Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0267964 (PAA)
 2,561 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A lectin was isolated from the fruiting bodies of Pholiota aurivella by preparative PAGE and named PAA (Pholiota aurivella agglutinin). PAA was a polymeric protein of more than several hundred kDa consisting of 18-kDa subunits. The amino acids were sequenced from the N-terminus of the lectin; they were YSVTTPNSVKGGTNQG. PAA agglutinated human erythrocytes regardless of blood type equally and Pronase treatment of erythrocytes increased the sensitivity to agglutination by the lectin. In a hemaggluting inhibition assay, none of the mono-and oligosaccharides used affected agglutination by the lectin. Among glycoproteins, asialofetuin was the best inhibitor. This is first isolated and characterized lectin from the family Strophariaceae.
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PMID:A lectin from the mushroom Pholiota aurivella. 136 55

A panel of 14 lectins was used to investigate the expression of saccharides by cerebral microvessels (MBV) in ageing, Alzheimer's disease (AD) and Down's syndrome (DS). Broad increases in lectin binding with age may reflect changes in amount and diversity of glycoproteins due to the thickening of the basement membrane (BM) common in older persons. In AD, and in persons over 50 years of age with DS, binding of e-PHA, 1-PHA and PAA was increased beyond that of age alone, as was that of UEA-I and BSA-1B4 in AD, but not in DS. Persons under 50 years of age with DS showed no changes inappropriate to their age. These specific increases in AD and DS may reflect selective disease-related changes in BM and could indicate an impaired blood-brain barrier (bbb) function or integrity. However, because they occur (in DS) after the deposition of amyloid (A4) protein and onset of neurofibrillary degeneration, it is unlikely they induce plaque and tangle formation. Such changes in MBV could stem from the loss of neurones from locus caeruleus, raphe and nucleus basalis (which are thought to innervate MBV and exert control over blood flow and permeability) that occurs in DS after 50 years of age.
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PMID:Lectin histochemistry of cerebral microvessels in ageing, Alzheimer's disease and Down's syndrome. 153 63

Nonspecific T cell factors produced by lectin-activated human peripheral blood lymphocytes (PBL) were used to restore the T-dependent B cell response to trinitrophenyl-polyacrylamide (TNP-PAA). Preincubation experiments with the particulate antigen TNP-PAA and/or a soluble TNP-protein conjugate show that a first specific signal provided by the antigen and nonspecific lymphokines sequentially acts on B cells. By gel filtration the T cell-replacing factor (TRF) activity is present in the 30-15-kDa fraction of T cell supernatants and is associated to interleukin 2 (IL2). However, absorption of IL2 does not abolish the TRF activity. Moreover, chromatofocusing of this 30-15-kDa material allows the obtaining of an IL2-free fraction containing a differentiation factor (with an isoelectric point of 5.7 +/- 0.2). The ability of this fraction to restore the anti-TNP response is manifest in the presence of a 50-kDa B cell growth factor. This latter, prepared by a combination of absorption on concanavalin A-Sepharose and gel filtration, was IL2 free and unable to support the anti-TNP response. We thus directly demonstrate that in the absence of IL2 three separate signals (the antigen, T cell-derived growth and differentiation factors) are involved in human-specific B cell response.
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PMID:Differentiation factors for human specific B cell response. 348 60

Considering that nitric oxide (NO) may be involved in anti-tumoral and anti-parasite lectin effects, in this report we investigated whether lectin induces NO production. Lectins from Canavalia brasiliensis, Dioclea grandiflora, Pisum arvense (PAA), and concanavalin A induced murine peritoneal cells to produce NO in vitro. PAA induced similar levels to that obtained with lipopolysaccharide plus interferon-gamma. NO production by adherent cells was significantly lower than that of unfractionated cells, suggesting a combination of lectin stimuli directly on macrophages and via lymphocyte stimulation. Ex vivo experiments showed that cells stimulated in vivo could maintain NO production in vitro without further stimuli. NO synthesis blockage in vivo can significantly increase cell numbers in draining lymph nodes after lectin injection compared to unblocked controls, suggesting an in vivo association of lectin stimuli and NO production. Taken together these data show that lectins can induce NO production both in vitro and in vivo.
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PMID:Lectin-induced nitric oxide production. 1035 85

Fluorescein labeled carbohydrate (Glyc) probes were synthesized as analytical tools for the study of cellular lectins, i.e. SiaLe(x)-PAA-flu, Sia2-PAA-flu, GlcNAc2-PAA-flu, LacNAc-PAA-flu and a number of similar ones, with PAA a soluble polyacrylamide carrier. The binding of SiaLe(x)-PAA-flu was assessed using CHO cells transfected with E-selectin, and the binding of Sia2-PAA-flu was assessed by COS cells transfected with siglec-9. In flow cytometry assays, the fluorescein probes demonstrated a specific binding to the lectin-transfected cells that was inhibited by unlabeled carbohydrate ligands. The intense binding of SiaLe(x)-PAA-3H to the E-selectin transfected cells and the lack of binding to both native and permeabilized control cells lead to the conclusion that the polyacrylamide carrier itself and the spacer arm connecting the carbohydrate moiety with PAA did not contribute anymore to the binding. Tumors were obtained from nude mice by injection of CHO E-selectin or mock transfected cells. The fluorescent SiaLe(x)-PAA-flu probe could bind to the tumor sections from E-selectin positive CHO cells, but not from the control ones. Thus, these probes can be used to reveal specifically the carbohydrate binding sites on cells in culture as well as cells in tissue sections. The use of the confocal spectral imaging technique with Glyc-PAA-flu probes offered the unique possibility to detect lectins in different cells, even when the level of lectin expression was rather low. The confocal mode of spectrum recording provided an analysis of the probe localization with 3D submicron resolution. The spectral analysis (as a constituent part of the confocal spectral imaging technique) enabled interfering signals of the probe and intrinsic cellular fluorescence to be accurately separated, the distribution of the probe to be revealed and its local concentration to be measured.
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PMID:Fluorescent carbohydrate probes for cell lectins. 1160 44

A specific apoptotic glycosylation pattern may play an assistant or even a causative role in phagocytosis of apoptotic bodies. To elucidate the role of macrophages in lectin-mediated phagocytosis, an experimental system was used, where monocyte-derived THP-1 cells engulf the apoptotic bodies from the melanoma cell line MELJUSO. A flow cytometry assay was performed to reveal lectin expression and quantify the phagocytosis of apoptotic bodies. Taking into account that siglecs, a mannose receptor and galectins expressed on macrophages could be involved in engulfment of apoptotic bodies we studied their potential expression on THP-1 cells by means of polyacrylamide glycoconjugates. A strong binding of the cells to siglec ligands (3'SiaLac, 6'SiaLac, [Neu5Acalpha2-8]2) and galectin ligands (LacNAc, GalNAcbeta1 - 4GlcNAc, Galbeta1 - 3GalNAcbeta and asialoGM1) was observed. To reveal the corresponding targets on apoptotic bodies, the carbohydrate pattern of MELJUSO cells was analyzed. The apoptotic membrane was characterized by a high level of glycans terminated by galactose or sialic acid. To study lectin-mediated phagocytosis of apoptotic bodies by THP-1 cells, an inhibitory phagocytosis assay was performed. Binding of Galbeta1 - 3GalNAc- or LacNAc-specific reagents (lectins and antibodies) to apoptotic bodies abolished their engulfment by the THP-1 cells whereas blocking of Neu5Acalpha2 - 6 or Neu5Acalpha2 - 3 sites by the corresponding lectins was not effective. Furthermore, Galbeta1 - 3GalNAcbeta-PAA or asialoGM1-PAA binding to the THP-1 cells decreased phagocytosis, whereas two other potent THP-1-binding probes, LacNAc-PAA and GalNAcbeta1 - 4GlcNAc-PAA did not inhibit phagocytosis. Thus, Galbeta1 - 3GalNAcbeta-terminated chains represented on the apoptotic bodies but not the other tested galectin ligands appear to be a target for THP-1 cells.
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PMID:Involvement of the Galbeta1 - 3GalNAcbeta structure in the recognition of apoptotic bodies by THP-1 cells. 1286 97

Previously we isolated GlcNAc-specific lectin (DTL) from the ascidian Didemnum ternatanum by affinity chromatography on cross-linked ovalbumin. Here we report the purification and characterization of new D-GlcNAc/D-GalNAc-specific lectin DTL-A from the same ascidian. This lectin was isolated from non-bound cross-linked ovalbumin fraction and further was purified by gel filtration on Sepharose CL-4B, affinity chromatography on GlcNAc-agarose and gel filtration on Superdex 200. SDS-polyacrylamide gel electrophoresis and gel filtration of purified lectin on Sepharose CL-4B indicates that it exists as large aggregates in the native state. Investigations of the carbohydrate specificity of DTL-A by enzyme-linked lectin assay suggest the multi-specificity of this lectin. DTL-A binds BSM, asialo-BSM as well as heparin and dextran sulfate. The binding of DTL-A to BSM was inhibited by monosaccharides D-GlcNAc and D-GalNAc, their alpha- but not beta-anomers. Among polysaccharides and glycoconjugates, DTL-A binding to BSM was effectively inhibited by BSM, asialo-BSM, pronase-treated BSM and synthetic alpha-D-GalNAc-PAA. Fetuin and asialofetuin showed a much lower inhibitory potency, heparin and dextran sulfate were noninhibitory. On the other hand, DTL-A binding to heparin was effectively inhibited by dextran sulfate, fucoidan, whereas BSM showed insignificantly inhibitory effect. DTL-A binding to heparin was not inhibited by D-GlcNAc and D-GalNAc.
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PMID:New GlcNAc/GalNAc-specific lectin from the ascidian Didemnum ternatanum. 1578 80

In the present study we evaluated Canavalia brasiliensis (ConBr), Pisum arvense (PAA) and Artocarpus integrifolia (KM+) lectins as immunostimulatory molecules in vaccination against Leishmania amazonensis infection. Although they induced IFN-gamma production, the combination of the lectins with SLA antigen did not lead to lesion reduction. However, parasite load was largely reduced in mice immunized with KM+ lectin and SLA. KM+ induced a smaller inflammatory reaction in the air pouch model and was able to inhibit differentiation of dendritic cells (BMDC), but to induce maturation by enhancing the expression of MHC II, CD80 and CD86. These observations indicate the modulatory role of plant lectins in leishmaniasis vaccination may be related to their action on the initial innate response.
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PMID:Potential of KM+ lectin in immunization against Leishmania amazonensis infection. 1645 70

Galectin-1 (gal-1), a member of the mammalian beta-galactoside-binding proteins, recognizes preferentially Galbeta1-4GlcNAc sequences of several cell surface oligosaccharides. We demonstrate histochemically that the lectin recognizes appropriate glycotopes on the syncytiotrophoblast and extravillous trophoblast layer from second trimester human placenta and on BeWo chorion carcinoma cells. Gal-1 binding to BeWo cells was diminished by the Thomsen-Friedreich (TF)-disaccharide (Galbeta1-3GalNAc-) conjugated to polyacrylamide (TF-PAA). Gal-1 also inhibited BeWo cell proliferation in a concentration-dependent manner. Similar antiproliferative effects were also observed with an anti-TF monoclonal antibody (mAb, A78-G/A7). Therefore, we conclude that ligation of Galbeta1-4GlcNAc and Galbeta1-3GalNAc epitopes on BeWo cells may have regulatory effects on cell proliferation.
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PMID:Binding of galectin-1 (gal-1) to the Thomsen-Friedenreich (TF) antigen on trophoblast cells and inhibition of proliferation of trophoblast tumor cells in vitro by gal-1 or an anti-TF antibody. 1660 38

Polyacrylamide glycoconjugates, Glyc-PAA, having various tags or labels are convenient tools for analysis of cellular lectins. Adaptation of such glycoprobes for flow cytometry allows us to reveal lectins expressed on cell surface and analyze their carbohydrate specificity as well as functionality. Localization of lectins is visualized by labeling of cells with fluorescein-tagged glycoprobes, Glyc-PAA-fluo, in combination with fluorescent microscopy techniques. Additionally, biotinylated glycoprobes can be immobilized on magnetic particles making it possible to separate a cell population according to its carbohydrate-binding profile. Here, we exemplify application of glycoprobes in the study of cellular siglecs and galectins, as well as lectin patterning of tumor cells. The specificity of sialic acid binding membrane-anchored lectins, siglecs-1, -5, -7, -8 and -9 was determined using this methodology. To study the carbohydrate-binding profile of soluble galactoside-binding lectins, galectins-1 or -3, these were loaded on (initially galectin free) Raji cells and probed using Glyc-PAA-fluo. Lessons learned from this model system allowed us to study the galectin distribution pattern of tumors: cells obtained from mice carrying mammary adenocarcinoma or lymphoma were probed with Glyc-PAA-fluo using flow cytometry. Disaccharide 6OSuLacdiNAc was shown to be the most potent probe for adenocarcinoma cells, demonstrating that 6OSuLacdiNAc-binding molecules accumulate on cell surface in a patch-wise distribution.
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PMID:Glycoprobes as a tool for the study of lectins expressed on tumor cells. 1928 39


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