scholarly journals Society Medal and Awards Winners for 2006

2005 ◽  
Vol 27 (4) ◽  
pp. 57-60
Keyword(s):  
Cell Surface ◽  
B Lymphocytes ◽  
Cell Types ◽  
Surface Antigens ◽  
Surface Proteins ◽  
Specific Cell ◽  
Cell Surface Antigens ◽  
Cell Surface Proteins ◽  
Extracellular Signals ◽  
Proliferation And Differentiation

Congratulations go to the following scientists who will be recipients of the Society's Awards in 2006. use antibodies against cell-surface antigens to distinguish and separate T- and B-lymphocytes and to show that antibody binding causes a redistribution and endocytosis of cell-surface proteins. He has studied the intracellular programmes and extracellular signals that control the survival, growth, proliferation and differentiation of specific cell types of the developing rodent nervous system.

Monoclonal antibodies to tissue-specific cell surface antigens

1984 ◽  
Vol 33 (2) ◽  
pp. 268-281 ◽  
Author(s):  
Ann M. Carroll ◽  
Michael Zalutsky ◽  
Sam Schatten ◽  
Atul Bhan ◽  
Linda L. Perry ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Cell Surface ◽  
Surface Antigens ◽  
Specific Cell ◽  
Cell Surface Antigens ◽  
Tissue Specific ◽  
Specific Cell Surface

scholarly journals Β-Galactosidase-Catalyzed Fluorescent Reporter Labeling of Living Cells for Sensitive Detection of Cell Surface Antigens

2020 ◽  
Author(s):  
Katsuya Noguchi ◽  
Takashi Shimomura ◽  
Yuya Ohuchi ◽  
Munetaka Ishiyama ◽  
Masanobu Shiga ◽  
...  
Keyword(s):  
Cell Surface ◽  
Enzymatic Reaction ◽  
Wavelength Region ◽  
Living Cells ◽  
Fluorescent Dye ◽  
Surface Proteins ◽  
Quinone Methide ◽  
Fluorescence Signal ◽  
Cell Surface Antigens ◽  
Cell Surface Proteins

The ability to detect cell surface proteins using fluorescent dye-labeled antibodies is crucial for the reliable identification of many cell types. However, the different types of cell surface proteins used to identify cells are currently limited in number because they need to be expressed at high levels to exceed background cellular autofluorescence, especially in the shorter wavelength region. Herein, we report on a new method (CLAMP: quinone methide-based <u>c</u>atalyzed signa<u>l</u> <u>amp</u>lification) in which the fluorescence signal is amplified by an enzymatic reaction that strongly facilitates the detection of cell surface proteins on living cells. We used β-galactosidase as an amplification enzyme and designed a substrate for it, called MUGF, which contains a fluoromethyl group. Upon removal of the galactosyl group in MUGF by β-galactosidase labeling of the target cell surface proteins, the resulting quinone methide group-containing product was found to be both cell membrane permeable and reactive with intracellular nucleophiles, thereby providing fluorescent adducts. Using this method, we successfully detected several cell surface proteins including programmed death ligand 1 protein, which is difficult to detect using conventional fluorescent dye-labeled antibodies.

scholarly journals Interaction of single-chain urokinase with its receptor induces the appearance and disappearance of binding epitopes within the resultant complex for other cell surface proteins

Blood ◽  
1996 ◽  
Vol 88 (2) ◽  
pp. 542-551 ◽  
Author(s):  
AA Higazi ◽  
RH Upson ◽  
RL Cohen ◽  
J Manuppello ◽  
J Bognacki ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Cell Surface ◽  
Binding Sites ◽  
Ldl Receptor ◽  
Cell Types ◽  
Surface Proteins ◽  
Single Chain ◽  
Cell Surface Proteins ◽  
Functional Changes ◽  
And Migration

Binding of urokinase-type plasminogen activator (uPA) to its glycosylphosphatidylinositol-anchored receptor (uPAR) initiates signal transduction, adhesion, and migration in certain cell types. To determine whether some of these activities may be mediated by associations between the uPA/uPAR complex and other cell surface proteins, we studied the binding of complexes composed of recombinant, soluble uPA receptor (suPAR) and single chain uPA (scuPA) to a cell line (LM-TK- fibroblasts) that does not express glycosylphosphatidylinositol (GPI)-anchored proteins to eliminate potential competition by endogenous uPA receptors. scuPA induced the binding of suPAR to LM-TK- cells. Binding of labeled suPAR/scuPA was inhibited by unlabeled complex, but not by scuPA or suPAR added separately, indicating cellular binding sites had been formed that are not present in either component. Binding of the complex was inhibited by low molecular weight uPA (LMW-uPA) indicating exposure of an epitope found normally in the isolated B chain of two chain uPA (tcuPA), but hidden in soluble scuPA. Binding of LMW-uPA was independent of its catalytic site and was associated with retention of its enzymatic activity. Additional cell binding epitopes were generated within suPAR itself by the aminoterminal fragment of scuPA, which itself does not bind to LM-TK- cells. When scuPA bound to suPAR, a binding site for alpha 2-macroglobulin receptor/LDL receptor-related protein (alpha 2 MR/LRP) was lost, while binding sites for cell-associated vitronectin and thrombospondin were induced. In accord with this, the internalization and degradation of cell-associated tcuPA and tcuPA-PAI- 1 complexes proceeded less efficiently in the presence of suPAR. Further, little degradation of suPAR was detected, suggesting that cell- bound complex dissociated during the initial stages of endocytosis. Thus, the interaction of scuPA with its receptor causes multiple functional changes within the complex including the dis-appearance of an epitope in scuPA involved in its clearance from the cell surface and the generation of novel epitopes that promote its binding to proteins involved in cell adhesion and signal transduction.

scholarly journals Large-scale co-aggregation of fluorescent lipid probes with cell surface proteins.

1994 ◽  
Vol 125 (4) ◽  
pp. 795-802 ◽  
Author(s):  
J L Thomas ◽  
D Holowka ◽  
B Baird ◽  
W W Webb
Keyword(s):  
Cell Surface ◽  
Large Scale ◽  
Plasma Membranes ◽  
Immunoglobulin E ◽  
Large Fraction ◽  
Surface Antigens ◽  
Specific Cell ◽  
Cell Surface Antigens ◽  
Receptor Complexes ◽  
Ige Receptors

Large scale aggregation of fluorescein-labeled immunoglobulin E (IgE) receptor complexes on the surface of RBL cells results in the co-aggregation of a large fraction of the lipophilic fluorescent probe 3,3'-dihexadecylindocarbocyanine (diI) that labels the plasma membranes much more uniformly in the absence of receptor aggregation. Most of the diI molecules that are localized in patches of aggregated receptors have lost their lateral mobility as determined by fluorescence photobleaching recovery. The diI outside of patches is mobile, and its mobility is similar to that in control cells without receptor aggregates. It is unlikely that the co-aggregation of diI with IgE receptors is due to specific interactions between these components, as two other lipophilic probes of different structures are also observed to redistribute with aggregated IgE receptors, and aggregation of two other cell surface antigens also results in the coredistribution of diI at the RBL cell surface. Quantitative analysis of CCD images of labeled cells reveals some differences in the spatial distributions of co-aggregated diI and IgE receptors. The results indicate that cross-linking of specific cell surface antigens causes a substantial change in the organization of the plasma membrane by redistributing pre-existing membrane domains or causing their formation.

scholarly journals TISSUE-SPECIFIC CELL-SURFACE ANTIGENS IN EMBRYONIC CELLS

1972 ◽  
Vol 53 (2) ◽  
pp. 435-449 ◽  
Author(s):  
Irving Goldschneider ◽  
A. A. Moscona
Keyword(s):  
Cell Surface ◽  
Surface Antigens ◽  
Embryonic Cell ◽  
Specific Cell ◽  
Embryonic Chick ◽  
Embryonic Cells ◽  
Cell Surfaces ◽  
Cell Surface Antigens ◽  
Tissue Specific ◽  
High Degree

With the use of antisera prepared in rabbits against suspensions of live embryonic chick tissue cells, qualitative differences in cell surface antigens were demonstrated on cells from different embryonic chick tissues by immune agglutination and immunofluorescence. Unabsorbed antisera reacted with both homologous and nonhomologous cells; thorough absorption of the antisera with heterologous tissues removed cross-reacting antibodies, and the antisera acquired a high degree of tissue specificity. Thus, antiretina cell serum absorbed with nonretina cells or tissues, agglutinated only neural retina cells, and was shown by immunofluorescence tests to react specifically with the surface of retina cells, both in cell suspensions and in frozen tissue sections. Comparable results with antisera against cells from embryonic liver and other tissues demonstrated the existence of tissue-specific, phenotypic disparities in the antigenicities of embryonic cell surfaces, in addition to the presence of cell-surface antigens shared by certain classes of cells, and of antigens common to all cells in the embryo. The results are discussed in terms of the possible involvement of such phenotypic determinants in the specification of cell surfaces, in relation to cell recognition and developmental interactions.

scholarly journals Prediction of the Secretome and the Surfaceome: A Strategy to Decipher the Crosstalk between Adipose Tissue and Muscle during Fetal Growth

2020 ◽  
Vol 21 (12) ◽  
pp. 4375
Author(s):  
Muriel Bonnet ◽  
Nicolas Kaspric ◽  
Kimberly Vonnahme ◽  
Didier Viala ◽  
Christophe Chambon ◽  
...  
Keyword(s):  
Adipose Tissue ◽  
Cell Surface ◽  
Fetal Growth ◽  
Protein Interactions ◽  
Cell Types ◽  
Surface Proteins ◽  
Protein Protein Interactions ◽  
Cell Surface Proteins ◽  
Bovine Fetuses ◽  
Muscular Tissues

Crosstalk between adipose and muscular tissues is hypothesized to regulate the number of muscular and adipose cells during fetal growth, with post-natal consequences on lean and fat masses. Such crosstalk largely remains, however, to be described. We hypothesized that a characterization of the proteomes of adipose and muscular tissues from bovine fetuses may enhance the understanding of the crosstalk between these tissues through the prediction of their secretomes and surfaceomes. Proteomic experiments have identified 751 and 514 proteins in fetal adipose tissue and muscle. These are mainly involved in the regulation of cell proliferation or differentiation, but also in pathways such as apoptosis, Wnt signalling, or cytokine-mediated signalling. Of the identified proteins, 51 adipokines, 11 myokines, and 37 adipomyokines were predicted, together with 26 adipose and 13 muscular cell surface proteins. Analysis of protein–protein interactions suggested 13 links between secreted and cell surface proteins that may contribute to the adipose–muscular crosstalk. Of these, an interaction between the adipokine plasminogen and the muscular cell surface alpha-enolase may regulate the fetal myogenesis. The in silico secretome and surfaceome analyzed herein exemplify a powerful strategy to enhance the elucidation of the crosstalk between cell types or tissues.

Sign in / Sign up

Export Citation Format

Share Document