Brain Gangliosides and Thermal Adaptation in Vertebrates

Rahmann, H.; Hilbig, Reinhard; Probst, Wolfgang; Mühleisen, Martin

doi:10.1007/978-1-4684-1200-0_33

Cited by 16 publications

(9 citation statements)

References 8 publications

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“…Specific functions associated with the presence of glycosidically-bound 0-acetylsialates in biological systems include a diminished rate of cleavage from sialocarbohydrate chains by neuraminidase [37], an involvement in environmental adaption [38] and the binding of influenza C viruses [39], and an ability to influence alternate pathway complement activation [40] and bacterial antigenicity [41]. Hence, such differences in the physiochemical properties of the glycoprotein carbohydrate sidechains between rat and human blood plasmas are likely to have important biochemical, physiological and pathological ramifications.…”

Section: Discussionmentioning

confidence: 99%

High resolution proton NMR investigations of rat blood plasma Assignment of resonances for the molecularly mobile carbohydrate side‐chains of ‘acute‐phase’ glycoproteins

et al. 1993

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An intense broad resonance at 2.14 ppm present in high field (400, 500 and 600 MHz) Hahn spin-echo 'H-NMR spectra of rat blood plasma, but absent from those of human blood plasma is attributable to the presence of terminal 0-acetylsialate sugars in the molecularly mobile carbohydrate side-chains of 'acute-phase' glycoproteins (predominantly a,-acid glycoprotein). The presence of such alternative acetylsugars in the carbohydrate side-chains of rat plasma glycoproteins are of much physiological and experimental significance in view of the regular use of these animals in model systems of human inflammatory conditions.

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Section: Discussionmentioning

confidence: 99%

High resolution proton NMR investigations of rat blood plasma Assignment of resonances for the molecularly mobile carbohydrate side‐chains of ‘acute‐phase’ glycoproteins

et al. 1993

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“…With regard to the biological role of 0-acetyl groups in sialic acids, information is accumulating about specific functions of these sialic acids. Typical examples are the decrease of the rate of the sialidase-initiated degradation of sialocarbohydrate chains [3], the involvement in the tumor antigenic properties of human melanoma cells [4], the role in environmental adaptation [5] and binding of influenza C viruses [6, 71. Prior to chemical characterization of the sialic acids, they are in most cases released by acid or enzymic hydrolysis followed by various isolation methods [8,91. Among the 0-acetylated species, obtained in this way, Neu5,9Ac2 is the most common neuraminic acid derivative [l, 21.…”

mentioning

confidence: 99%

Migration of O‐acetyl groups in N,O‐acetylneuraminic acids

Kamerling

Schauer

Shukla

et al. 1987

European Journal of Biochemistry

148

128

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Highly purified N-acetyl-4-0-acetylneuraminic acid (Neu4,5Ac2), N-acetyl-7-0-acetylneuraminic acid (Neu5,7Ac2) and N-acetyl-7,9-di-O-acetylneuraminic acid (Neu5,7,9Ac3) were used to study spontaneous migrations of acetyl groups between hydroxyl groups. The techniques applied involved thin-layer chromatography, gas-liquid chromatography/mass spectrometry, high-performance liquid chromatography and 360-MHz H-NMR spectroscopy. It was found that at pH values at which no significant de-0-acetylation is observed: (a) Neu5,7Ac2 can easily be transformed into Neu5,9Ac2, (b) Neu5,7,9Ac3 yields an equilibrium of Neu5,7,9Ac3 and Neu5,8,9Ac3 in a molar ratio of approximately 1 : 1, and (c) Neu4,5Ac2 does not give rise to 0-acetykmigrations. The importance of these findings is discussed in terms of the biosynthesis of 0-acetylated sialic acids.Sialic acids are known to form part of many complex carbohydrates. They can bear 0-acetyl groups at different positions [l]. Especially, bovine submandibular gland glycoprotein has been shown to be a rich source of many members of the sialic acid family, i. e. mono-, di-, and tri-0-acetylated N-acetyl-and N-glycolylneuraminic acids [2]. With regard to the biological role of 0-acetyl groups in sialic acids, information is accumulating about specific functions of these sialic acids. Typical examples are the decrease of the rate of the sialidase-initiated degradation of sialocarbohydrate chains [3], the involvement in the tumor antigenic properties of human melanoma cells [4], the role in environmental adaptation [5] and binding of influenza C viruses [6, 71. Prior to chemical characterization of the sialic acids, they are in most cases released by acid or enzymic hydrolysis followed by various isolation methods [8, 91. Among the 0-acetylated species, obtained in this way, Neu5,9Ac2 is the most common neuraminic acid derivative [l, 21. In erythrocytes from various mammals, glycosidically bound Neu5,9Ac2 is the predominant 0-acetylated sialic acid species, as determined on intact cells or isolated membranes by treatment with periodate followed by acetylacetone [lo, 111. Neu5,9Ac2 often appears to be accompanied by the 7-0-acetyl analogue in variable amounts. The observation that Neu5,7Ac2 decreases frequently in favour of Neu5,9Ac2 during storage indicates 0-acetyl migration. Spontaneous migration of acetyl groups between hydroxyl groups has been Correspondence to J. P. Kamerling, Afdeling Bio-Organische Chemie, Transitorium 111, Rijksuniversiteit Utrecht, Postbus 80.075, NL-3508 TB Utrecht, The Netherlands Abbreviations. NeuSAc, N-acetyheurdminic acid; Neu4,5Ac2, Nacetyl-4-O-acetylneuraminic acid; Neu5,7Ac2, N-acetyl-7-O-acetylneurarninic acid; Neu5,8Ac2, N-acetyl-8-0-acetylneuraminic acid; Neu5,9Ac2, N-acetyl-9-0-acetylneuraminic acid; Neu5,7,9Ac3, Nacetyl-7,9-di-O-acetylneuraminic acid ; Neu5,8,9Ac3, Neu5,7,8,9Ac4, N-acetyl-7,8,9-tri-0-acetylneuraminic acid; TLC, thin-layer chromatography; GLC, gas-liquid chromatography; GLC-MS, gas-liquid chromatography/mass spectrometry; HPLC, h...

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“…The importance of divalent cation regulation at the cell surface has been studied in connection with cell growth control and synaptic transmission. Rahmann (1978) has suggested that gangliosides at the synapse bind to calcium, regulating the membrane permeability, thus controlling the movement of neurotransmitters. There are also reports of a calcium-dependent control of cell proliferation (Swierenga et al, 1978).…”

mentioning

confidence: 99%

Effects of Divalent Cations on the Glycolipids from Cultured Mouse Neuroblastoma Cells

Bremer

Sapirstein

Savage

et al. 1982

Journal of Neurochemistry

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The influence of divalent cations on glycosphingolipid metabolism was examined in the NB41A mouse neuroblastoma clonal cell line. HPLC methods were utilized to quantitate the effects on neutral glycolipids and monosialogangliosides. NB41A cells were shown to contain GM3, GM2, GM1, GD3, and GD1a by HPLC and TLC. The neutral glycosphingolipids consisted of glucosylceramide (GlcCer), lactosylceramide (LacCer), GalNAc (beta 1 leads to 4) Gal(beta 1 leads to 4)Glc(beta 1 leads to 1)Cer (GgOse3Cer), and GalNAc(beta 1 leads to 3)Gal(alpha 1 leads to 4) Gal(beta 1 leads to 4)Glc(beta 1 leads to 1)Cer (GbOse4Cer) according to their HPLC behavior. Cells grown in the presence of 1.85 mM-EGTA showed a two-to threefold increase in GM3 whereas other glycosphingolipids were only slightly affected. When cells were grown in the presence of 1.45 mM-EGTA plus 0.4 mM-EDTA a similar increase in GM3 was observed but this change was now accompanied by decreases in GM2, GM1, GgOse3Cer. The EGTA-EDTA effects were reversed when growth was in the presence of Ca2+ sufficient to bind all chelator. Mn2+ replacement reversed the chelator effects differentially; GM2 and GM1 levels were the most sensitive to increases in Mn2+ concentration; GgOse3Cer and GbOse4Cer were also sensitive, whereas GM3 was the least affected. These results suggest calcium serves an important regulatory role on GM3 levels and that manganese concentration may regulate the levels of galactosamine-containing glycolipids in mouse NB41A neuroblastoma cells.

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Brain Gangliosides and Thermal Adaptation in Vertebrates

Cited by 16 publications

References 8 publications

High resolution proton NMR investigations of rat blood plasma Assignment of resonances for the molecularly mobile carbohydrate side‐chains of ‘acute‐phase’ glycoproteins

High resolution proton NMR investigations of rat blood plasma Assignment of resonances for the molecularly mobile carbohydrate side‐chains of ‘acute‐phase’ glycoproteins

Migration of O‐acetyl groups in N,O‐acetylneuraminic acids

Effects of Divalent Cations on the Glycolipids from Cultured Mouse Neuroblastoma Cells

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