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PubMedDate not supplied

[Tolerance tests in the diagnosis of mono- and disaccharides malabsorption in children].

The carbohydrate tolerance test is a very common method employed in the diagnosis of carbohydrate malabsorption, despite the possibility of some pitfalls in its interpretation. There are some factors, namely, the omission of the 15 minute blood sample, slow gastric emptying, malnutrition and venous blood sampling, that can condition the characterization of false positive intolerance. We studied 177 curves performed in 110 children during a 4 year period, and we observed that: a) the highest peak level occurred at 15 minutes in 57,3% of the tolerance tests; b) if the 15 minutes sample was not obtained it resulted in 28% of false positive intolerance; c) regarding the nutritional status malnourished children had more frequently a delayed peak level, been 17% at 15 minutes and 67% at 30 minutes. Misinterpretation of the carbohydrate tolerance test can be minimized taking into account these known factors that induced the diagnosis of false positive intolerance.

Blood Glucose↗
PubMed1995

Monoclonal antibody BW835 defines a site-specific Thomsen-Friedenreich disaccharide linked to threonine within the VTSA motif of MUC1 tandem repeats.

mAb BW835 (IgG1) has been generated to breast cancer cell lines by alternating injections of MCF-7 or SW-613 cells and has been demonstrated to be of value in the serodiagnosis of mammary carcinoma. BW835 defines a carbohydrate epitope on integrated or secreted MUC1 glycoforms from carcinoma cells and human milk. To identify BW835-reactive glycopeptides on MUC1, proteolytic fragments of the mucin obtained by digestion with the Gly-C-specific endopeptidase IV from papaya corresponding to low molecular mass fragments (< 10 kilodaltons) of the tandem repeat domain were screened. A glycosylated fragment (glycopeptide 17) containing the mAb HMFG-2-defined epitope was highly reactive to BW835 antibody, while nonglycosylated tandem repeat peptide TAP25 or its in vitro-glycosylated N-acetylgalactosamine (GalNAc) derivatives were unreactive. Glycopeptide 17 bound to peanut agglutinin and to a Thomsen-Friedenreich antigen (TF alpha)-specific mAb (A78-G/A7). Binding of BW835 to glycopeptide 17 or to MUC1 was competitively inhibited by peanut agglutinin and by the synthetic glycopeptides TF alpha Ser or TF alpha Thr but not by their beta-anomers. Evidence for site specificity of binding by BW835 to glycopeptide 17 was revealed by demonstrating nonreactivity of the antibody to other TF alpha-expressing glycoproteins with peptide moieties lacking MUC1-specific motifs at putative glycosylation sites. The epitope of BW835 was localized to threonine within the VTSA-peptide motif by site-specific enzymatic beta-galactosylation of the synthetic tandem repeat peptide TAP25-GalNAc1 TAPPAHGVT(-O-alpha GalNAc)SAPDTRPAPGSTAPPA. This is the first report on a TF alpha-specific mAb that shows a strict peptide sequence dependency of binding.

Amino Acid Sequence↗
PubMed1983

Selective depolymerisation of keratan sulfate: production of radiolabelled substrates for 6-O-sulfogalactose sulfatase and beta-D-galactosidase.

Keratan sulfate (KS) was N-deacetylated with anhydrous hydrazine and then degraded with nitrous acid, and the products were reduced with NaBT4. Radiolabelled disaccharides constituted at least 76% of the total oligosaccharide fraction. Three major disaccharides were isolated and identified. Of the total disaccharide isolated from bovine intervertebral-disc and human costal-cartilage, 91 and 79%, respectively, was identified as a disulfated disaccharide, O-(beta-D-galactopyranosyl 6-sulfate)-(1 leads to 4)-2,5-anhydro-D-[1-3H]mannitol 6-sulfate (Gal6S-anM6S). The disaccharide fraction isolated from bovine-cornea KS contained only 14% of Gal6S-anM6S. The yield of monosulfated disaccharide, identified as O-beta-D-galactopyranosyl-(1 leads to 4)-2,5-anhydro-D-[1-3H]mannitol 6-sulfate, was 9, 17, and 84% of the total KS-disaccharide fraction isolated from intervertebral disc, costal cartilage, and cornea, respectively. For each of the KS type studied, the yield of unsulfated disaccharide was less than 4% of the total disaccharide-fraction. The tetrasaccharides were fractionated, on the basis of their sulfate content, into at least four species by paper electrophoresis, and some tentative structures are proposed. Disaccharide and tetrasaccharide species were evaluated as substrates for beta-D-galactosidase and 6-O-sulfogalactose sulfatase.

Animals↗
PubMed1994

The sulphation pattern in chondroitin sulphate chains investigated by chondroitinase ABC and ACII digestion and reactivity with monoclonal antibodies.

We have used progressive chondroitinase digestion of pig aggrecan in conjunction with ELISA assays and disaccharide analysis to derive information about the pattern of 4- and 6-sulphation in chondroitin sulphate chains. Digestion with chondroitinase ABC resulted in the release of mainly disaccharides from the nonreducing terminal of chondroitin sulphate chains but there was also the release of some tetra- and hexa-saccharides which were degraded to disaccharides with more extensive digestion. Chondroitinase ACII, in contrast, released only disaccharides. Analysis of the disaccharide composition of the intact and digested products at different stages of digestion showed that there was a slight increase in 6-sulphate content of the chains as they were shortened. Reaction of the partially digested proteoglycans with monoclonal antibodies 3-B-3 and 3-D-5 which recognise chains terminating in 6- or 4-sulphated disaccharides, respectively, showed major differences between chondroitinase ABC and ACII products. The results suggested that chondroitinase ABC preferentially cleaved next to 4-sulphated, rather than 6-sulphated disaccharides and this resulted in some oligosaccharides as well as disaccharide being released. Chondroitinase ACII also cleaved an additional disaccharide next to the linkage to protein of chondroitin sulphate, which was not removed by chondroitinase ABC and this disaccharide was mainly nonsulphated.

Aggrecans↗
PubMed1998

Detection of a potential receptor for the H-blood-group antigen on rat colon-carcinoma cells and normal tissues.

Up-regulation of the synthesis of carbohydrate tumor-associated antigens terminated by the disaccharide Fucalpha1-2Gal is frequent in colon carcinoma and associated with poor prognosis. There is evidence that Fucalpha1-2Gal (H-disaccharide) structures increase cancer-cell motility and tumorigenicity by as-yet unknown mechanisms. Using polyacrylamide-based neoglycoconjugates, we looked for a potential receptor for this disaccharide, and observed that a neoglycoconjugate probe containing the H-disaccharide could bind rat colon-carcinoma cells in a dose-dependent manner, whereas very little binding was evidenced when a probe containing glucose was used. Binding of the H-disaccharide probe could be inhibited by the free H-disaccharide as well as by unlabeled neoglycoconjugates containing a terminal H-disaccharide. The best inhibitor was the H-type-1 trisaccharide neoglycoconjugate. Histochemical detection of the potential H-receptor was performed on rat normal tissues and in situ 1,2-dimethylhydrazine-induced colon carcinomas. A strong binding of the H-disaccharide probe was evidenced on most tumors that could be partly inhibited by the trisaccharide Fucalpha1-2Galbeta1-4Glc and by the unlabeled H-disaccharide neoglycoconjugate, indicating carbohydrate specificity of the binding. Staining of normal colonic mucosa was much weaker. Strong staining was also observed on some normal tissues, such as the spleen or lymph nodes, while others, such as lungs or liver, were negative. Probes containing glucose or the Lewis-a trisaccharide did not stain tumors or normal tissues. These results provide preliminary evidence for the existence of H-specific binding sites, the number of which increases in colon carcinoma.

ABO Blood-Group System↗