[51] Glycolipids

Basu, Manju; De, Trim; Das, Kinsuk; Kyle, John W.; Chon, Hung-Che; Schaeper, Robert J.; Basu, Subhash

doi:10.1016/0076-6879(87)38053-x

Cited by 98 publications

(54 citation statements)

References 72 publications

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“…As for sialyltransferase I, which is involved in gdnglioside biosynthesis, Basu et al suggested that this enzyme may recognize the terminal fi-galactosyl residue of any glycolipid or glycoconjugate acceptor [22].…”

Section: Discussionmentioning

confidence: 99%

Substrate specificity of α2↔3‐sialyltransferases in ganglioside biosynthesis of rat liver golgi^*

Iber

Echten

Sandhoff

1991

European Journal of Biochemistry

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The acceptor specificities of four sialyltransferases (I, 11, IV and V) involved in ganglioside biosynthesis were studied in Golgi vesicles derived from rat liver. The activities of these sialyltransferases were strongly detergent-dependent. Competition experiments with different detergent concentrations using LacCer (Gal~1+4GlcP1 -+lCer), GMia [Gal~1-+3GalNAc~1+4(NeuAca2+3)Gal~1-+4Glc~1 +1Cer] and GDlb [GalPI -+3GalNAc~l+4(NeuAca2+8NeuAca2+3)Gal~1+4Glc/31 +1Cer] as substrates, and as mutual inhibitors for ganglioside sialyltransferase activity, suggested that sialyltransferase IV was able to catalyze the sialyltransfer in a 2 4 3 linkage to the galactose residues of LacCer as well as of GMia and GDlb. The other three sialyltransferases (I, I1 and V) seemed to be quite specific for their respective glycolipid acceptors, LacCer, GM3 and GMlb, GDla and GTlb. Furthermore the kinetic data showed that sialyltransferase I was inactive at higher detergent concentrations (> 75 pg Triton CF-54); under these conditions, formation of GM3 and GDla was catalyzed only by sialyltransferase IV. These results have been integrated into a model for ganglioside biosynthesis and its regulation.Correspondence to K. Sandhoff, Institut fur Orgdnische Chemie und Biochemie der Universitat Bonn, Gerhard-Domagk-StraDe 1 , W-5300 Bonn 1, Federal Republic of Germany Abbreviations. Cer, ceramide (N-acylsphingosine); Gal, galactose; GalNAc, N-acetylgalactosamine; Glc, glucose; NeuAc, N-acetylneuraminic acid; UDP-Gal, uridine 5'-diphosphogalactose; UDPGalNAc, uridine 5'-diphospho-N-acetylgalactosamine ; CDP-choline, cytidine 5'-diphosphocholine; CMP-NeuAc, cytidine 5'-monophospho-N-acetylneuraminic acid; GlcCer, glucosylceramide, Glcl + 1Cer; LacCer,Gal~l+4Glc~I+ 1Cer; GM3,NeuAca2+3Galbl +4Glc/j'l+ 1Cer;GD3,NeuACa2 + 8NeuAca2 + 3GalP1 + 4Glcbl + 1Cer; GT3, NeuAca2+ 8NeuAca2+ 8NeuAca2-3Gal~l+4Glcfll+ 1Cer; GAZ, GalNAc~1-+4Gal~l+4Glc/?l+ 1Cer; GM2,GalNAcpl +4(NeuAca2 + 3)Galfll + 4GlcP1 + 1Cer; GDZ, GalNAcPl + 4(NeuAca2 + 8NeuAca2+3)Gal~1-+4GlcfiI + 1Cer; GT2,GalNAcP1 +4(NeuAca2 +8NeuAca2+8NeuAca2+3)Gal~I+4Glc~l+ 1Cer; GAI,Galbl + 3GalNAc~1+4Gal/31+4Glc~I +lCer; Gall1 +3GalNAcbl+ 4(NeuAca2+3)Galfl1 -+4GlcP1+ 1Cer; GDlb, GalPl+3GalNAcBI + 4(NeuAca2 + 8NeuAca2 + 3)GalBl -t4Glc/31+ 1Cer; GTlcrGalbl + 3GalNAcP1 + 4(NeuAca2 + 8NeuAca2 + 8NeuAca2 + 3)GalbI + 4GlcB1+ 1Cer; GDl,,NeuAca2-+3GalP1 +3GalNAcb1 +4(NeuAca2 -+3)Galfi1+4Glc~1+ 1Cer; GTihiNeuAca2+3Gal~1 + 3GalNAcP1 + 4(NeuAca2 + 8NeuAca2 + 3)Galbl + 4Glcj1 + 1Cer; GQ,,, NeuAca2 + 3Galb1 + 3GalNAcb1 + 4(NeuAca2 + 8NeuAca2 + 8-NeuAca2+ 3)GalP1+4GlcPI+ 1 Cer; GD1,,NeuAca2+8NeuAca2+ 3 C a l~1 + 3 G a l N A c~1 + 4 G a l~1 + 4 G l c~l +ICer; GTla,NeuAca2-+ 8NeuAca2 + 3Galb1 + 3GalNAcBI + 4(NeuAca2 + 3)GalBl -+ 4GlcPl+ 1Cer; GQlb,NeuAca2 +8NeuAca2+3Gal~l+3GalNAcPl 4(NeuAca2 --t 8NeuAca2 + 3)Galjl + 4GlcP1 + 1Cer; GPlcr NeuAca2 + 8NeuAca2 + 3GalP1 --* 3GalNAcP1 + 4(NeuAca2 + 8NeuAca2 + 8NeuAca2 + 3 ) G a l~1 + 4 G l c~I +

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Section: Discussionmentioning

confidence: 99%

Substrate specificity of α2↔3‐sialyltransferases in ganglioside biosynthesis of rat liver golgi^*

Iber

Echten

Sandhoff

1991

European Journal of Biochemistry

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“…Traditionally, this is accomplished by dispersing the substrate with detergents [18,29,30]. For this reason, the enzyme activity was assayed in the presence of Triton CF-54 [15] and labeled CMPNeu5Ac. Four GM1 molecular species carrying the same C18:1 LCB moiety and acyl chains of different length were tested.…”

Section: Pitto Et Al/febs Letters 383 (1996) 223-226mentioning

confidence: 99%

“…Incubation was at 37°C for 1 h. Blanks were prepared by omitting GM~ in the reaction mixture. At the end of the incubation, the reaction mixture was applied on Whatman 3MM paper and developed by descending chromatography in 1% tetraborate, followed by radioactivity counting of the appropriate areas [15].…”

Section: Preparation Of Rat Liver Golgi Membranesmentioning

confidence: 99%

“…Assay of SAT IV activity on GM1 ganglioside using CMP- [9-aH]Neu5Ac SAT IV activity was routinely assayed upon GM~ ganglioside according to a widely used procedure [15][16][17], by radiochemical quantification of the product (GDla ganglioside). Briefly, incubation mixtures contained 0.2% Triton CF-54, 20-30 Bg of the Golgi fraction (as protein), 0.0254).4 mM GM1 and 0.5 mM CMP-[9-3H]Neu5Ac (100000 dpm) as sialic acid acceptor and donor, respectively, in a final volume of 50 B1 of 154 mM cacodylate buffer, pH 6.5.…”

Section: Preparation Of Rat Liver Golgi Membranesmentioning

confidence: 99%

See 1 more Smart Citation

Dependence of rat liver CMP‐N‐acetylneuraminate:GM₁ sialyltransferase (SAT IV) activity on the ceramide composition of GM₁ ganglioside

Pitto¹,

Palestini²,

Masserini³

1996

FEBS Letters

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The dependence of CMP-N-acetylneuraminate:GMl sialyltransferase (SAT IV) activity of rat liver Golgi apparatus on GM1 ganglioside ceramide composition was evaluated. SAT IV activity was assayed on GMI molecular species carrying homogeneous ceramide moieties containing long chain bases of different length (18 or 20 C atoms) unsaturated or not, linked to 14:0, 16:0, 18:0 or 22:0 fatty acids. The results obtained in the presence of the detergent Triton CF-54, when enzyme and substrate are presumably part of the same supramolecular structure, show that either the long chain base or the fatty acid composition can affect enzyme activity. This feature was not displayed when GM1 was embedded in dipalmitoylphosphatidylcholine vesicles in the absence of detergent. Under the latter conditions, the enzyme was not sensitive to the lipid composition of GMI but to the gangliosidelphospholipid ratio in the vesicles. These results indicate for the first time that SAT IV is affected by the lipid composition of the substrate and strengthen the hypothesis that glycosyltransferases may contribute to control the cellular glycosphingolipid ceramide pattern.1~ ey words." Sialyltransferase; GM1 ; Ceramide [6,7]. Moreover, it has been shown that glycosyltransferases are able to recognize different molecular species of the substrate, providing a mechanism aiming to maintain the glycolipid ceramide pattern of a given tissue [8]. The present work was carried out in order to assess whether SAT IV differentially affects molecular species of the same substrate, namely GM1 ganglioside, carrying different, homogeneous, ceramide moieties.

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“…In gangliosides, more than 100 molecular species have been identified on the basis of the diversity of their carbohydrate structures [l]. The structural diversity is caused by specific glycosyltransferases which sequentially transfer monosaccharides [2]. Previous studies have suggested that gangliosides may play important rolds in a variety of biological phenomena, such as cell-cell and cell-substratum interactions, growth and differentiation, cell transformation, and signal transduction pathways (for reviews see [3][4][5][6]).…”

Section: Intmduetlonmentioning

confidence: 99%

A unique biosynthetic pathway for gangliosides exists in Xenopus laevis oocytes

1994

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It was previously reported that monosialosylgangliopentaosyl ceramide (Ga1NAc‐GM1b) was a major ganglioside in Xenopus laevis oocytes. Here we determined biosynthetic pathways for the ganglioside by detailed measurements of glycosyltransferase activities. CMP‐NeuAc:asialo‐GM1 α2–3 sialyltransferase (α2–3 ST) and UDP‐Ga1NAc:GM1b β1–4 N‐acetylgalactosaminyltransferase (β1–4 Ga1NAcT) exhibited much higher activity than CMP‐NeuAc:Ga1NAc‐GA1 α2–3 ST and UDP‐Ga1NAc:asialo‐GM1 β1–4 Ga1NAcT, respectively. These observations indicated the existence of a unique biosynthetic pathway in the oocytes as follows; asialo‐GM1 → GM1b → Ga1NAc‐GM1b.

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[51] Glycolipids

Cited by 98 publications

References 72 publications

Substrate specificity of α2↔3‐sialyltransferases in ganglioside biosynthesis of rat liver golgi^*

Substrate specificity of α2↔3‐sialyltransferases in ganglioside biosynthesis of rat liver golgi^*

Dependence of rat liver CMP‐N‐acetylneuraminate:GM₁ sialyltransferase (SAT IV) activity on the ceramide composition of GM₁ ganglioside

A unique biosynthetic pathway for gangliosides exists in Xenopus laevis oocytes

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[51] Glycolipids

Cited by 98 publications

References 72 publications

Substrate specificity of α2↔3‐sialyltransferases in ganglioside biosynthesis of rat liver golgi*

Substrate specificity of α2↔3‐sialyltransferases in ganglioside biosynthesis of rat liver golgi*

Dependence of rat liver CMP‐N‐acetylneuraminate:GM1 sialyltransferase (SAT IV) activity on the ceramide composition of GM1 ganglioside

A unique biosynthetic pathway for gangliosides exists in Xenopus laevis oocytes

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Substrate specificity of α2↔3‐sialyltransferases in ganglioside biosynthesis of rat liver golgi^*

Substrate specificity of α2↔3‐sialyltransferases in ganglioside biosynthesis of rat liver golgi^*

Dependence of rat liver CMP‐N‐acetylneuraminate:GM₁ sialyltransferase (SAT IV) activity on the ceramide composition of GM₁ ganglioside