized lesions (Gao et al., 2004a). Similar A expression was found in mechanically induced hyperkeratinized lesions of buccal mucosa (Dabelsteen et al., 1975). These findings indicate that loss of antigen is not invariably associated with hyperkeratinization.
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Specific allelic loss occurs in oral carcinomas of blood-group AO- and BO-patients. By laser capture microscopy and restriction enzyme analysis, it was possible to genotype tumor tissue and to detect specific allelic loss in oral carcinomas (Figs. 3E, 3F, 3G). From an investigation of formalin-fixed and paraffin-embedded materials, it appeared that 1/3 of the carcinomas showed specific loss of A and B alleles; whereas in another study, based on frozen sections only, 1/6 of the cases had specific allelic loss, indicating that tissue processing may influence the results (Gao et al., 2004a,b). Since 80% of the cases showed loss of blood-group antigen expression by immunohistochemical staining, mechanisms other than specific loss of alleles play a role in the AB glycosyltransferase expression in oral carcinomas (Gao et al., 2004b).
Studies of bladder cancer indicate that loss of A/B expression involves the deletion of a large chromosomal region including the ABO locus at 9q34 1-2, which may contain one or more tumor suppressor genes (Orlow et al., 1994, 1998). The investigation of oral carcinomas for alteration in this region by microsatellite analysis found LOH or microsatellite instability in this region in 1/3 of the patients. These changes correlated well with the lack of expression of A and B antigens in the tissue.
A CpG island, a stretch of GC-rich DNA sequence, is frequently located at the 5' end of regulatory regions of a gene, extending from the promoter to the first exon region (Bird, 1986). This area of genomic sequence is subject to epigenetic modifications, including DNA methylation and histone acetylation and methylation, which are known to play an important role in regulating gene expression (Bird, 2002). In cancer cells, it has been shown that an increase in regional DNA methylation occurs in many promoter CpG islands, resulting in a closed chromatin configuration that disables transcription initiation of the associated genes (Baylin and Herman, 2000; Esteller et al., 2001). Studies of the regulatory mechanism of the ABO gene transcripts have demonstrated the presence of two promoter regions (Kominato et al., 1999). Expression of the A/B gene in epithelial cell lines has been shown to be dependent on the methylation status of the proximal constitutive promoter encoding most of the A/B transcripts, since an inverse relationship was found between promoter hypermethylation and A/B gene expression (Iwamoto et al., 1999; Kominato et al., 1999). These studies were supported by experiments in which cells were treated with the demethylating agent 5-aza-2'-deoxycytidine, a treatment that can result in demethylation of the ABO promoter region and restore transcriptional activity. The activity of the distal promoter is less well-understood, but appears to be dependent on cell types (Kominato et al., 2002).
Hypermethylation of the distal promoter appeared not to be of significance for expression of blood-group antigens in either normal or oral carcinoma tissue. However, hypermethylation of the A/B gene constitutive proximal promoter region was demonstrated in 1/3 of the cases of oral carcinomas (Fig. 4) (Gao et al., 2004b). The study also showed that hypermethylation was frequent in hyperplastic or dysplastic epithelium adjacent to tumors. A hypermethylation of the A/B promoter corresponds to the lack of expression of blood-group antigens seen by immunohistochemical staining. Studies have also been undertaken to determine if A/B expression in normal epithelium is controlled by hypermethylation of the promoter. In both epidermis and keratinized epithelium from gingiva, it was found that, although these tissues expressed little or no blood-group antigen, the A/B promoter was not hypermethylated, suggesting that the hypermethylation is a specific tumor-related event (Gao et al., 2004b).
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). These findings suggest that ABO hypermethylation is a tumor-specific event leading to loss of AB expression. Knudson’s two-hit model predicts that a phenotypic consequence of tumor suppressor gene loss is not seen unless both alleles of a gene are inactivated in a tumor (Knudson, 2001). The fact that A/B allelic loss or LOH in the ABO region and hypermethylation of the ABO gene promoter are frequently found in the same patients also suggests that the inactivation of the A/B gene is of significance for oral cancer development. It is impossible, however, to explain all losses of A/B antigens in oral carcinomas by allelic loss or hypermethylation of the ABO promoter, which suggests that other regulatory factors outside the ABO promoter are functional in transcriptional regulation of the ABO gene (Kominato et al., 1999; Gao et al., 2004b).
Function of the ABO Antigen
Blood-group antigens can be present on key receptors controlling cell proliferation, adhesion, and motility, such as epidermal growth factor receptor, integrins, cadherins, and CD-44 (Greenwell, 1997; Hakomori, 1999; Prokopishyn et al., 1999). The expression patterns of these various receptors differ according to the type of normal epithelium and the type of cancer, and therefore the role of ABH antigens in the biology of human cancers may also vary. The function of the ABO expression in normal stratified oral epithelium is unclear. Half of the population is blood group O, and 20% of the A/B individuals do not express A/B due to their non-secretor status. In the O phenotype, the A/B precursor is transformed into the difucosylated structures Leb and Ley, whereas in the non-secretors, the monofucosylated structures Lea and Lex are found (Mandel et al., 1991). It is known that specific strains of pathogens bind to carbohydrates of the histo-blood-group family, and that individuals devoid of carbohydrates are less likely to be infected (Stapleton et al., 1992). Although there are reports suggesting that non-secretors have a higher incidence of Candida albicans infections, which can be explained by differences in binding of the Candida to the oral mucosa, there appears to be no difference in the function of the normal stratified oral epithelium in any of the different blood-group phenotypes (Johansson et al., 2000).
A higher incidence of various types of carcinomas has been reported in blood-group A/B individuals, but the reason for this propensity is not clear. It is possible that blood-group A-positive and A-negative individuals may have different binding properties of as-yet-unknown micro-organisms, which may then influence their susceptibility to carcinoma development. For example, extensive studies of Helicobacter pylori, which is responsible for gastroduodenal ulcers and eventually gastric carcinoma, have shown that one of the binding mechanisms of the Helicobacter to the mucosal cells involves blood-group antigen precursor structures (Ilver et al., 1998). However, at present, there are no indications of such mechanisms in oral cancer development.
Experimental studies of rat colon carcinoma cells indicate that cells with A expression are resistant to apoptosis and are strongly tumorigenic in synergenic rats (Marionneau et al., 2002). Similar findings were found when cells expressed the A precursor H antigen, whereas cells expressing structures of shorter carbohydrates were less tumorigenic. The significance of these studies in relationship to human tumor development is difficult to interpret. Studies in the rat and the mouse have shown that, in stratified epithelium, the expression of blood-group antigen is opposite that seen in humans, since basal cells express the full blood-group antigen A or B, whereas spinous cells express the precursor structure H. Therefore, the rat model cannot be compared with human carcinogenesis (Reibel et al., 1984; Mackenzie et al., 1995; Marionneau et al., 2002).
Studies with human colon carcinoma cell lines have shown that loss of expression of AB glycosyltransferase can enhance malignancy of the cell lines (Ichikawa et al., 1997). cDNA encoding A transferases was transfected into a human colorectal carcinoma cell line expressing the A precursor structures H/Ley. The investigators thus established cell lines that express A antigens and showed that conversion of H to A inhibited Matrigel-dependent motility, a standard measure of tumor cell motility and invasiveness (Ichikawa et al., 1997). The investigators further provided evidence that the A expression seems to be associated with 6, 3, and ß1 integrins and suggested that glycosylation of the integrins may affect the degree of 6 or ß3 interaction with ß1 subunit, which is known to be involved in the Matrigel motility of colon tumor cells (Ichikawa et al., 1997). The correlation between glycosylation and cell migration is evidenced by the finding that the motility of a melanoma cell expressing H precursor structures could be inhibited by anti-H antibodies (Miyake and Hakomori, 1991). Taken together, these studies suggest that blocking of H, either by antibodies or by elongation of the carbohydrate chains, has a strong influence on cell motility. Since transfection per se causes artificial overexpression of A antigens, a later study attempted to determine if there was any difference in cell motility among tumor cells from a cell line in which there were both blood-group antigen A-negative and blood-group A-positive cells (Ichikawa et al., 1998). This study showed a marked enhancement of motility in the A-negative population as compared with the A-positive population. It was also shown that A glycosylation occurs on 3, 6, and ß1 integrin receptors, again suggesting that altered glycosylation of the integrins alters their function (Ichikawa et al., 1998). The fact that the blood-group antigen expression correlates with integrin receptors was further supported by studies showing that ABO antigens in human colon carcinoma cells were carried on 3, ß1 integrins (Prokopishyn et al., 1999). Other experiments have supported the finding that decreased expression of AB blood-group structures and increased expression of the precursor Ley are related to increased cell motility (Figs. 3D, 5). Migrating breast carcinoma cell lines have up-regulated expression of Ley that is found mainly on microspikes and ruffled membranes (Garrigues et al., 1994). These structures are involved in cell migration and are known to express clusters of integrins and associated proteins that mediate cell adhesion and cell signaling. The relationship between enhanced cell migration and loss of expression of AB antigens has been clearly demonstrated in in vivo studies of oral mucosal wound-healing in both humans and Rhesus monkeys (Dabelsteen and Fejerskov, 1974; Mackenzie et al., 1977). Migrating epithelial cells show loss of AB antigens and up-regulation of precursor H and Ley (Dabelsteen et al., 1998). One further aspect of the H/Ley expression in wounds and tumors is the recent finding that both Ley and H possess angiogenic activity (Halloran et al., 2000). This finding is of course of major interest, since angiogenesis is essential for both tumor development and wound-healing.
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Increased expression of sialyl-Lex, molecules closely related to the ABO precursor molecules, is correlated with a poor prognosis for certain types of carcinomas. The reason for the poor prognosis is that expression of sialosyl-Lex on tumor cells will facilitate metastasis through binding to selectin adhesion receptors expressed on activated platelets and endothelial cells. However, no increased expression of either Lex, sialyl-Lex, Lea, or sialyl-Lea has been found in oral carcinomas. Thus, these ABO-related molecules seem to play a minor role in the spread of oral carcinomas (Renkonen et al., 2000).
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FUTURE RESEARCH |
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TOPABSTRACTINTRODUCTIONABO BLOOD-GROUP ANTIGENSFUTURE RESEARCHREFERENCES |
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Received January 27, 2004; Accepted July 7, 2004
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| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| IADR Journals | Advances in Dental Research ® |
| Journal of Dental Research ® | Critical Reviews (1990-2004) |
