Polysialosyl glycoconjugates defined by monoclonal antibody M6704 are expressed in human gliomas and embryonic neurons.

Nakayama, Jun; Katsuyama, Tsutomu; Sugiyama, Eiji; Hirabayashi, Yoshio

doi:10.1177/41.10.8245415

Cited by 8 publications

(6 citation statements)

References 25 publications

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“…Some speculation on the biological functions of oligo-Neu5Gc can be allowed if one considers that oligo-Sia is now the common structural unit in both glycoproteins and gangliosides in mammals. Higher gangliosides such as G D3 , G T3 , G D1c , and G Q1b are considered to be involved in cell adhesion (52), differentiation (47, 53, 54), signal transduction (55), ADP-ribosylation (56), and specific oncodevelopmental markers (57,58), where the sialic acid species of these gangliosides is, however, largely of the Neu5Ac type at present. Interestingly, (Neu5Gc)G D1c has recently been identified as a marker for rat CD4 ϩ T lymphocytes that produce interleukin-2 (47), where some di-Neu5Gc-specific functions were suggested, including regulation of differentiation of this type of T cells.…”

Section: Oligo-neu5gc Unit In Mammalian Glycoproteinsmentioning

confidence: 99%

Identification of Oligo-N-glycolylneuraminic Acid Residues in Mammal-derived Glycoproteins by a Newly Developed Immunochemical Reagent and Biochemical Methods

Sato¹,

Kitajima²,

Inoue³

et al. 1998

Journal of Biological Chemistry

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The occurrence of the ␣238-linked oligomeric form of N-glycolylneuraminic acid (oligo-Neu5Gc) residues in mammalian glycoproteins was unequivocally demonstrated using a newly developed anti-oligo/poly-Neu5Gc monoclonal antibody as well as by chemical and biochemical methods. First, the antibody, designated mAb.2-4B, which specifically recognized oligo/polyNeu5Gc with a degree of polymerization of >2, was developed by establishing a hybridoma cell line from P3U1 myeloma cells fused with splenocytes from an MRL autoimmune mouse immunized with dipalmitoylphosphatidylethanolamine-conjugated oligo/poly-Neu5Gc. Second, oligo-Neu5Gc was shown to occur in glycoproteins derived from pig spleen by Western blot analysis using mAb.2-4B, which was also confirmed by fluorometric high performance liquid chromatographic analysis of the product of periodate oxidation/reduction/ acid hydrolysis of the purified glycopeptide fractions and by TLC and 600-MHz 1 H NMR spectroscopic analysis of their mild acid hydrolysates. Finally, the ubiquitous occurrence of oligo-Neu5Gc chains as glycoproteinaceous components in Wistar rat tissue was immunochemically indicated. This is the first example demonstrating the diversity in oligo/poly-Sia structure in mammalian glycoproteins, where only poly-N-acetylneuraminic acid is known to occur. Such diversity in oligo/poly-Sia structure also implicates a diverged array of biological functions of this glycan unit in glycoproteins.Oligo/polysialic acid structure represents a group of glycan chains consisting of N-acetylneuraminic acid (Neu5Ac), 1 Nglycolylneuraminic acid (Neu5Gc), and deaminoneuraminic acid (KDN) (1, 2). ␣238-Linked oligo/poly-Neu5Gc structure was first found in polysialoglycoprotein (PSGP) isolated from the unfertilized eggs of rainbow trout (Oncorhynchus mykiss) (3). Following this discovery, ␣238-linked poly-Neu5Ac structure was shown to occur in various animal glycoproteins from insect to human by using immunochemical and enzymatic probes specific to ␣238-linked oligo/poly-Neu5Ac glycotopes (4 -11). Recently, we demonstrated that oligo/poly-Sia chains on PSGP isolated from Salvelinus fish eggs exhibit a remarkable degree of diversity in their building blocks arising from the different substitution at C-5, i.e. Neu5Ac, Neu5Gc, and KDN, and in the presence of either O-acetyl or O-lactyl substitution (2). These structural diversities in oligo/poly-Sia may be potentially relevant to the functional diversity that may be required for multiple cellular recognition processes on the cell surface in biological events, such as fertilization and early embryogenesis (2, 12).Rather extensive debates have long been going on regarding the biological significance of the structural diversity in Sia residues that are expressed in species-specific, tissue-specific, developmental stage-specific, and tumor-specific manners (1, 13-17). We were motivated to confirm the diversity in oligo/ poly-Sia structure not only in teleost fishes, but also in mammals because the components of Sia in most animal tissu...

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Section: Oligo-neu5gc Unit In Mammalian Glycoproteinsmentioning

confidence: 99%

Identification of Oligo-N-glycolylneuraminic Acid Residues in Mammal-derived Glycoproteins by a Newly Developed Immunochemical Reagent and Biochemical Methods

Sato¹,

Kitajima²,

Inoue³

et al. 1998

Journal of Biological Chemistry

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“…Immunohistochemistry for Polysialic Acid-The Hybrid-Ready tissue slides were subjected to the immunohistochemical staining for detection of polysialic acid as described previously (12,23). A monoclonal antibody 12F8 specific for polysialic acid (24) (Pharmingen) was used in this study, and immunochemical detection was performed by indirect method using anti-rat immunoglobulins conjugated with horseradish peroxidase (Dako) (25), followed by counterstaining with hematoxylin.…”

Section: Northern Blot Analysis Of Various Human Tissues-northern Blomentioning

confidence: 99%

Human STX Polysialyltransferase Forms the Embryonic Form of the Neural Cell Adhesion Molecule

Angata

Nakayama

Fredette

et al. 1997

Journal of Biological Chemistry

126

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PST and STX are polysialyltransferases that form polysialic acid in the neural cell adhesion molecule (N-CAM), although it is not known why these two polysialyltransferases exist. In the present study, we have first isolated cDNA encoding human STX, which includes 5-untranslated sequence. Northern blot analysis, using this cDNA and PST cDNA previously isolated by us, demonstrated that PST and STX are expressed in different fetal and adult tissues. STX is primarily expressed in embryonic tissues, but only modestly in adult heart, brain, and thymus. PST, on the other hand, is continuously expressed in adult heart, brain, thymus, spleen, small and large intestines, and peripheral blood leukocytes. In various parts of adult brain, the relative amount of PST and STX appears to be substantially different depending on the regions. The analysis by in situ hybridization of mouse adult brain, however, suggests that polysialic acid in the hippocampal formation is synthesized by both STX and PST. HeLa cells doubly transfected with the isolated STX cDNA and N-CAM cDNA supported neurite outgrowth much better than HeLa cells expressing N-CAM alone. However, polysialic acid synthesized by PST appears to be a better substratum than that synthesized by STX. Moreover, the genes for PST and STX were found to reside at chromosome 5, band p21 and chromosome 15, band q26, respectively. These results, taken together, strongly suggest that PST and STX are expressed distinctly in tissue-specific and cell-specific manners and that they apparently have distinct roles in development and organogenesis.Polysialic acid is a developmentally regulated glycan composed of a linear homopolymer of ␣-2,8-linked sialic acid residues. Polysialic acid is mainly attached to the neural cell adhesion molecule (N-CAM) 1 and is more abundant in embryonic brain than adult brain (1-3). Presence of this large negatively charged carbohydrate modulates the adhesive property of N-CAM, and removal of polysialic acid increases binding between N-CAMs (4, 5). During embryonic development, the polysialylated embryonic from of N-CAM is restricted to migrating cells (6, 7), and the removal of polysialic acid from the N-CAM during embryonic development affects motor-axon projection patterns (8). Polysialylated N-CAM was also shown to attenuate cell-cell interactions mediated by other cell adhesion molecules (9 -11).Recently, we and others have cloned cDNAs encoding human, hamster, and mouse polysialyltransferases (PST for human, PST-1 for hamster, and ST8Sia IV for mouse, respectively) (12-14). The amino acid sequences of PST and PST-1 are more than 97% identical. Both PST and PST-1 directed the expression of polysialic acid on the cell surface. The same studies also revealed that PST is highly homologous to STX (sialyltransferase X, or ST8Sia II) (12, 13), and STX and PST have 59% identity at the amino acid level. STX was originally cloned as a developmentally regulated sialyltransferase from the rat fetal brain (15). Although the substrate specificity of STX was not kno...

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“…11). M6703 antibody was shown to react with oligosialic acid with 2-3 residues of ␣-2,8-linked sialic acid (15), while 12E3 and 735 were shown to react with polysialic acid with 6 or more (for 12E3) residues of ␣-2,8-linked sialic acid and 8 or more (for 735) residues of ␣-2,8-linked sialic acid (18,19), respectively. The results shown in Fig.…”

Section: Pst Does Not Necessarily Require N-cam For the Expression Ofmentioning

confidence: 99%

“…This chimeric protein, released into the culture medium from COS- (15). The antibodies 12E3 and 735 were shown to react with polysialic acid containing six or more ␣-2,8-linked sialic acid residues (for 12E3) (18) or eight or more ␣-2,8-linked sialic acid residues (for 735) (19).…”

mentioning

confidence: 99%

A Human Polysialyltransferase Directs in Vitro Synthesis of Polysialic Acid

Nakayama

Fukuda

1996

Journal of Biological Chemistry

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Polysialosyl glycoconjugates defined by monoclonal antibody M6704 are expressed in human gliomas and embryonic neurons.

Cited by 8 publications

References 25 publications

Identification of Oligo-N-glycolylneuraminic Acid Residues in Mammal-derived Glycoproteins by a Newly Developed Immunochemical Reagent and Biochemical Methods

Identification of Oligo-N-glycolylneuraminic Acid Residues in Mammal-derived Glycoproteins by a Newly Developed Immunochemical Reagent and Biochemical Methods

Human STX Polysialyltransferase Forms the Embryonic Form of the Neural Cell Adhesion Molecule

A Human Polysialyltransferase Directs in Vitro Synthesis of Polysialic Acid

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