Sensitive Enzyme-Immunostaining and Densitometric Determination on Thin-Layer Chromatography of N-Glycolylneuraminic Acid-Containing Glycosphingolipids, Hanganutziu-Deicher Antigens1

Higashi, Hideyoshi; Fukui, Yuichi; Ueda, Shigeharu; Kato, Shiro; Hirabayashi, Yoshio; Matsumoto, M; Naiki, Masaharu

doi:10.1093/oxfordjournals.jbchem.a134760

Cited by 126 publications

(57 citation statements)

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“…Existing data about Neu5Gc in human cells is controversial (16,18,19,21,22). Even in studies claiming its presence in malignant tissues, the cell type specificity of the presumed Neu5Gc was not defined.…”

Section: Discussionmentioning

confidence: 99%

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Human uptake and incorporation of an immunogenic nonhuman dietary sialic acid

Tangvoranuntakul

Gagneux

Díaz

et al. 2003

Proc. Natl. Acad. Sci. U.S.A.

551

586

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Humans are genetically unable to produce the sialic acid N-glycolylneuraminic acid (Neu5Gc), because of a mutation that occurred after our last common ancestor with great apes. Although Neu5Gc is presumed absent from normal humans, small amounts have been claimed to exist in human tumors and fetal meconium. We have generated an antibody with high specificity and avidity for Neu5Gc. Fetal tissues, normal adult tissues, and breast carcinomas from humans showed reactivity to this antibody, primarily within secretory epithelia and blood vessels. The presence of small amounts of Neu5Gc was confirmed by MS. Absent any known alternate pathway for its synthesis, we reasoned that these small amounts of Neu5Gc might originate from exogenous sources. Indeed, human cells fed with Neu5Gc incorporated it into endogenous glycoproteins. When normal human volunteers ingested Neu5Gc, a portion was absorbed and eliminated in urine, and small quantities were incorporated into newly synthesized glycoproteins. Neu5Gc has never been reported in plants or microbes to our knowledge. We found that Neu5Gc is rare in poultry and fish, common in milk products, and enriched in red meats. Furthermore, normal humans have variable amounts of circulating IgA, IgM, and IgG antibodies against Neu5Gc, with the highest levels comparable to those of the previously known anti-␣-galactose xenoreactive antibodies. This finding represents an instance wherein humans absorb and metabolically incorporate a nonhuman dietary component enriched in foods of mammalian origin, even while generating xenoreactive, and potentially autoreactive, antibodies against the same molecule. Potential implications for human diseases are briefly discussed.

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Section: Discussionmentioning

confidence: 99%

“…Despite no known alternate pathway for Neu5Gc synthesis in humans, antibodies have been used to claim its presence in some human cancers (15)(16)(17)(18)(19)(20) and human fetal meconium (15). However, the specificity of the polyclonal antibodies used was not well defined.…”

mentioning

confidence: 99%

Human uptake and incorporation of an immunogenic nonhuman dietary sialic acid

Tangvoranuntakul

Gagneux

Díaz

et al. 2003

Proc. Natl. Acad. Sci. U.S.A.

551

586

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“…Glycolipids were isolated from DIM fractions of HL60 cells (22). Specificity of PhGlc was confirmed by using TLC or two-dimensional TLC immunostaining with biotinylated rGL-7 and 3,3Ј-diaminobenzidine tetrahydrochloride (ICN) as the chromagen (16,23).…”

Section: Production Of Recombinant Gl-2 Fab Fragment Rgl-7mentioning

confidence: 99%

Carbohydrate-dependent signaling from the phosphatidylglucoside-based microdomain induces granulocytic differentiation of HL60 cells

Nagatsuka

Miki

Kasama

et al. 2003

Proc. Natl. Acad. Sci. U.S.A.

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“…6,8,9 4-O-Acetyl-GM3 has also been detected in human colon carcinomas. 10 Loss of O-acetylation of sLe x in human colon cancer facilitates metastasis. 2a Modifications on sialic acids usually lead to the reduction or even resistance of sialidases or trans-sialidases.…”

Section: Sialic Acidsmentioning

confidence: 99%

Carbohydrate post-glycosylational modifications

Chen

2007

Org. Biomol. Chem.

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Carbohydrate modification is a common phenomenon in nature. Many carbohydrate modifications such as some epimerization, O-acetylation, O-sulfation, O-methylation, N-deacetylation, and Nsulfation, take place after the formation of oligosaccharide or polysaccharide backbones. These modifications can be categorized as carbohydrate post-glycosylational modifications (PGMs). Carbohydrate PGMs further extend the complexity of the structures and the synthesis of carbohydrates and glycoconjugates. They also increase the capacity of the biological information that can be controlled by finely tuning the structures of carbohydrates. Developing efficient methods to obtain structurally defined naturally occurring oligosaccharides, polysaccharides, and glycoconjugates with carbohydrate PGMs is essential for understanding the biological significance of carbohydrate PGMs. Combine with high-throughput screening methods, synthetic carbohydrates with PGMs are invaluable probes in structure-activity relationship studies. We illustrate here several classes of carbohydrates with PGMs and their applications. Recent progress in chemical, enzymatic, and chemoenzymatic syntheses of these carbohydrates and their derivatives are also presented.

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Sensitive Enzyme-Immunostaining and Densitometric Determination on Thin-Layer Chromatography of N-Glycolylneuraminic Acid-Containing Glycosphingolipids, Hanganutziu-Deicher Antigens1

Cited by 126 publications

References 0 publications

Human uptake and incorporation of an immunogenic nonhuman dietary sialic acid

Human uptake and incorporation of an immunogenic nonhuman dietary sialic acid

Carbohydrate-dependent signaling from the phosphatidylglucoside-based microdomain induces granulocytic differentiation of HL60 cells

Carbohydrate post-glycosylational modifications

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