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At least 883 records · Page 49Linked to original sources
PubMed2003

Occurrence of O-linked Xyl-GlcNAc and Xyl-Glc disaccharides in trocarin, a factor Xa homolog from snake venom.

Trocarin is a 46515-Da group D prothrombin-activating glycoprotein from the venom of the Australian elapid, Tropidechis carinatus. Amino acid sequencing and functional characterization of trocarin demonstrated that it is a structural and functional homolog of mammalian blood coagulation factor (F)Xa. In this study we show that, in contrast to mammalian Xa, which is not glycosylated, trocarin contains an O-linked carbohydrate moiety in its light chain and an N-linked carbohydrate oligosaccharide in its heavy chain. Mass spectrometry and sugar compositional analysis indicate that the O-linked carbohydrate moiety is a mixture of Xyl-GlcNAc-, GlcNAc-, Xyl-Glc- and Glc- structures linked to Ser 52. The N-linked carbohydrate on Asn 45 of the heavy chain is a sialylated, diantennary oligosaccharide that is located at the lip of the active site of the prothrombin activator.

Acetylglucosamine↗
PubMed2002

Enzymatic synthesis in vitro of the disulfated disaccharide unit of corneal keratan sulfate.

Among the enzymes of the carbohydrate sulfotransferase family, human corneal GlcNAc 6-O-sulfotransferase (hCGn6ST, also known as human GlcNAc6ST-5/GST4beta) and human intestinal GlcNAc 6-O-sulfotransferase (hIGn6ST or human GlcNAc6ST-3/GST4alpha) are highly homologous. In the mouse, intestinal GlcNAc 6-O-sulfotransferase (mIGn6ST or mouse GlcNAc6ST-3/GST4) is the only orthologue of hCGn6ST and hIGn6ST. In the previous study, we found that hCGn6ST and mIGn6ST, but not hIGn6ST, have sulfotransferase activity to produce keratan sulfate (Akama, T. O., Nakayama, J., Nishida, K., Hiraoka, N., Suzuki, M., McAuliffe, J., Hindsgaul, O., Fukuda, M., and Fukuda, M. N. (2001) J. Biol. Chem. 276, 16271-16278). In this study, we analyzed the substrate specificities of these sulfotransferases in vitro using synthetic carbohydrate substrates. We found that all three sulfotransferases can transfer sulfate to the nonreducing terminal GlcNAc of short carbohydrate substrates. Both hCGn6ST and mIGn6ST, but not hIGn6ST, transfer sulfate to longer carbohydrate substrates that have poly-N-acetyllactosamine structures, suggesting the involvement of hCGn6ST and mIGn6ST in production of keratan sulfate. To clarify further the involvement of hCGn6ST in biosynthesis of keratan sulfate, we reconstituted the biosynthetic pathway in vitro by sequential enzymatic treatment of a synthetic carbohydrate substrate. Using four enzymes, beta1,4-galactosyltransferase-I, beta1,3-N-acetylglucosaminyltransferase-2, hCGn6ST, and keratan sulfate Gal 6-O-sulfotransferase, we were able to synthesize in vitro a product that conformed to the basic structural unit of keratan sulfate. Based on these results, we propose a biosynthetic pathway for N-linked keratan sulfate on corneal proteoglycans.

Amino Acid Substitution↗
PubMed2002

A bifunctional diglycosyltransferase forms the Fucalpha1,2Galbeta1,3-disaccharide on Skp1 in the cytoplasm of dictyostelium.

Skp1 is a subunit of the Skp1 cullin-1 F-box protein (SCF) family of E3 ubiquitin ligases and of other regulatory complexes in the cytoplasm and nucleus. In Dictyostelium, Skp1 is modified by a pentasaccharide with the type I blood group H antigen (Fucalpha1,2Galbeta1,3GlcNAc-) at its core. Addition of the Fuc is catalyzed by FT85, a 768-amino acid protein whose fucosyltransferase activity maps to the C-terminal half of the protein. A strain whose FT85 gene is interrupted by a genetic insertion produces a truncated, GlcNAc-terminated glycan on Skp1, suggesting that FT85 may also have beta-galactosyltransferase activity. In support of this model, highly purified native and recombinant FT85 are each able to galactosylate Skp1 from FT85 mutant cells. Site-directed mutagenesis of predicted key amino acids in the N-terminal region of FT85 abolishes Skp1 beta-galactosyltransferase activity with minimal effects on the fucosyltransferase. In addition, a recombinant form of the N-terminal region exhibits beta-galactosyltransferase but not fucosyltransferase activity. Kinetic analysis of FT85 suggests that its two glycosyltransferase activities normally modify Skp1 processively but can have partial function individually. In conclusion, FT85 is a bifunctional diglycosyltransferase that appears to be designed to efficiently extend the Skp1 glycan in vivo.

Animals↗
PubMed2006

Galectin-3 interaction with Thomsen-Friedenreich disaccharide on cancer-associated MUC1 causes increased cancer cell endothelial adhesion.

Patients with metastatic cancer commonly have increased serum galectin-3 concentrations, but it is not known whether this has any functional implications for cancer progression. We report that MUC1, a large transmembrane mucin protein that is overexpressed and aberrantly glycosylated in epithelial cancer, is a natural ligand for galectin-3. Recombinant galectin-3 at concentrations (0.2-1.0 microg/ml) similar to those found in the sera of patients with metastatic cancer increased adhesion of MUC1-expressing human breast (ZR-75-1) and colon (HT29-5F7) cancer cells to human umbilical vein endothelial cells (HUVEC) by 111% (111 +/- 21%, mean +/- S.D.) and 93% (93 +/- 17%), respectively. Recombinant galectin-3 also increased adhesion to HUVEC of MUC1 transfected HCA1.7+ human breast epithelial cells that express MUC1 bearing the oncofetal Thomsen-Friedenreich antigen (Galbeta1,3 GalNAc-alpha (TF)) but did not affect adhesion of MUC1-negative HCA1.7-cells. MUC1-transfected, Ras-transformed, canine kidney epithelial-like (MDE9.2+) cells, bearing MUC1 that predominantly carries sialyl-TF, only demonstrated an adhesive response to galectin-3 after sialidase pretreatment. Furthermore, galectin-3-mediated adhesion of HCA1.7+ to HUVEC was reduced by O-glycanase pretreatment of the cells to remove TF. Recombinant galectin-3 caused focal disappearance of cell surface MUC1 in HCA1.7+ cells, suggesting clustering of MUC1. Co-incubation with antibodies against E-Selectin or CD44H, but not integrin-beta1, ICAM-1 or VCAM-1, largely abolished the epithelial cell adhesion to HUVEC induced by galectin-3. Thus, galectin-3, by interacting with cancer-associated MUC1 via TF, promotes cancer cell adhesion to endothelium by revealing epithelial adhesion molecules that are otherwise concealed by MUC1. This suggests a critical role for circulating galectin-3 in cancer metastasis and highlights the functional importance of altered cell surface glycosylation in cancer progression.

Antigens, Tumor-Associated, Carbohydrate↗
PubMed1985

Dose dependence of breath hydrogen and methane in healthy volunteers after ingestion of a commercial disaccharide mixture, Palatinit.

Breath hydrogen and methane were determined by gas chromatography in eleven normal individuals given a low-fibre, mixed diet (control) and after ingestion of 20-50 g Palatinit/d, an equimolar mixture of D-glucosyl-alpha(1----1)-D-mannitol and D-glucosyl-alpha(1----6)-D-glucitol (Isomalt). A linear relation was found (r 0.85; P less than 0.001) between the amount of Palatinit ingested and breath H2 per 10 h in subjects who did not exhale methane. If methane was formed in addition to H2, the sum of both gases followed a linear dose-effect relation. The mouth-to-caecum time, indicated by the first increase in breath H2 after ingestion, was shortened by about half, yet no sign of diarrhoea was observed. Stool weight and stool frequency did not change significantly. The linear relation between a dose of 20-50 g Palatinit and exhalation of H2 (eventually plus methane) indicated that a relatively constant fraction of the dose given underwent cleavage and absorption in the small intestine, the remainder being transported into the large bowel. Microbial gas formation in the colon as well as the fractional transfer of these gases into the expiratory air occurred at fixed proportions, thus allowing an insight into colonic microbial contributions to carbohydrate utilization in the human large bowel.

Adult↗
PubMed1994

DNA-carbohydrate interaction. The effects of mono- and disaccharides on the solution structure of calf-thymus DNA.

We report the interaction of calf-thymus DNA with D-glucose, D-fructose, D-galactose and sucrose in aqueous solution at physiological pH with sugar/DNA(P)(P = phosphate) molar ratios (r) of 1/10, 1/5, 1, 5 and 10. FTIR difference spectroscopy was used to characterize the nature of sugar-DNA interaction and correlations between spectral changes and structural variations for both sugar and DNA complexes have been established.

Animals↗
PubMed2001

First isolation of geranyl disaccharides from ginger and their relations to aroma formation.

Three geraniol glycosides were isolated from immature fresh ginger rhizomes (Zingiber officinale Roscoe). Their structures were identified as geranyl 6-O-alpha-L-arabinopyranosyl-beta-D-glucopyranoside (1) geranyl 6-O-beta-D-apiofuranosyl-beta-D-glucopyranoside (2) and geranyl 6-O-beta-D-xylopyranosyl-beta-D-glucopyranoside (3) by spectrometric analyses. After incubating each glycoside with a crude enzyme solution prepared from ginger, geraniol was liberated in all of those fractions. This result indicates that the glycosides are related to the formation of geraniol-related compounds in ginger aroma.

Acyclic Monoterpenes↗
PubMed1994

The clinical significance of disaccharide maldigestion.

The prevalence of lactose maldigestion is lowest in Scandinavia and Northwest Europe (3-8%) and close to 100% in most of Southeast Asia. In Europe the frequency increases in the southern and eastern directions, reaching 70% in southern Italy and Turkey. There is also a high prevalence of lactose maldigestion in the people of Africa with the exception of cattle-raising nomads. Lactose maldigestion causes uncharacteristic abdominal symptoms such as bloating, borborygmus, colic, flatulence, and diarrhea. The degree of discomfort depends on the amount of lactose consumed, but also on an individual sensitivity to lactose. The symptoms of irritable bowel syndrome (IBS) and lactose maldigestion are similar. Consequently, most investigations indicate an increased frequency of lactose maldigestion in patients suffering from IBS. Recurrent abdominal pain (RAP) in children corresponds to IBS in adults. Lactose maldigestion is a frequent cause of RAP in regions with a high prevalence of lactose maldigestion in early childhood. Diffuse small-intestinal damage in celiac disease or kwashiorkor leads to a proportional decrease of all disaccharidase activities, with the most pronounced being decrease of lactase. The consumption of milk may then cause abdominal discomfort and increased diarrhea. Several investigations have indicated an increased frequency of lactose maldigestion in patients with osteoporosis. A connection between lactose maldigestion and decreased absorption of calcium has not been proven, however. The increased tendency toward osteoporosis is more likely caused by a lower calcium intake because of milk intolerance. Milk and dairy products with reduced lactose content are better tolerated by patients with lactose maldigestion.(ABSTRACT TRUNCATED AT 250 WORDS)

Disaccharides↗
PubMed1996

Forssman disaccharide is the specific ligand of a galectin from the sponge Geodia cydonium but does not mediate its binding to nuclear protein np56.

The galectin from Geodia cydonium (GCA) had previously been shown to be involved in regulatory mechanisms of cell sorting and adhesion during reaggregation of allogeneic sponge cells. In this contribution the binding specificity of GCA was established to be GalNAc alpha 1-3GalNAc beta as structural component of Forssman pentasaccharide. Crossreactivities of terminal structural elements were revealed in the order GalNAc alpha 1-3GalNAc beta > GalNAc alpha 1-3(Fuc alpha 1-2)Gal beta >> Gal beta 1-3GlcNAc beta > Gal beta 1-4Glc. Lectin binding to the Forssman antigen (Ki range 10(-7)) or to blood group A-trisaccharide exceeded that to lactose (Ki range 10(-3)/10(-2)) by three to four orders of magnitude. Cytochemical staining of eukaryotic cells on the light and electron microscopic level revealed lectin binding in the cytosol and in the nucleus (nucleoli), which was inhibitable with the soluble high affinity ligands. The nuclear binding of GCA could be ascribed to affinity-isolated 56 kDa protein (np56) in the nucleoplasm and was shown to be mediated by the peptide conformation of the ligand. Although GCA-np56 interaction was inhibitable with Forssman glycolipid or globopentaose, the carbohydrate binding site of the lectin is not involved due to the lack of competition by Forssman-specific lectins HPA or DBA. Since anti-CBP70 was immunologically cross-reactive to np56, it is concluded that the galectin GCA binds to np56 via similar mechanisms as reported previously for the interaction of CBP-35 (galectin-3) and CBP-70. Thus, GCA resembles galectin-3 in its binding characteristics but is likewise related to galectin-1 by sequence homology of its primary structure and by the molecular mass of its subunits.

Animals↗
PubMed2003

Cleavage of DNA without loss of genetic information by incorporation of a disaccharide nucleoside.

A ribose residue inserted between the 3'-OH of one nucleotide and the 5'-phosphate group of the next nucleotide, functions as a site-specific cleavage site within DNA. This extra ribose does not interrupt helix formation and it protects duplex DNA against cleavage by restriction enzymes. Cleavage can be obtained with periodate and all ribose fragments can be removed with sodium hydroxide. As a result of this, an intact natural oligodeoxynucleotide is obtained after ligation reaction, which means that site-specific cleavage and recovering of intact DNA occurs without loss of genetic information.

Adenosine Triphosphate↗