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PubMed1981

Relationship between transport of D-xylose and other monosaccharides in jejunal mucosa of children.

In order to clarify the relationship between the transport of D-xylose, D-glucose, and Na in human gut, several characteristics of D-xylose uptake were examined in jejunal biopsies from 47 children (45 with normal intestinal function and 2 with glucose-galactose malabsorption). Standard in vitro techniques were used, with the following results: In tissue accumulation experiments with Ringer solution, the intracellular D-xylose concentration (C) was not significantly different from the medium D-xylose concentration (M) (C/M = 1.10 +/- 0.08). D-Xylose uptake was not affected by the disappearance of the Na electrochemical gradient in the presence of ouabain or DNP (C/M = 1.02 +/- 0.16 and 0.96 +/- 0.04, respectively). However, in Na-free solution, D-xylose uptake decreased (C/M = 0.47 +/- 0.08). The influx of 10 mM D-xylose across the luminal membrane (Jmcxyl = 1.34 mumol/h . cm2) was not significantly influenced by 2 mM phlorizin (Jmcxyl - 1.25 mumol/h . cm2), which is a competitive inhibitor of D-glucose transport. Removal of Na from the incubation medium, reduced Jmcxyl by 55%. Galactose (40 mM) and fructose (40 mM) did not inhibit Jmcxyl (2.18 and 2.27 mumol/h . cm2, respectively). In Ussing chambers, D-xylose did not stimulate the short-circuit current (Isc), neither did it interfere with the increase in Isc induced by glucose. In the congenital absence of glucose and galactose active transport, D-xylose entry into the cell was unaltered. These results support the concept that in jejunal mucosa of children, D-xylose is at least in part, transported by a system that is different from those for fructose and Na-dependent D-glucose (hexose) transport.

Adolescent↗
PubMed1994

Novel (rhamnosyl and ribosyl) and uncommon (xylosyl) monosaccharide residues are present in asparagine-linked oligosaccharides of the trypanosomatid Blastocrithidia culicis.

Blastocrithidia culicis is a trypanosomatid protozoon that transfers Man6GlcNAc2 in protein N-glycosylation. Compounds containing mannosyl, xylosyl, and rhamnosyl residues were found among the endo-beta-N-acetylglucosaminidase H-sensitive oligosaccharides of whole cell glycoproteins of this parasite. The compositions of some of them were as follows: Man5GlcNAc2, Man6GlcNAc2, Rha1Man5GlcNAc2, Rha2Man6GlcNAc2, Xyl1Rha2Man6-GlcNAc2, Xyl1Rha3Man6GlcNAc2, and Xyl2Rha3Man6-GlcNAc2. On the other hand, oligosaccharides containing mannosyl, xylosyl, rhamnosyl, and ribosyl units were liberated from endo-beta-N-acetylglucosaminidase-resistant glycopeptides upon treatment with N-glycanase. This is the first report on the presence of ribosyl units in eukaryote glycoconjugates, of rhamnosyl residues in asparagine-linked oligosaccharides, and of xylosyl units in high mannose-type compounds.

Animals↗
PubMedDate not supplied

[Effects of the monosaccharide derivative 8RN-DAGal on the putative P-type calcium channel expressed in Xenopus oocytes].

P-type calcium channels are expressed in Xenopus oocytes after injection of rat cerebellar mRNA. The FTX and omega-Aga-IVa toxins extracted from Agelenopsis aperta venom are known to inhibit the activity of this channel. The present results demonstrate that 8RN-DAGal is also a antagonist of P-type calcium channels. The inhibition of the current, obtained with Ba2+, as charge carrier, is voltage dependent.

Animals↗