Specific recognition of the neuronal cell surface by an antiserum raised plasma membrane preparations of immature rat cerebellum

1982 ◽  
Vol 7 (9) ◽  
pp. 1031-1043 ◽  
Author(s):  
E. Meier ◽  
C. Regan ◽  
R. Bal�zs ◽  
G. P. Wilkin
Keyword(s):  
Plasma Membrane ◽  
Cell Surface ◽  
Neuronal Cell ◽  
Immature Rat ◽  
Specific Recognition ◽  
Rat Cerebellum

Glycoconjugates on the surface of spores of the pathogenic fungus Phytophthora cinnamomi studied using fluorescence and electron microscopy and flow cytometry

1990 ◽  
Vol 36 (3) ◽  
pp. 183-192 ◽  
Author(s):  
A. R. Hardham ◽  
E. Suzaki
Keyword(s):  
Flow Cytometry ◽  
Plasma Membrane ◽  
Cell Surface ◽  
Phytophthora Cinnamomi ◽  
Pathogenic Fungus ◽  
Fluorescein Isothiocyanate ◽  
Pathogenic Fungi ◽  
Surface Flow ◽  
Soybean Agglutinin ◽  
Binding Material

Glycoconjugates on the surface of zoospores and cysts of the pathogenic fungus Phytophthora cinnamomi have been studied using fluorescein isothiocyanate labelled lectins for fluorescence microscopy and flow cytometry, and ferritin- and gold-labelled lectins for ultrastructural analysis. Of the five lectins used, only concanavalin A (ConA) binds to the surface of the zoospores, including the flagella and water expulsion vacuole. This suggests that of accessible saccharides, glucosyl or mannosyl residues predominate on the outer surface of the zoospore plasma membrane. Early in encystment, a system of flat disc-like cisternae, which underlie the zoospore plasma membrane, vesiculate. These and other small peripheral vesicles quickly disappear. After the induction of encystment, ConA is no longer localised close to the plasma membrane but binds to material loosely associated with the cell surface. Quantitative measurements by flow cytometry indicate that the ConA-binding material is gradually lost from the cell surface. The cyst wall is weakly labelled, but the site of germ tube emergence stains intensely. During the first 2 min after the induction of encystment, material that binds soybean agglutinin, Helix pommatia agglutinin, and peanut agglutinin appears on the surface of the fungal cells. The distribution of this material, rich in galactosyl or N-acetyl-D-galactosaminosyl residues, is initially patchy, but by 5 min the material evenly coats most of the cell surface. Labelling of zoospores in which intracellular sites are accessible indicates that the soybean agglutinin binding material is stored in vesicles that lie beneath the plasma membrane. Quantitation of soybean agglutinin labelling shows that maximum binding occurs 2–3 min after the induction of encystment. Key words: cell surface, flow cytometry, lectins, pathogenic fungi, Phytophthora cinnamomi.

Identification of the neuronal cell surface molecule B2 in chick

1992 ◽  
Vol 17 ◽  
pp. 165
Author(s):  
Akihito Mizutani ◽  
Kunimasa Ohta ◽  
Hajime Fujisawa
Keyword(s):  
Cell Surface ◽  
Neuronal Cell ◽  
Surface Molecule ◽  
Cell Surface Molecule

scholarly journals CELL SURFACE IMMUNOGLOBULIN

1972 ◽  
Vol 135 (6) ◽  
pp. 1392-1405 ◽  
Author(s):  
Charles J. Sherr ◽  
Sonia Baur ◽  
Inge Grundke ◽  
Joseph Zeligs ◽  
Barbara Zeligs ◽  
...  
Keyword(s):  
Bone Marrow ◽  
Plasma Membrane ◽  
Cell Surface ◽  
Noncovalent Interactions ◽  
Subcellular Fractionation ◽  
Splenic Lymphocytes ◽  
Surface Immunoglobulin ◽  
Established Line ◽  
Intracellular Proteins ◽  
Daudi Cells

Cells from an established line of Burkitt lymphoma (Daudi) were enzymatically radioiodinated, and labeled Ig from the cell surface was isolated and studied. Subcellular fractionation of labeled cells confirmed that intracellular proteins from the cytoplasm are not iodinated by this method. Radioactive Ig was identified as monomeric (8S) IgM, and an average of 105 Ig molecules was found per cell. Ig molecules could be released from the plasma membrane by detergent lysis under nonreducing conditions indicating that attachment of Ig to the plasma membrane occurs via noncovalent interactions. The ratio of µ/L radioactivity in surface Ig was the same as that of total cellular Ig radioiodinated in solution suggesting that a large portion of the Fc fragment is not buried within the membrane. In contrast to the results obtained with cell surface Ig, most intracellular Ig was found as "free" µ- and L chains regardless of whether lysates were labeled with 125I or cells were labeled with leucine-3H. The results indicate that only a small percentage of the total Ig of Daudi cells is associated with the cell surface and suggest that covalent assembly of Ig occurs at or near the time that the molecule becomes part of the plasma membrane. Similarities between cell surface Ig on normal splenic lymphocytes and Daudi cells suggest that the latter is a neoplasm of bone marrow-derived lymphocytes.

scholarly journals Vesicular Transport Is Not Required for the Cytoplasmic Pool of Cholera Toxin To Interact with the Stimulatory Alpha Subunit of the Heterotrimeric G Protein

2004 ◽  
Vol 72 (12) ◽  
pp. 6826-6835 ◽  
Author(s):  
Ken Teter ◽  
Michael G. Jobling ◽  
Randall K. Holmes
Keyword(s):  
Plasma Membrane ◽  
Cell Surface ◽  
Cholera Toxin ◽  
G Protein ◽  
Vesicular Transport ◽  
Cytotoxic Action ◽  
Anterograde Transport ◽  
Heterotrimeric G Protein ◽  
Α Subunit ◽  
Vesicular Traffic

ABSTRACT Cholera toxin (CT) moves from the cell surface to the endoplasmic reticulum (ER) by retrograde vesicular transport. The catalytic A1 polypeptide of CT (CTA1) then crosses the ER membrane, enters the cytosol, ADP-ribosylates the stimulatory α subunit of the heterotrimeric G protein (Gsα) at the cytoplasmic face of the plasma membrane, and activates adenylate cyclase. The cytosolic pool of CTA1 may reach the plasma membrane and its Gsα target by traveling on anterograde-directed transport vesicles. We examined this possibility with the use of a plasmid-based transfection system that directed newly synthesized CTA1 to either the ER lumen or the cytosol of CHO cells. Such a system allowed us to bypass the CT retrograde trafficking itinerary from the cell surface to the ER. Previous work has shown that the ER-localized pool of CTA1 is rapidly exported from the ER to the cytosol. Expression of CTA1 in either the ER or the cytosol led to the activation of Gsα, and Gsα activation was not inhibited in transfected cells exposed to drugs that inhibit vesicular traffic. Thus, anterograde transport from the ER to the plasma membrane is not required for the cytotoxic action of CTA1.

Evidence for a multiple innervation of purkinje cells by climbing fibers in the immature rat cerebellum

1976 ◽  
Vol 7 (6) ◽  
pp. 567-578 ◽  
Author(s):  
Francis Crepel ◽  
Jean Mariani ◽  
Nicole Delhaye-Bouchaud
Keyword(s):  
Purkinje Cells ◽  
Climbing Fibers ◽  
Immature Rat ◽  
Rat Cerebellum

scholarly journals Eisosomes are metabolically regulated storage compartments for APC-type nutrient transporters

2018 ◽  
Vol 29 (17) ◽  
pp. 2113-2127 ◽  
Author(s):  
Akshay Moharir ◽  
Lincoln Gay ◽  
Daniel Appadurai ◽  
James Keener ◽  
Markus Babst
Keyword(s):  
Plasma Membrane ◽  
Cell Surface ◽  
Proton Pumping ◽  
Proton Gradient ◽  
Lipid Domains ◽  
Nutrient Transporters ◽  
Major Function ◽  
Show Evidence ◽  
Higher Eukaryotes ◽  
Pumping Activity

Eisosomes are lipid domains of the yeast plasma membrane that share similarities to caveolae of higher eukaryotes. Eisosomes harbor APC-type nutrient transporters for reasons that are poorly understood. Our analyses support the model that eisosomes function as storage compartments, keeping APC transporters in a stable, inactive state. By regulating eisosomes, yeast is able to balance the number of proton-driven APC transporters with the proton-pumping activity of Pma1, thereby maintaining the plasma membrane proton gradient. Environmental or metabolic changes that disrupt the proton gradient cause the rapid restructuring of eisosomes and results in the removal of the APC transporters from the cell surface. Furthermore, we show evidence that eisosomes require the presence of APC transporters, suggesting that regulating activity of nutrient transporters is a major function of eisosomes.

Sign in / Sign up

Export Citation Format

Share Document