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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Lectin-binding studies were performed on rat pancreatic zymogen granules to investigate the influence of glucocorticoid levels on saccharide membrane composition. The following animal groups were used: (1) control rats; (2) rats treated with hydrocortisone (1, 10 and 25 mg/kg/day) for 1, 3 and 8 days; (3) postadrenalectomized rats at days +1, +3 and +8; and (4) adrenalectomized rats receiving hydrocortisone therapy (10 mg/kg/day) for 8 days. By flow cytometry, fluoresceinated (FITC) lectins were used to measure the amount of Concanavalin A (Con A) (specific for D-mannose), wheat germ agglutinin (WGA) (specific for N-acetyl-D-glucosamine) and sialic acids and Tetragonolobus purpureus (TP) (specific for L-fucose) bound to individual zymogen granules from two subpopulations, Z1 and Z2, identified on the basis of their forward and side scatter properties. The molar ratio of the different FITC-lectins revealed significant differences in the glycoconjugate composition of Z1 and Z2 granules, the Z1 granules showing higher ratios of N-acetyl-D-glucosamine:L-fucose and N-acetyl-D-glucosamine:D-mannose, both in control, adrenalectomized and hydrocortisone-treated rats. It was also observed that N-acetyl-D-glucosamine and/or sialic acids were more abundant than L-fucose and D-mannose in the zymogen granule membrane. Z1 and Z2 granules had different glycosylation patterns. Neither adrenalectomy nor hydrocortisone treatments varied the Con A binding to zymogen granules. An increase in WGA binding was only induced by administration of very high doses of hydrocortisone (25 mg/kg/day) for 8 days, an effect not directly related to glucocorticoids. In contrast, a correlation between the FITC-TP labelling and glucocorticoid levels can be established, so that, in a time-dose dependent way, an increase was observed in zymogen granules of rats treated with hydrocortisone while a decreased TP binding was found in adrenalectomized rats-an effect which was reversed with hydrocortisone therapy. Therefore, glucocorticoids exert a direct influence on the saccharide composition of rat pancreatic zymogen granules, regulating the amount of L-fucose glycoconjugates, with Z2 granules more sensitive than Z1 ones.
Mol Cell Endocrinol 1997 Oct 20
PMID:Glucocorticoids regulate L-fucose glycoconjugates in rat pancreatic zymogen granules. 940 57

Curcumin, the coloring principle of the commonly used spice turmeric (Curcuma longa) was fed at 0.5% in the diet to streptozotocin-induced diabetic Wistar rats for 8 weeks. Renal damage was assessed by the amount of proteins excreted in the urine and the extent of leaching of renal tubular enzymes: NAG, LDH, AsAT, AlAT, alkaline and acid phosphatases. The integrity of kidney was assessed by measuring the activities of several key enzymes of the renal tissue: glucose-6-phosphate dehydrogenase, glucose-6-phosphatase, and LDH (Carbohydrate metabolism), aldose reductase and sorbitol dehydrogenase (polyol pathway), transaminases, ATPases and membrane PUFA/SFA ratio (membrane integrity). Data on enzymuria, albuminuria, activity of kidney ATPases and fatty acid composition of renal membranes in diabetic condition suggested that dietary curcumin brought about significant beneficial modulation of the progression of renal lesions in diabetes. These findings were also corroborated by histological examination of kidney sections. It is inferred that this beneficial ameliorating influence of dietary curcumin on diabetic nephropathy is possibly mediated through its ability to lower blood cholesterol levels.
Mol Cell Biochem 1998 Apr
PMID:Amelioration of renal lesions associated with diabetes by dietary curcumin in streptozotocin diabetic rats. 956 45

Ursodeoxycholic acid 7-N-acetylglucosaminides (UDCA 7-NAGs) are novel conjugated metabolites whose urine levels are expected to be a specific diagnostic index for primary biliary cirrhosis. To obtain a specific antibody which is useful for developing immunochemical analytical methods of UDCA 7-NAGs, a variety of monoclonal antibodies have been generated. Spleen cells from an A/J mouse, which had been immunized with a conjugate of nonamidated UDCA 7-NAG and bovine serum albumin, were fused with P3/NS1/1-Ag4-1 myeloma cells. After screening by an enzyme-linked immunosorbent assay (ELISA) using a beta-galactosidase-labeled antigen, thirteen kinds of antibody-secreting hybridoma clones were established. Binding properties of these monoclonal antibodies were investigated in detail by ELISA. One of these antibodies, Ab-#8 (gamma1, kappa) had the most favorable characteristics for clinical application, which was group-specific to the 7-NAG conjugates of nonamidated, glycine- and taurine-amidated UDCAs providing a highly sensitive dose-response curve for each conjugate (midpoint 17 pg per assay for nonamidated UDCA 7-NAG). Cross-reactivities with eleven kinds of bile acids, including some potential interfering metabolites as UDCA 3-sulfate, were negligibly low. By using direct ELISA based on Ab-#8, daily urinary excretion rates of UDCA 7-NAGs of two healthy subjects were determined to be 1030 and 469 microg as GUDCA 7-NAG equivalent.
J Steroid Biochem Mol Biol 1998 Feb
PMID:Production and characterization of group-specific monoclonal antibodies recognizing nonamidated, glycine- and taurine-amidated ursodeoxycholic acid 7-N-acetylglucosaminides. 960 11

Soil bacteria of the genera Azorhizobium, Bradyrhizobium, and Rhizobium liberate morphogenetic lipochitin-oligosaccharides (Nod factors) into legume rhizospheres. Nod factors, which are synthesized by the products of rhizobial nodulation (nod) genes, vary in core length as well as in the number and type of substitutions. In Rhizobium sp. NGR234, the N-acylated pentamers of N-acetyl-D-glucosamine carry an O-methylfucose group on the reducing terminus that is substituted, on a mutually exclusive basis, with either an acetyl or a sulfuryl group. A sulfotransferase encoded by noeE is required for adjunction of activated sulfate donated by 3'-phosphoadenosine 5'-phosphosulfate (PAPS). Here we show that when expressed in NGR234 cured of its symbiotic plasmid (= ANU265) or when purified as a fusion protein (MBP-NoeE), NoeE transfers sulfate from PAPS to fucosylated lipochitin-oligosaccharides. Enzyme assays showed that sulfotransferase activity is dependent on the presence of an acyl group (stearic and vaccenic acids were tested) since no activity was detected when fucosylated oligochitins (oligomers of two to six N-acetyl-D-glucosamine units) were used as substrates. Thus, NoeE is unique in that it is the only characterized sulfotransferase that is specific for fucosylated Nod factors. It probably acts after NodA, which acylates the amino-sugar backbone.
Mol Plant Microbe Interact 1998 Jul
PMID:In vitro sulfotransferase activity of NoeE, a nodulation protein of Rhizobium sp. NGR234. 965 Feb 93

The activity of the isoenzymes of N-acetyl-beta-D-glucosaminidase (NAG, EC 3.2.1.30) is determined in the serum of insulin-dependent (IDDM) and non-insulin-dependent diabetics (NIDDM) with or without diabetic complications. The increase in total activity of serum NAG in diabetics is proportional to the A form activity (r = 0.976, p < 0.0001). The contribution of the A form activity (65.87 +/- 5.99%) to total NAG activity of IDDM and NIDDM diabetics with and without complications does not change considerably compared to the control group. The contribution of the B form activity depends on the state of metabolic monitoring and diabetic complications. A significantly lower activity of the serum B form was found in IDDM (p < 0.001) and NIDDM diabetics (p < 0.05) compared to the healthy individuals, as well as the higher activity ratios of the A/B forms. A decrease in serum B form is correlated with the occurrence and abundance of the intermediary I forms (r = 0.665). These changes are particularly significant in the individuals with the pronounced microangiopathy.
Biochem Mol Biol Int 1998 Jul
PMID:Changes of isoenzymes of serum N-acetyl-beta-D-glucosaminidase in relation to different types of diabetes. 967 55

A mutant lysozyme where R14 and H15 are deleted together has higher activity and a similar binding ability to an inhibitor, trimer of N-acetylglucosamine ((NAG)3), compared with wild-type lysozyme. Since this has been attributed to intrinsic protein dynamic properties, we investigated the relationship between the activity and the internal motions of proteins. Backbone dynamics of the free and the complex forms with the (NAG)3 have been studied by measurement of the 15N T1 and T2 relaxation rates and NOE determinations at 600 MHz. Analysis of the data using the model-free formalism showed that the generalized order parameters (S2) were almost the same in wild-type and mutant lysozyme in unbound state, indicating that the mutation had little effect on the global internal motions. On the other hand, in the presence of (NAG)3, although some signals located around the active site were broadened or decreased in intensity because of strong perturbation by (NAG)3, there were several residues that showed increased or decreased backbone S2 in the complexed lysozymes. A comparison of the internal motions of the wild-type and mutant complexes showed a number of distinct dynamic differences between them. In particular, many residues located at or near active-site regions (turn 1, strand 2, turn 2 and long loop), displayed greater backbone dynamics reflecting the order parameter in mutant complex relative to mutant free. Furthermore, the Rex values at the loop C-D region, which was considered to be important for enzymatic activity, significantly increased. From these results, it was suggested that variations in the dynamics of these regions may play an important role in the enzyme activity.
J Mol Biol 1999 Mar 12
PMID:Analysis of the relationship between enzyme activity and its internal motion using nuclear magnetic resonance: 15N relaxation studies of wild-type and mutant lysozyme. 1006 15

We previously identified a novel lectin cDNA from the fall webworm [Shin et al. (1998) Insect Biochem. Mol. Biol. 28, 827-837], which encodes two carbohydrate recognition domains (CRD-N and CRD-C) and is up-regulated following bacterial challenge. The lipopolysaccharide (LPS) binding activities of the recombinant CRD-N and CRD-C (rCRD-N and rCRD-C) were investigated by enzyme-linked immunosorbent assay. The LPS binding of rCRD-N and rCRD-C was pH-dependent: at pH below 6.0, they show a higher binding ability to LPS. The binding of the rCRD-N was inhibited by both D-mannose and N-acetyl-D-glucosamine, whereas the binding of the rCRD-C was inhibited only by D-mannose. The binding of both rCRD-N and rCRD-C to Escherichia coli was mainly mediated through the O-specific chain.
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PMID:Two carbohydrate recognition domains of Hyphantria cunea lectin bind to bacterial lipopolysaccharides through O-specific chain. 1066 59

Urtica dioica agglutinin is a small plant lectin that binds chitin. We purified the isolectin VI (UDA-VI) and crystal structures of the isolectin and its complex with tri-N-acetylchitotriose (NAG3) were determined by X-ray analysis. The UDA-VI consists of two domains analogous to hevein and the backbone folding of each domain is maintained by four disulfide bridges. The sequence similarity of the two domains is not high (42 %) but their backbone structures are well superimposed except some loop regions. The chitin binding sites are located on the molecular surface at both ends of the dumbbell-shape molecule. The crystal of the NAG3 complex contains two independent molecules forming a protein-sugar 2:2 complex. One NAG3 molecule is sandwiched between two independent UDA-VI molecules and the other sugar molecule is also sandwiched by one UDA-VI molecule and symmetry-related another one. The sugar binding site of N-terminal domain consists of three subsites accommodating NAG3 while two NAG residues are bound to the C-terminal domain. In each sugar-binding site, three aromatic amino acid residues and one serine residue participate to the NAG3 binding. The sugar rings bound to two subsites are stacked to the side-chain groups of tryptophan or histidine and a tyrosine residue is in face-to-face contact with an acetylamino group, to which the hydroxyl group of a serine residue is hydrogen-bonded. The third subsite of the N-terminal domain binds a NAG moiety with hydrogen bonds. The results suggest that the triad of aromatic amino acid residues is intrinsic in sugar binding of hevein-like domains.
J Mol Biol 2000 Mar 31
PMID:Crystal structures of Urtica dioica agglutinin and its complex with tri-N-acetylchitotriose. 1073 20

A lectin with high hemagglutinating activity, which we have named Dorin M, was identified in the plasma of the soft tick Ornithodoros moubata. The activity of the plasma lectin could be efficiently inhibited by sialic acid, N-acetyl-D-hexosamines and sialoglycoproteins. Dorin M was purified to homogeneity using two different isolation systems: affinity chromatography on a column of bovine submaxillary mucin conjugated to Sepharose 4B with specific elution by N-acetyl-D-glucosamine and chromatography on Blue-Sepharose followed by anion exchange FPLC on a MonoQ column. The purified lectin is a glycoprotein which, in the native state, forms aggregates with molecular mass of about 640 kDa. Non-reducing SDS PAGE revealed that the lectin consists of two noncovalently bound subunits migrating closely around 37 kDa. Dorin M is a glycoprotein, probably modified by N-type glycosylation. After chemical deglycosylation, only one band of about 32 kDa was detected. Dorin M is the first lectin purified from ticks.
Insect Biochem Mol Biol 2000 Mar
PMID:Isolation and characterization of Dorin M, a lectin from plasma of the soft tick Ornithodoros moubata. 1073 87

The present study describes the activity and localisation of three putative lysosomal marker enzymes, acid phosphatase (AP), N-acetyl-beta-D-glucosaminidase (beta-NAG), and beta-galactosidase (beta-Gal), in whole individuals and in distinct parts of the earthworms, Eisenia veneta and Eisenia fetida. Activities of AP and beta-NAG were high in the two species with most of the activity located to the anterior and mid-parts of the worms. The activity of beta-Gal was low in all body regions. We found interspecies difference in the AP activity as E. veneta had significantly higher activity of AP than E. fetida in posterior and mid-parts, as well as in whole individuals. Of the three enzymes tested, AP was the only enzyme located to lysosomes, yielding high latency all over the worms with especially high latency in the coelomic fluids and posterior regions. The lysosomal APs in E. veneta and E. fetida may be utilised as a new biomarker for xenobiotic-induced lysosomal membrane damage in earthworms.
Comp Biochem Physiol B Biochem Mol Biol 2000 Mar
PMID:Activity and localisation of the lysosomal marker enzymes acid phosphatase, N-acetyl-beta-D-glucosaminidase, and beta-galactosidase in the earthworms Eisenia fetida and E. veneta. 1081 77


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