Wheat germ agglutinin and Lens culinaris agglutinin sensitized anisotropic silver nanoparticles in detection of bacteria: A simple photometric assay

To evaluate the relative mobilities of cell surface glycoconjugates during myogenesis we have studied the redistribution of fluorescein-conjugated plant lectins on L6 rat myogenic cells. Previous experiments had demonstrated that the receptors for the lectins soybean agglutinin (SBA), wheat germ agglutinin, concanavalin A and Lens culinaris agglutinin all were relatively uniformly distributed on both myoblasts and myotubes, and that SBA receptors were capable of rapid redistribution on myotubes but not myoblasts at 4 degrees C (Sawyer & Akeson, 1983). Here we show that when SBA-labelled myoblasts are incubated at 37 degrees C, or for extended times at 4 degrees C, the lectin aggregates as on myotubes. So it appears that SBA-binding components show a quantitative rather than qualitative change in their mobility during L6 differentiation. In addition, the redistribution of the three other lectins on myoblasts and myotubes was either less prominent (i.e. showing fewer apparent surface clusters) or occurred less rapidly than with SBA. None of these three lectins showed striking differences in mobility between myoblasts and myotubes. Thus, it appears that SBA binds to a subset of surface glycoconjugates that is relatively highly mobile, and that this mobility is specifically enhanced with differentiation.

Download Full-text

Interaction of Lens culinaris lectin, Concanavalin A, Ricinus communis agglutinin and wheat germ agglutinin with the cell surface of normal and transformed rat liver cells

Experimentelle Pathologie ◽

10.1016/s0014-4908(75)80039-1 ◽

1975 ◽

Vol 10 (5-6) ◽

pp. 309-317 ◽

Cited By ~ 1

Author(s):

J. Roth ◽

G. Neupert ◽

K. Thoss

Keyword(s):

Cell Surface ◽

Rat Liver ◽

Concanavalin A ◽

Wheat Germ Agglutinin ◽

Wheat Germ ◽

Lens Culinaris ◽

Ricinus Communis ◽

Liver Cells ◽

Ricinus Communis Agglutinin ◽

Rat Liver Cells

Download Full-text

Failure of 6D1 or Exposure of Platelets to ADP to Affect Agglutination Induced by Wheat Germ Agglutinin

Thrombosis and Haemostasis ◽

10.1055/s-0038-1646911 ◽

1989 ◽

Vol 62 (02) ◽

pp. 815 ◽

Cited By ~ 1

Author(s):

Marjorie B Zucker ◽

Robert A Grant ◽

Evelyn A Mauss

Keyword(s):

Wheat Germ Agglutinin ◽

Wheat Germ

Download Full-text

Transport Characteristics of Wheat Germ Agglutinin-Modified Insulin-Liposomes and Solid Lipid Nanoparticles in a Perfused Rat Intestinal Model

Journal of Nanoscience and Nanotechnology ◽

10.1166/jnn.2006.425 ◽

2006 ◽

Vol 6 (9) ◽

pp. 2959-2966 ◽

Cited By ~ 16

Author(s):

Na Zhang ◽

Qineng Ping ◽

Guihua Huang ◽

Xiuzhen Han ◽

Yanna Cheng ◽

...

Keyword(s):

Solid Lipid Nanoparticles ◽

Wheat Germ Agglutinin ◽

Wheat Germ ◽

Serum Insulin ◽

Lipid Nanoparticles ◽

Solid Lipid ◽

Mucosal Absorption ◽

Perfusion Experiment ◽

Absorption Sites

Wheat germ agglutinin (WGA) modified liposomes and solid lipid nanoparticles (SLNs) were evaluated for improving intestinal absorption of insulin. In an in situ local intestinal perfusion experiment, formulations containing 100 IU/kg insulin were administered to the duodenum, jejunum, and ileum of fasted rats. As hypothesized, ileum was the best intestinal location for the absorption of insulin-containing liposomes. Serum insulin concentrations decreased for the various formulations in different absorption sites according to the following trends: Duodenum > ileum > jejunum for WGA-modified insulin-containing liposomes; duodenum > jejunum > ileum for WGA-modified insulin-containing SLNs; ileum > jejunum > duodenum for insulin-containing liposomes; ileum > duodenum > jejunum for insulin-containing SLNs; and duodenum ≥ ileum > jejunum for aqueous solution of insulin. These results imply that the nanoparticle type and delivery site were important factors with respect to increasing the bioavailability of insulin following oral administration. The proteolytic degradation as well as the epithelial permeability were primary determinants influcing insulin mucosal absorption.

Download Full-text

Identification of distinct haemocyte populations from the freshwater bivalves swan mussel (Anodonta cygnea) and duck mussel (Anodonta anatina) using wheat-germ agglutinin

Canadian Journal of Zoology ◽

10.1139/cjz-2017-0006 ◽

2017 ◽

Vol 95 (12) ◽

pp. 937-947 ◽

Cited By ~ 3

Author(s):

M. Hinzmann ◽

M. Lopes-Lima ◽

F. Cerca ◽

A. Correia ◽

J. Machado ◽

...

Keyword(s):

Flow Cytometry ◽

Wheat Germ Agglutinin ◽

Wheat Germ ◽

Transmission Microscopy ◽

Anodonta Cygnea ◽

Functional Studies ◽

Lectin Staining ◽

Surface Staining ◽

Cytological Features ◽

Freshwater Bivalves

Haemocytes play a major role in molluscs immunity. Functional studies are, however, impaired by limited available experimental tools to identify and sort distinct haemocyte populations. Therefore, using nonlethal methods, we aimed at evaluating whether lectin staining combined with flow cytometry could be used to distinguish circulating haemocyte populations from two freshwater bivalves of the family Unionidae, the duck mussel (Anodonta anatina (L., 1758)) and the swan mussel (Anodonta cygnea (L., 1758)). Based on classical classification, haemocytes were distinguished as granulocytes and hyalinocytes and cytological features were visualized using transmission microscopy and staining techniques. Size, granularity, viability, and surface staining using lectins as specific probes were analysed by flow cytometry and fluorescence microscopy. The microscopic proportions of granulocytes and hyalinocytes significantly differed, being of 70% and 30% for A. cygnea and of 85% and 15% for A. anatina, respectively. Two haemocyte populations were sorted by flow cytometry based on size and granularity and confirmed as granulocytes and hyalinocytes. Interestingly, two different granulocyte populations could be further discriminated in A. cygnea according to their binding affinity to wheat-germ agglutinin (WGA), whereas granulocytes of A. anatina all stained similarly. Our results show that WGA labelling combined with flow cytometry can be used to better discriminate Anodonta haemocyte populations and obtain purified populations for functional studies.

Download Full-text