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PubMed1988

Heterogeneity of apical glycoconjugates in kidney collecting ducts: further studies using simultaneous detection of lectin binding sites and immunocytochemical detection of key transport enzymes.

In the search for a functional role for the polarized glycoconjugates of rat collecting duct epithelial cells, the relation between binding of various lectins and expression of cellular transport enzyme profile of the cells was studied. For this purpose, principal and intercalated cells of rat kidney collecting duct were identified by morphological criteria and by their immunocytochemically determined content of (Na+ + K+)-ATPase and carbonic anhydrase (CA II), respectively. Various N-acetylgalactosamine-specific lectins such as those from Helix pomatia and Maclura pomifera revealed heterogeneity among both principal and intercalated cells, whereas alpha-N-acetylgalactosamine-specific lectin from Dolichos biflorus and Vicia villosa bound preferentially to principal cells. Still another lectin from Arachis hypogaea reacted with most collecting duct cells in the cortex and outer medulla, but only with a subpopulation of cells in the inner medulla. Interestingly, some lectins reacted exclusively with the apical aspect of the collecting duct epithelial cells, whereas others revealed both an apical and basolateral distribution of lectin reactive glycoconjugates. The results thus show subtle differences in the glycocalyx structure of principal and intercalated cells and differences in the intracellular polarization of glycoconjugates of these cells. Thus, lectins may be useful tools in the study of the molecular mechanisms which establish and maintain the polarized functions of principal and intercalated cells.

Animals↗
PubMed1990

Antibodies directed against the thiomannose moiety of a glycoconjugate of 2-imino-2-methoxyethyl 1-thio-alpha-D-mannopyranoside and bovine serum albumin.

Anti-thiomannose antibodies were induced in rabbits immunized with a glycoconjugate of 2-imino-2-methoxyethyl 1-thio-alpha-D-mannopyranoside (Man-S) and bovine serum albumin (BSA). Also anti-BSA antibodies directed against the BSA moiety of the glycoconjugate were detected in low concentrations in the immune serum. However, antibodies against the combinatorial epitope of the hapten group and the carrier protein were not detected. The anti-thiomannose and the anti-BSA antibodies were isolated in pure forms by affinity chromatography on Sepharose 4B-bearing thiomannosyl-BSA ligands or BSA ligands. The anti-thiomannose antibodies constituted the major fraction of the antibodies, and these antibodies were isolated in pure form for the first time. The specificity of the thiomannose antibodies was established from data of experiments of periodate oxidation, perpropionic acid oxidation, hapten inhibition, and agar diffusion, Isoelectrofocusing showed that the anti-thiomannose antibody preparation consisted of at least six isomeric proteins, all of which exhibited antibody activity against the glycoconjugate of thiomannose and BSA.

Animals↗
PubMed1996

An improved ELISA for the determination of sialyl Lewis(x) structures on purified glycoconjugates.

The membrane carbohydrate antigen, sialyl Lewis x (sLe(x)), is involved in cellular adhesive interactions in many diseases, such as cancer, inflammation and thrombosis. This antigen is also found on soluble macromolecules, such as serum glycoproteins, but the precise role of soluble sLe(x) in modifying disease processes, or reflecting the pathological changes is still unclear. Although methods were previously reported for the measurement of soluble sLe(x), many of these were not well characterised, measurements were mainly made on mixtures of molecules, and the anti-sLe(x) antibodies were used at concentrations that made the assay expensive. In this study an ELISA has been devised that detects sLe(x) in purified soluble glycoconjugates using the anti-sLe(x) antibody, CSLEX I. Commercially-available haptoglobin (Hp) and synthetic complexes of Lewis antigens with polyacrylamide were used as model substances in developing the procedure. Key steps were washing the antibody/antigen complex with ten times diluted salt solution to prevent dissociation of the complex and the use of bovine serum albumin for blocking non-specific interactions. The assay was shown to be very specific, its precision was in the range 6-12%, and it could detect less than a pmol of sLe(x). It could also distinguish between different densities of sLe(x) on the same amount of glycoconjugate. Determination of sLe(x) in Hp isolated from small groups of healthy individuals, cancer patients, and rheumatoid arthritis sufferers suggested that the antigen expression is increased in disease. This method, which is an improvement on those previously described will be useful for determining sLe(x) in many different types of soluble glycoconjugate, and used in combination with synthetic carbohydrate polyacrylamide complexes, will help to standardize measurements of soluble sLe(x) in the future.

Adult↗
PubMed1990

Histochemical characterization of glycoconjugates in the epithelium of the extrapulmonary airways of several vertebrates.

The glycoconjugates of the extrapulmonary airways of 11 tetrapode vertebrates have been characterized by means of both conventional and lectin histochemistry. Abundant sialosulphomucins were detected in the secretory cells and periciliary layer of turtles, snakes, birds and mammals while only sialomucins were observed in amphibians. Neutral and traces of acidic mucins were detected in the secretory cells of lizards. The secretory cells of the amphibian airways were reactive to Con-A, DBA and WGA. No alpha-L-fucose residues reactive with UEA-I or LTA were detected in amphibians. The goblet cells of the turtles were stained by DBA, SBA and WGA. Secretory cells of snakes and lizards reacted with Con-A and WGA. The mucous goblet cells of the birds were reactive to Con-A, LTA and WGA. In the chicken, they also showed affinity for PNA and SBA. The ciliated cells of the avian species studied were stained by Con-A and WGA. Mammalian goblet cells were reactive to Con-A, UEA-I and WGA. In the rat, affinity for DBA and SBA was also observed. The present results reveal the existence of marked differences in the sugar residues of the glycoconjugates of the extrapulmonary airways of tetrapode vertebrates. Only sialic acid residues appear to be constant constituents of the glycoconjugates of the airways of all species studied.

Animals↗
PubMed1996

Oligosaccharides and glycoconjugates in human milk: their role in host defense.

Human milk contains an extremely high concentration of complex carbohydrates, especially oligosaccharides, the third most abundant solid constituent of human milk. The value of human milk nutrients to infants is now widely recognized, and a role for the secretory antibodies of human milk in the defense of the infant is generally accepted. However, a function for nonimmunoglobulin milk protective factors, many of them non-nutrients, in providing for the defense of the nursling is only now beginning to be appreciated. Prominent among postulated defense agents are the milk oligosaccharides and glycoconjugates. Their complex carbohydrate structures are thought to be assembled by the same enzymes, the glycosyltransferases, that synthesize the cell surface glycoconjugates often used as receptors by pathogens. Some milk oligosaccharides and glycoconjugates may protect the nursing infant by acting as receptor homologs, inhibiting the binding of enteropathogens to their host receptors. Ongoing research is linking specific carbohydrate structures with protection against specific pathogens. Current information regarding the composition, protective activities, and protective mechanisms of the milk glycolipids, glycoproteins, mucins, glycosaminoglycans, and oligosaccharides is reviewed.

Female↗
PubMed1990

Characterization of glycoconjugates found in granular cell tumors, with special reference to keratan sulfate.

Nine granular cell tumors (GCTs) were studied using the immunoperoxidase technique with a mouse monoclonal antibody to keratan sulfate and a polyclonal antibody to S-100 protein. Various lectins and basic dye stains were also employed. Schwannomas benign and a malignant, a neurofibroma, a leiomyoma, two examples of nevus pigmentosus and a congenital epulis were similarly examined to compare the histochemical reactivities. Tumor cells of all the GCTs reacted intensely with the antibodies to keratan sulfate and S-100 protein. Peripheral nerve bundles and other neurogenic tumors showed stained for S-100 protein but not for keratan sulfate. Basic dye stain indicated the presence of sulfated glycoconjugates in GCTs. Lectin stains demonstrated that GCTs were rich in glycoconjugates but the reactivity patterns for 14 lectins differed between GCTs and normal tissue components. None of the lectins used in this study was specific for GCTs. These results indicate that GCTs contain abundant glycoconjugates and that the monoclonal antibody to keratan sulfate may be an immunohistochemical marker for GCT.

Adolescent↗
PubMed2005

Morphology and glycoconjugate histochemistry of the eccrine glands in the snout skin of the North American raccoon (Procyon lotor).

The eccrine nasolabial glands were found in the hypodermis of the nasal plane in the North American raccoon (Procyon lotor). In addition to light and electron microscopic observations, the distribution and selectivity of complex glycoconjugates in the eccrine tubular glands of the raccoon snout skin were studied using various histochemical methods, particularly lectin staining. The secretory epithelium and the luminal secretions exhibited high amounts of glycoconjugates with various saccharide residues (alpha-D: -mannose, alpha-L: -fucose, beta-D: -galactose, beta-N-acetyl-D: -glucosamine, sialic acid). The excretory duct cells also showed positive reactions with most of the histochemical methods applied. The results are discussed with regard to possible functions of the glandular secretions. The complex glycoconjugates that are produced by the eccrine nasolabial glands may be related to moistening of the skin surface as well as protecting the epidermis against physical damage or microbial contamination. This is the first report on the glands in the snout skin of carnivores.

Animals↗
PubMed1997

Analysis of the distribution of glycoconjugates in the digestive gland of the bivalve mollusc Mytilus galloprovincialis by conventional and lectin histochemistry.

We examined the distribution and pattern of reactivity of a panel of 16 lectins in the digestive gland of the bivalve mollusc Mytilus galloprovincialis at the light-microscopic level. Various chemical treatments were applied in combination with lectins to differentiate between N- and O-linked oligosaccharides. Several control reactions were carried out, including replacement of lectins by buffer and incubation with their specific competitive inhibitors. Some lectins reacted selectively with particular cell types, thus revealing a cell-specific glycoconjugate distribution pattern which is possibly related to the metabolic role of each cell type in the digestive gland. Glycoconjugates containing glucosamine, mannose, and sulfated galactose were associated with the endolysosomal system of digestive cells. These glycoconjugates were also found in small vesicles randomly distributed in the cytoplasm of adipogranular cells in the connective tissue. However galactosamine residues appeared to be associated mainly with basophilic cells. Fucose residues did not exhibit a cell-specific distribution and appeared in small amounts homogeneously distributed throughout the digestive gland tissue. Conventional histochemical reactions for carbohydrate detection revealed moderate amounts of periodic-acid-Schiff-positive, neutral carbohydrates widely distributed in digestive and connective tissues. Among the acid carbohydrates, most cell types contained complex sulfated carbohydrates, but not carboxylated ones; this agreed well with the complete lack of sialic acid residues in all cell types studied, as observed by lectin histochemistry.

Animals↗
PubMed2005

Characterization of corpora amylacea glycoconjugates in normal and hyperplastic glands of human prostate.

It has been shown that there are sugars in corpora amylacea, but little attention has been focused on the expression of glycoconjugates in corpora amylacea of normal and hyperplastic prostatic glands. The present study characterizes and compares the expression of glycoconjugates in corpora amylacea of normal and hyperplastic prostatic glands of elderly men by using alcian blue (AB) stain and lectin histochemistry. Corpora amylacea were larger and more numerous in hyperplastic glands compared to normal glands. The stain with AB revealed the presence of sulfated and carboxyl components in corpora amylacea. In hyperplastic prostatic glands the sulfur and acid contents of corpora amylacea were increased. Lectin affinities of corpora amylacea from normal prostatic glands demonstrated the presence of fucose, mannose, sialic acid, N-acetyl galactosamine and N-acetyl glucosamine residues. In the hyperplastic glands the lectin binding pattern of corpora amylacea was qualitatively similar to normal glands, but an increase in GalNAc, sialic acid, mannose and fucose residues was observed. Normal prostatic glands showed a weak to moderate content of mannose residues, and in contrast a strong GNA and Con-A staining was observed in hyperplastic glands. MAA and SNA affinities indicated that the content of sialic acid residues was higher in hyperplastic glands compared with normal prostatic glands. Also NAcGal residues were increased in hyperplastic glands. Luminal secretion, secretory cells and apical border of epithelium showed a similar although more intense Lectin-binding pattern as compared with corpora amylacea both in normal and hyperplastic prostatic glands. Lectin histochemistry shows that the glycoconjugates expressed in the glandular epithelium are similar to those found in corpora amylacea both in normal and hyperplastic glands. In addition, in hyperplastic glands, where the corpora amylacea are higher in size and more numerous, the reaction to lectins is more intense especially with mannose and sialic acid residues. The results suggest that corpora amylacea are originated at least in part from prostatic secretion.

Glycoconjugates↗
PubMed2005

Ultrastructural localization of alpha-galactose-containing glycoconjugates in the rat vomeronasal organ.

Binding sites of Griffonia simplicifolia I-B4 isolectin (GS-I-B4), which recognizes terminal alpha-galactose residues of glycoconjugates, were examined in the juxtaluminal region of the rat vomeronasal sensory epithelium and its associated glands of the vomeronasal organ, using a lectin cytochemical technique. Lowicryl K4M-embedded ultra-thin sections, which were treated successively with biotinylated GS-I-B4 and streptavidin-conjugated 10 nm colloidal gold particles, were observed under a transmission electron microscope. Colloidal gold particles, which reflect the presence of terminal alpha-galactose-containing glycoconjugates, were present in vomeronasal receptor neurons in the sensory epithelium and secretory granules of acinar cells of associated glands of the epithelium. Quantitative analysis demonstrated that the density of colloidal gold particles associated with sensory cell microvilli that projected from dendritic endings of vomeronasal neurons was considerably higher than that of microvilli that projected from neighboring sustentacular cells. The same was true for the apical cytoplasms of these cells just below the microvilli. These results suggest that of the sensory microvilli and dendritic endings contained a much larger amount of the alpha-galactose-containing glycoconjugates, compared with those in sustentacular microvilli. Further, biochemical analyses demonstrated several vomeronasal organ-specific glycoproteins with terminal alpha-galactose.

Animals↗
PubMed1988

Biocytin hydrazide--a selective label for sialic acids, galactose, and other sugars in glycoconjugates using avidin-biotin technology.

Biocytin hydrazide (BCHZ), a new, water-soluble, long-chained, biotin-containing hydrazide, was synthesized and used for the selective nonradioactive detection of glycoconjugates. Procedures were developed for labeling glycoconjugates on blots. The method involves either chemical (periodate-induced) or enzymatic (via galactose oxidase) oxidation of glycoconjugates, the resultant aldehyde groups are then labeled with biocytin hydrazide, followed by interaction with an avidin-based enzyme probe. Since the biotin-containing reagent is a relatively small, charged molecule, the primary labeling step may be carried out on intact cells and on membrane preparations as well as on blotted samples. On blots, the labeling pattern was similar for both periodate- and galactose oxidase-induced biotinylation procedures. In contrast, periodate-induced labeling of either erythrocyte membranes or cells (prior to blotting) produced an altered labeling pattern. Combined enzyme-induced biotinylation of membranes or cells resulted in a pattern similar to that observed for the direct staining of blots. Using galactose oxidase on human erythrocyte membranes, the procedure was sensitive enough to selectively label the Band 3 lactosaminoglycoprotein.

Avidin↗
PubMed1988

Analysis of cell surface glycoconjugates in fibroblasts from patients with cystic fibrosis.

Although the basic biochemical defect in cystic fibrosis (CF) is unknown, previous studies have indicated that errors in protein glycosylation may be involved in the pathogenesis of the disease. Utilizing human skin fibroblasts, the present study was designed to quantitatively analyze glycosylation of cell surface glycoconjugates in CF and normal cells. Cell surface glycoconjugates were analyzed using 125I-concanavilin A (Con A), 125I-WGA, and Con A-ferritin conjugates. Under our binding conditions, Con A was used as a probe for mannose residues and WGA was used as a probe for N-acetylglucosamine residues. Saturable binding of both probes was observed and appropriate sugar controls confirmed the specificity of each lectin. When compared on a DNA basis, iodinated lectin binding studies indicated that no consistent differences existed between CF and normal strains of human skin fibroblasts. Ultrastructural quantitative morphometric analysis of Con A-ferritin conjugate binding indicated that neither proteolysis of cell surface glycoconjugates or internalization of lectin probes was occurring at saturable binding concentrations. In summary, our results indicated that no consistent differences in cell surface mannose and N-acetylglucosamine residues could be detected between the normal and CF strains of human skin fibroblasts used in these studies.

Acetylglucosamine↗
PubMed1991

Pericellular glycoconjugates of cultured fibroblasts from control and cystic fibrosis patients.

1. Labeled glycoconjugates released by trypsin from cell surfaces of control and cystic fibrosis (CF) skin fibroblasts were purified and fractionated by column chromatography on Sephadex G-50 and Concanavalin A Sepharose. Based on chemical analysis and specific enzymatic digestions: (1) Glycoconjugates were characterized as O-linked glycopeptides consisting predominantly of glycosaminoglycan type and N-linked glycopeptides with glycans of complex type. Their relative proportions were similar between the two groups. (2) The N-linked glycopeptides exhibited an increased molar ratio of fucose to galactose in CF fibroblasts. (3) When pericellular glycoconjugates were metabolically labeled with [14C]glucosamine and [3H]fucose, incorporation and degradation kinetics were similar between the two groups.

Carbohydrates↗
PubMed1994

CGRP induces [Ca2+]i rise and glycoconjugate secretion in feline tracheal submucosal gland.

Submucosal glands were isolated from feline trachea. The intracellular Ca2+ concentration ([Ca2+]i) of the acinar cells of isolated glands was measured using the fluorescent dye Fura-2. Calcitonin gene-related peptide (CGRP) at 10(-8) to 10(-5) M produced a significant and sustained rise in the [Ca2+]i of isolated glands, reaching a maximal response of 127% of the prior baseline level but did not alter the intracellular adenosine 3', 5'-cyclic monophosphate ([cAMP]i). In a Ca(2+)-free solution, CGRP produced no significant alteration in [Ca++]i. Glycoconjugate secretion from isolated glands was stimulated by CGRP in a dose dependent fashion, reaching a maximal response of 167% of control at 10(-6) M but was without effect in tracheal explants. Further, CGRP did not produce any significant increase in glycoconjugate secretion in the Ca(2+)-free medium. These findings indicate that CGRP stimulates glycoconjugate secretion from airway submucosal glands by inducing Ca2+ influx from the extracellular solution.

Animals↗
PubMed1993

Galactofuranose-containing glycoconjugates of epimastigote and trypomastigote forms of Trypanosoma cruzi.

Antiserum to LPPG, a lipopeptidophosphoglycan originally described on the surface of Trypanosoma cruzi epimastigotes of the Y strain, and antibodies to furanoic galactose (galf) were obtained in rabbits. A micromethod for the extraction and purification of LPPG from a limited amount of parasites is described. Analysis by Western blots of the purified glycoconjugate probed with both antisera confirmed the presence of galf-containing LPPG-like molecules in 10 different strains and clones of T. cruzi. An analogous approach indicated that trypomastigotes also contain LPPG-like components. Quantitation experiments allowed to calculate an average value of 1.0 x 10(7) LPPG molecules per epimastigote cell and 0.16 x 10(7) LPPG-like molecules per trypomastigote cell. Immunoelectron microscopy has shown a homogenous distribution of LPPG on the surface of epimastigotes. The trypomastigote population, however, is highly heterogenous with no more than 15% of the parasites being labeled by the anti-LPPG serum. Intense labeling has also been found in vesicles inside the epimastigote and trypomastigote forms. The distribution of galf epitopes among glycoconjugates of epimastigotes and trypomastigotes was further investigated. It was shown that galf units in epimastigotes are bound to low molecular mass compounds which co-migrate with LPPG whereas in trypomastigotes they have been found in both low molecular mass LPPG-like molecules and glycoproteins of 80-90 kDa. Direct chemical evidence for the presence of galf residues in the N-linked oligosaccharide chains of these surface glycoproteins has been obtained. Finally, the natural antigenicity of LPPG and galf in chronic Chagas' disease was investigated. It was found that all chronic chagasic sera investigated recognize this glycoconjugate and that an important part of such recognition can be attributed to galf residues. Furthermore, no correlation among reactivity to LPPG, strain zymodeme and clinical forms of the disease was found.

Animals↗
PubMed2005

Effect of the carbohydrate side-chain on the conformation of a glycoconjugate polystyrene in aqueous solution.

An oligomaltose-carrying polystyrene "glycoconjugate polystyrene" was synthesized by the homopolymerization of 4-vinylbenzylamine oligomaltonic amides, derived from maltose, maltotriose, maltopentaose, and maltoheptaose. The resultant amphiphilic glycoconjugate polystyrenes were dissolved in 0.1 M aqueous urea, and their structures characterized by small-angle X-ray scattering and molecular modeling. "Glycoconjugate polystyrene" was found to behave as a "molecular bottle brush", composed of a large pseudo-helical polystyrene backbone and carbohydrate brushes. A large pseudo-helical polystyrene backbone is formed by a random sequence of TT, TG, and/or TTGG. The results indicate that the cross-section of a backbone chain with smaller oligosaccharide side-chains is obliged to expand more than that with longer side-chains. Even with rigid hydrophilic pendant oligosaccharide chains, the larger pseudo-helix of the main chain could orient the side-chains so as to envelop the hydrophobic backbone in aqueous solution. Thus the conformation of the main chain is determined not only by the chemical nature of an oligosaccharide chain but also by its length.

Computer Simulation↗
PubMed2005

Influence of the endosymbiont of Blastocrithidia culicis and Crithidia deanei on the glycoconjugate expression and on Aedes aegypti interaction.

Blastocrithidia culicis and Crithidia deanei are trypanosomatid protozoa of insects that normally contain intracellular symbiotic bacteria. The protozoa can be rid of their endosymbionts by antibiotics, producing a cured cell line. Here, we analyzed the glycoconjugate profiles of endosymbiont-harboring and cured strains of B. culicis and C. deanei by Western blotting and flow cytometry analyses using lectins that recognize specifically sialic acid and mannose-like residues. The absence of the endosymbiont increased the intensity of the lectins binding on both trypanosomatids. In addition, wild and cured strain-specific glycoconjugate bands were identified. The role of the surface saccharide residues on the interaction with explanted guts from Aedes aegypti gut was assessed. The aposymbiotic strains of B. culicis and C. deanei presented interaction rates 3.3- and 2.3-fold lower with the insect gut, respectively, when compared with the endosymbiont-bearing strains. The interaction rate of sialidase-treated cells of the wild and cured strains of B. culicis and C. deanei was reduced in at least 90% in relation to the control. The interaction of B. culicis (wild strain) with explanted guts was inhibited in the presence of mucin (56%), fetuin (62%), sialyllactose (64%) and alpha-methyl-D-mannoside (80%), while in C. deanei (wild strain) the inhibition was 53%, 56%, 79% and 34%, respectively. Collectively, our results suggest a possible involvement of sialomolecules and mannose-rich glycoconjugates in the interaction between insect trypanosomatids and the invertebrate host.

Aedes↗
PubMed1992

Glycoconjugate composition of mammalian parotid glands elucidated in situ by lectins and glycosidases.

Sugar specific lectins (PNA, RCA I, LPA, SBA, DBA, GSA IB4, GSA II, WGA, LTA, UEA I, Con A, LCA) with and without prior selective glycosidase digestion (sialidase, alpha-fucosidase, alpha-mannosidase, beta-N-acetylglucosaminidase, alpha- and beta-galactosidase, beta-glucosidase) were used in order to investigate the distribution of native accessible carbohydrates and obtain information dealing with the composition of terminal disaccharides within glycoconjugates present in acinar compartments and ductal segments of mammalian (mouse, rat, hare, and rabbit) parotid glands. Glycoconjugates containing variable amounts of mannose, glucose, N-acetylgalactosamine and N-acetylglucosamine were present in the parotid glands of all species. However, these carbohydrate chains exhibited a different composition of terminal sequences within each type of gland. For example, sialylated components having the terminal dimers sialic acid-galactose and sialic acid-N-acetylgalactosamine were found in all acinar cells, whereas fucoglycoconjugates with terminal disaccharide fucose-galactose were localized in the rat striated ducts and hare acinar cells. The terminal sequence alpha-galactose-beta-galactose was demonstrated in the mouse acinar cells. Finally, glycoconjugates characterized by the terminal dimer beta-galactose-N-acetylgalactosamine were demonstrated in the mouse acinar and ductal cells and the rat ductal ones. Thus, present findings outlined and further confirmed the possibility to elucidate the oligosaccharide structure in situ using lectin histochemistry combined with enzymatic degradation.

Animals↗