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

Mannan-binding proteins found in the liver and serum of several vertebrate species are supposed to play an important role in the intracellular transport of glycoproteins, as well as in several protective reactions including complement activation and elimination of various pathogens. To study these protective functions at molecular level it is necessary to understand the fine oligosaccharide specificity and mutual relation among various forms of these soluble lectins. We have isolated mannan-binding protein as peripheral membrane proteins of porcine lymphocytes. This lectin was purified to homogeneity and shown to possess many properties in common with the well studied rat liver proteins (mol. mass, subunit composition and general organization of the molecule). Binding studies performed with three series of defined oligosaccharides (high mannose, hybrid type, and complex) on native lectin molecules as well as isolated carbohydrate-binding domains revealed distinctive features of this mannan-binding protein, including its impaired ability to bind the oligosaccharide ligand after reduction and decyclization at core N-acetyl-D-glucosamine 1.
Mol Immunol 1992 Dec
PMID:Localization and characterization of the carbohydrate-binding site of the porcine lymphocyte mannan-binding protein. 145 63

As part of a strategy to determine the precise role of pea (Pisum sativum) lectin, Psl, in nodulation of pea by Rhizobium leguminosarum, mutations were introduced into the genetic determinant for pea lectin by site-directed mutagenesis using PCR. Introduction of a specific mutation, N125D, into a central area of the sugar-binding site resulted in complete loss of binding of Psl to dextran as well as of mannose/glucose-sensitive haemagglutination activity. As a control, substitution of an adjacent residue, A126V, did not have any detectable influence on sugar-binding activity. Both mutants appeared to represent normal Psl dimers with a molecular mass of about 55 kDa, in which binding of Ca2+ and Mn2+ ions was not affected. These results demonstrate that the NHD2 group of Asn125 is essential in sugar binding by Psl. To our knowledge, Psl N125D is the first mutant legume lectin which is unable to bind sugar residues. This mutant could be useful in the identification of the potential role of the lectin in the recognition of homologous symbionts.
Plant Mol Biol 1992 Dec
PMID:Mutational analysis of pea lectin. Substitution of Asn125 for Asp in the monosaccharide-binding site eliminates mannose/glucose-binding activity. 146 40

Twelve plant lectins from the Papilionoideae subfamily were selected to represent a range of carbohydrate specificities, and their sequences were aligned. Two variability indices were applied to the aligned sequences and the results were analysed using the three-dimensional structures of concanavalin A and the pea lectin. The areas of greatest variability were located in the carbohydrate-binding site region, forming a perimeter around a well-conserved core. These residues are inferred to be specificity determining, in the manner of antibodies, and the most variable position corresponded to Tyr100 in concanavalin A, a known ligand contact residue. In addition to the five peptide loops known to form the binding site from crystallographic studies, a sixth segment with variable residues was located in the binding-site region, and this may contribute to oligosaccharide specificity. In their overall composition, the lectin sites resemble those of the sugar-transport proteins rather than antibodies. The prospects for modelling lectin binding sites by the methods used for antibodies were also assessed.
J Mol Biol 1992 Dec 05
PMID:Analysis of sequence variation among legume lectins. A ring of hypervariable residues forms the perimeter of the carbohydrate-binding site. 146 24

We describe studies of a new model cell adhesion system involving liposomes bearing lectins and the glycosphingolipid, asialomonosialoganglioside (asialoGM1). The model provides a simple analysis of experimental data to elucidate the mechanism of heterophilic cell-cell adhesion mediated by multiple protein-carbohydrate interactions. Phospholipid vesicles bearing the fatty acid conjugate of a glycoprotein lectin from Ricinus communis (RCAI vesicle) are shown to react with vesicles bearing the fatty acid conjugate of Concanavalin A (Con A) and asialoGM1 (Con A vesicle). The kinetics of aggregation and monosaccharide-induced disaggregation of the two types of vesicles were followed by monitoring the time-dependent change in turbidity. Depending on the surface density of the asialoGM1, 40-60% of the resulting precipitin complex was dissociable only in the presence of both RCAI-specific galactose and Con A-specific alpha-methyl-D-mannoside. Results indicate simultaneous participation of both the saccharide-binding domain and carbohydrate sequence of RCAI, a model cell adhesion molecule, to stabilize the encounter complex by two types of interactions. These findings support the possibility of stable cell-cell adhesion in vivo occurring via interactions between cell adhesion molecules on apposing cell-surface membranes.
J Mol Recognit 1992 Jun
PMID:Complex carbohydrate-lectin interaction at the interface: a model for cellular adhesion. II. Reactivity of both the oligosaccharide chain and sugar-binding domain of a glycoprotein lectin. 147 82

The marine blood clam species Anadara granosa (L) belong to arcidae, a family with some extraordinary haematological features. The plasma of this species exhibited strong haemagglutinating activities, from which a galactosyl binding lectin, Anadarin P, was purified in a single step affinity chromatography using Sepharose 4B-asialofetuin as an affinity matrix. The purified lectin, eluted with lactose, was found to be homogeneous by alkaline polyacrylamide disc gels, gel-filtration and isoelectric focusing. Native M(r) of the lectin was 130,000 having a PI value of 6.82 and was composed of two subunits of M(r) 17,000 and M(r) 16,000 which were noncovalently bound. The lectin was remarkably thermostable; the agglutinating titre remained unchanged over a wide range of pH (from 5 to 10) but increased with neuraminidase treated rabbit erythrocytes. Anadarin P combining site has been proposed to be small pocket-like structure which recognised only C-3 and C-4 hydroxyl groups of D-galactose. Presence of bulky groups at C-2 and C-6 exert strong steric hindrance as L-arabinose, 2-deoxy-D-galactose and D-xylose are better inhibitors than D-galactose. The lectin fails to differentiate methyl substituted galactosides as both alpha- and beta- methyl galactosides are equally active; but in case of substituted phenyl glycosides, the lectin shows different affinity towards alpha and beta anomers. The avidity of the lectin to bind the aromatic aglycons of galactosides suggests the presence of a hydrophobic region in the combining site. Interactions with some disaccharides indicate the presence of an extended area near the monosaccharide binding site.
Mol Cell Biochem 1992 Nov 04
PMID:A novel galactosyl-binding lectin from the plasma of the blood clam, Anadara granosa (L) and a study of its combining site. 148 Jan 60

A sialic acid binding lectin, AchatininH was purified from the hemolymph of Achatina fulica snail. To identify the site of synthesis of AchatininH, in vitro incubation studies in presence of labelled amino acid precursor were performed. Different organs from the snail were sliced and incubated in methionine-deficient Eagle's minimum essential medium containing [35S]-methionine at 25 degrees C for 5 h. After termination of incubation, tissues were homogenized, centrifuged and the de novo synthesized protein was immunoprecipitated with specific AchatininH antibody, followed by protein-A. The precipitated antigen-antibody complex was analysed by SDS-PAGE. Data obtained from native gel electrophoresis and SDS-PAGE radioautographic analysis indicates that AchatininH is synthesized in the albumen gland.
Mol Cell Biochem 1992 Nov 18
PMID:Albumen gland of the snail Achatina fulica is the site for synthesis of AchatininH, a sialic acid binding lectin. 148 46

The present study describes the phenomenon of calciphylaxis, rapid calcification due to treatment with sensitizer dihydrotachysterol (DHT) and challenging agent 5-hydroxytryptamine (5-HT) in the rat submandibular gland (SMG) in terms of light and electron microscopy, and histochemistry. For biophysical analysis of the calcified bodies, X-ray microanalysis (XMA) and X-ray powdered diffraction methods were used. The calcified lesions in the salivary glands were histologically divided into 3 types: type 1, calcification of basal membranes in duct-like structures; type 2, granular calcified materials with remarkable necrotic changes in cell, containing 3 kinds of small vesicular structures observed in electron microscopy; and type 3, von Kossa's positive structures containing needle-like crystalline and electron-dense amorphous materials. Con A and UEA-1 lectin staining reactions were strong in the type 1 and 2 lesions. These findings suggest that the calcification matrix may contain mannose, fucose and glucose. The X-ray microanalysis of calcified materials revealed the magnesium whitelockite pattern, the type 3 displayed high quantities of Ca, P, and Mg ions comparing with the type 1 and 2, and the X-ray diffraction showed the hydroxyapatite pattern. We suggest that the above changes may be categorized as dystrophic calcification due to necrotic alterations brought about by the hypercalcaemic condition.
Cell Mol Biol 1992 Jul
PMID:Experimental calcification in rat submandibular gland. 149 41

We report the cloning and characterization of two lectin genes from Medicago truncatula, designated Mtlec1 and Mtlec2. The two genes show a high degree of homology and apparently belong to a small multigene family. Mtlec1 appears to encode a functional lectin with 277 amino acids, whereas Mtlec2 is probably non-functional, since a frameshift mutation (insertion of two nucleotides) leads to premature translation termination after only 98 amino acids. The deduced amino acid sequence of the polypeptide MtLEC1 suggests that this lectin is a metalloprotein with Glc/Man specificity.
Plant Mol Biol 1992 Sep
PMID:Lectin genes from the legume Medicago truncatula. 151 Nov 26

A 33 bp double-stranded oligonucleotide homologous to two AT-rich sequences located upstream (-907 to -889 and -843 to -826) to the start of transcription of heat shock gene Gmhsp17.5E of soybean stimulated transcription when placed 5' to a truncated (-140) maize Adh1 promoter. The chimeric promoter was assayed in vivo utilizing anaerobically stressed sunflower tumors transformed by a pTi-based vector of Agrobacterium tumefaciens. Nuclear proteins extracted from soybean plumules were shown to bind double-stranded oligonucleotides homologous to AT-rich sequences in the 5' flanking regions of soybean beta-conglycinin, lectin, leghemoglobin and heat shock genes. These proteins were also shown to bind AT-rich probes homologous to homeobox protein binding sites from the Antennapedia and engrailed/fushi tarazu genes of Drosophila. Binding activity specific for AT-rich sequences showed a wide distribution among various plant organs and species. Preliminary characterization indicated that two sets of nuclear proteins from soybean bind AT-rich DNA sequences: a diverse high-molecular-weight (ca. 46-69 kDa) group, and a low-molecular-weight (23 and 32 kDa) group of proteins. The latter meets the operational criteria for high-mobility group proteins (HMGs).
Plant Mol Biol 1992 Sep
PMID:AT-rich promoter elements of soybean heat shock gene Gmhsp17.5E bind two distinct sets of nuclear proteins in vitro. 151 Nov 43

The use of fluorescein-conjugated Pisum sativum agglutinin (FITC-PSA) was evaluated for its ability to distinguish acrosome-intact from acrosome-damaged stallion spermatozoa. Incubation of fresh (acrosome-intact) and frozen-thawed (acrosome-damaged) spermatozoa with FITC-PSA resulted in acrosome-intact spermatozoa that exhibited no fluorescence, while acrosome-damaged spermatozoa exhibited fluorescent staining over the rostral portion of the head and equatorial segment. Experiments using mixtures of various ratios of acrosome-intact and acrosome-damaged spermatozoa determined the precision (intrasample coefficient of variation), and linearity (increased percentage of spermatozoa with PSA binding, with increased percentage of frozen-thawed spermatozoa in a sample) of FITC-PSA binding. The binding of FITC-PSA increased in samples as the portion of frozen-thawed (acrosome-damaged) to fresh (acrosome-intact) spermatozoa increased. A positive correlation existed (r = 0.98, P less than 0.05) between the percentage of FITC-PSA bound sperm and the proportion of damaged spermatozoa added to a sample. Location of PSA lectin binding on acrosome-damaged spermatozoa, determined by electron microscopy using gold-conjugated PSA, was to components of the outer acrosomal membrane and acrosomal matrix. These results demonstrate that FITC-PSA binding may be useful in determining acrosomal integrity of fresh and frozen-thawed stallion spermatozoa.
Mol Reprod Dev 1992 May
PMID:Assessment of Pisum sativum agglutinin in identifying acrosomal damage in stallion spermatozoa. 151 46


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