scholarly journals CELL SURFACE IMMUNOGLOBULIN

1972 ◽  
Vol 136 (4) ◽  
pp. 676-696 ◽  
Author(s):  
Ellen S. Vitetta ◽  
Jonathan W. Uhr
Keyword(s):  
Medium Release ◽  
Plasma Membrane ◽  
Cell Surface ◽  
B Cell ◽  
Normal Mouse ◽  
Surface Phase ◽  
Temperature Dependent ◽  
Short Term ◽  
Surface Immunoglobulin ◽  
A Cell

Turnover and release of cell surface Ig and secretion of total intracellular Ig has been studied in small lymphocytes from normal mouse spleen. The major findings to emerge are: (a) small lymphocytes secrete 8S IgM and IgG. A small portion of the 8S IgM, but virtually none of the IgG appears to have a cell surface phase. (b) Cell surface IgM is actively turned over with a half-life of 6–8 hr, and turnover can be accounted for by release into the incubation medium. Release is temperature dependent. (c) Released cell surface Ig is noncovalently bound to a fragment of plasma membrane. (d) H-2 antigens are not released during short-term incubation. Based on the above findings, we propose a model for the transport and release of both cell surface and conventionally secreted Ig.

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 Cytoskeletal-membrane interactions: a stable interaction between cell surface glycoconjugates and doublet microtubules of the photoreceptor connecting cilium.

1987 ◽  
Vol 105 (6) ◽  
pp. 2973-2987 ◽  
Author(s):  
C J Horst ◽  
D M Forestner ◽  
J C Besharse
Keyword(s):  
Plasma Membrane ◽  
Cell Surface ◽  
Molecular Mass ◽  
Lipid Bilayer ◽  
Neonatal Rat ◽  
Sds Page ◽  
A Cell ◽  
The Cross ◽  
Triton X ◽  
Cell Surface Glycoconjugates

The ciliary base is marked by a transition zone in which Y-shaped cross-linkers extend from doublet microtubules to the plasma membrane. Our goal was to investigate the hypothesis that the cross-linkers form a stable interaction between membrane or cell surface components and the underlying microtubule cytoskeleton. We have combined Triton X-100 extraction with lectin cytochemistry in the photoreceptor sensory cilium to investigate the relationship between cell surface glycoconjugates and the underlying cytoskeleton, and to identify the cell surface components involved. Wheat germ agglutinin (WGA) binds heavily to the cell surface in the region of the Y-shaped cross-linkers of the neonatal rat photoreceptor cilium. WGA binding is not removed by prior digestion with neuraminidase and succinyl-WGA also binds the proximal cilium, suggesting a predominance of N-acetylglucosamine containing glycoconjugates. Extraction of the photoreceptor plasma membrane with Triton X-100 removes the lipid bilayer, leaving the Y-shaped crosslinkers associated with the axoneme. WGA-binding sites are found at the distal ends of the crosslinkers after Triton X-100 extraction, indicating that the microtubule-membrane cross-linkers retain both a transmembrane and a cell surface component after removal of the lipid bilayer. To identify glycoconjugate components of the cross-linkers we used a subcellular fraction enriched in axonemes from adult bovine retinas. Isolated, detergent-extracted bovine axonemes show WGA binding at the distal ends of the cross-linkers similar to that seen in the neonatal rat. Proteins of the axoneme fraction were separated by SDS-PAGE and electrophoretically transferred to nitrocellulose. WGA labeling of the nitrocellulose transblots reveals three glycoconjugates, all of molecular mass greater than 400 kD. The major WGA-binding glycoconjugate has an apparent molecular mass of approximately 600 kD and is insensitive to prior digestion with neuraminidase. This glycoconjugate may correspond to the dominant WGA-binding component seen in cytochemical experiments.

scholarly journals Inhibition of antibody-dependent cellular cytotoxicity and immunoglobulin synthesis by an antiserum prepared against a human B-cell Ia-like molecule.

1976 ◽  
Vol 144 (1) ◽  
pp. 113-122 ◽  
Author(s):  
L Chess ◽  
R Evans ◽  
R E Humphreys ◽  
J L Strominger ◽  
S F Schlossman
Keyword(s):  
Cell Surface ◽  
B Cell ◽  
Specific Antigen ◽  
Cell Populations ◽  
Antibody Dependent Cellular Cytotoxicity ◽  
Physical Separation ◽  
Effector Cells ◽  
Antigen Complex ◽  
A Cell ◽  
Human B Cell

Rabbit antisera to the human B-cell-specific antigen complex, p23,30, was used to define further the functional heterogeneity of isolated human lymphocyte subpopulations. Specific depletion of p23,30-bearing cells from Ig-negative cell populations and Ig-negative, E rosette-negative (Null) populations by either complement-mediated lysis or by physical separation on goat antirabbit Fab immunoabsorbent columns, eliminates the antibody-dependent cellular cytotoxic (ADCC) function. Furthermore, binding of anti-p23,30 serum to the effector cell surface inhibits ADCC but does not interfere with EA rosette formation. Apparently p23,30 represents a cell surface site which is distinct from the Fc receptor but which is important in the triggering of ADCC. In addition, depletion of p23,30-bearing cells from unfractionated cell populations, Ig-positive B-cell populations and Ig-negative, E rosette-negative (Null) populations eliminates the capacity of these populations to secrete immunoglobulin during subsequent culturing. Thus both the Ig-secreting cells and the ADCC effector cells within the Ig-negative, E rosette-negative (Null) population reside in the same population of cells which bears the p23,30 antigen.

scholarly journals BINDING OF SOLUBLE IMMUNE COMPLEXES TO HUMAN LYMPHOBLASTOID CELLS

1974 ◽  
Vol 140 (4) ◽  
pp. 877-894 ◽  
Author(s):  
Argyrios N. Theofilopoulos ◽  
Frank J. Dixon ◽  
Viktor A. Bokisch
Keyword(s):  
Cell Surface ◽  
B Cell ◽  
Cell Lines ◽  
Immune Complexes ◽  
Surface Membrane ◽  
Raji Cells ◽  
Human Lymphoblastoid Cell ◽  
C Cell ◽  
A Cell ◽  
Soluble Immune Complexes

In the present work we studied the expression of membrane-bound Ig (MBIg) as well as receptors for IgG Fc and complement on nine human lymphoblastoid cell lines. When MBIg and receptors for IgG Fc were compared, four categories of cell lines could be distinguished: (a) cell lines having both MBIg and receptors for IgG Fc, (b) cell lines having MBIg but lacking receptors for IgG Fc, (c) cell lines lacking MBIg but having receptors for IgG Fc, and (d) cell lines lacking both MBIg and receptors for IgG Fc. Two types of receptors for complement could be detected on the cell lines studied, one for C3-C3b and one for C3d. When sensitized red cells carrying C3b or C3d were used for rosette tests, three categories of cell lines could be distinguished: (a) cell lines having receptors for C3b and C3d, (b) cell lines having receptors only for C3d and (c) cell lines lacking both receptors. However, when a more sensitive immunofluorescent method was used instead of the rosette technique, it was found that cell lines unable to form rosettes with EAC1423bhu were able to bind soluble C3 or C3b which indicated the presence of these receptors on the cell surface. Inhibition experiments showed that receptors for C3-C3b and receptors for C3d are distinct and that receptors for C3-C3b and C3d are different from receptors for IgG Fc. A cell line (Raji) without MBIg but with receptors for IgG Fc, C3-C3b, and C3d was selected for use in studying the binding mechanism of soluble immune complexes to cell surface membrane. Aggregated human gamma globulin was used in place of immune complexes. Immune complexes containing complement bind to Raji cells only via receptors for complement, namely receptors for C3-C3b and C3d. Binding of immune complexes containing complement to cells is much greater than that of complexes without complement. Immune complexes bound to cells via receptors for complement can be partially released from the cell surface by addition of normal human serum as well as isolated human C3 or C3b. We postulate that such release is due to competition of immune complex bound C3b and free C3 or C3b for the receptors on Raji cells.

scholarly journals Retention of a cell adhesion complex at the paranodal junction requires the cytoplasmic region of Caspr

2002 ◽  
Vol 157 (7) ◽  
pp. 1247-1256 ◽  
Author(s):  
Leora Gollan ◽  
Helena Sabanay ◽  
Sebastian Poliak ◽  
Erik O. Berglund ◽  
Barbara Ranscht ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Cell Adhesion ◽  
Cell Surface ◽  
Cell Adhesion Molecules ◽  
Cytoplasmic Domain ◽  
Short Sequence ◽  
Extracellular Region ◽  
A Cell ◽  
Adhesion Complex ◽  
Protein 4.1B

An axonal complex of cell adhesion molecules consisting of Caspr and contactin has been found to be essential for the generation of the paranodal axo-glial junctions flanking the nodes of Ranvier. Here we report that although the extracellular region of Caspr was sufficient for directing it to the paranodes in transgenic mice, retention of the Caspr–contactin complex at the junction depended on the presence of an intact cytoplasmic domain of Caspr. Using immunoelectron microscopy, we found that a Caspr mutant lacking its intracellular domain was often found within the axon instead of the junctional axolemma. We further show that a short sequence in the cytoplasmic domain of Caspr mediated its binding to the cytoskeleton-associated protein 4.1B. Clustering of contactin on the cell surface induced coclustering of Caspr and immobilized protein 4.1B at the plasma membrane. Furthermore, deletion of the protein 4.1B binding site accelerated the internalization of a Caspr–contactin chimera from the cell surface. These results suggest that Caspr serves as a “transmembrane scaffold” that stabilizes the Caspr/contactin adhesion complex at the paranodal junction by connecting it to cytoskeletal components within the axon.

scholarly journals A cell surface/plasma membrane antigen of Candida albicans

1991 ◽  
Vol 137 (3) ◽  
pp. 455-464 ◽  
Author(s):  
R.-K. Li ◽  
J. E. Cutler
Keyword(s):  
Candida Albicans ◽  
Plasma Membrane ◽  
Cell Surface ◽  
Surface Plasma ◽  
A Cell

scholarly journals Neisseria gonorrhoeae Porin P1.B Induces Endosome Exocytosis and a Redistribution of Lamp1 to the Plasma Membrane

2002 ◽  
Vol 70 (11) ◽  
pp. 5965-5971 ◽  
Author(s):  
Patricia Ayala ◽  
Brandi Vasquez ◽  
Lee Wetzler ◽  
Magdalene So
Keyword(s):  
Plasma Membrane ◽  
Epithelial Cells ◽  
Cell Surface ◽  
Neisseria Gonorrhoeae ◽  
Bacterial Infection ◽  
Immunoglobulin A ◽  
Late Endosomes ◽  
A Cell ◽  
Iga Protease

ABSTRACT The immunoglobulin A (IgA) protease secreted by pathogenic Neisseria spp. cleaves Lamp1, thereby altering lysosomes in a cell and promoting bacterial intracellular survival. We sought to determine how the IgA protease gains access to cellular Lamp1 in order to better understand the role of this cleavage event in bacterial infection. In a previous report, we demonstrated that the pilus-induced Ca2+ transient triggers lysosome exocytosis in human epithelial cells. This, in turn, increases the level of Lamp1 at the plasma membrane, where it can be cleaved by IgA protease. Here, we show that porin also induces a Ca2+ flux in epithelial cells. This transient is similar in nature to that observed in phagocytes exposed to porin. In contrast to the pilus-induced Ca2+ transient, the porin-induced event does not trigger lysosome exocytosis. Instead, it stimulates exocytosis of early and late endosomes and increases Lamp1 on the cell surface. These results indicate that Neisseria pili and porin perturb Lamp1 trafficking in epithelial cells by triggering separate and distinct Ca2+-dependent exocytic events, bringing Lamp1 to the cell surface, where it can be cleaved by IgA protease.

CD5 Is A Potential Selecting Ligand for B-Cell Surface Immunoglobulin: A Possible Role in Maintenance and Selective Expansion of Normal and Malignant B Cells

2000 ◽  
Vol 36 (3-4) ◽  
pp. 353-365 ◽  
Author(s):  
Richard Pospisil ◽  
Gregg J. Silverman ◽  
Gerald E. Marti ◽  
Alejandro Aruffo ◽  
Michael A. Bowen ◽  
...  
Keyword(s):  
B Cells ◽  
Cell Surface ◽  
B Cell ◽  
Immunoglobulin A ◽  
Surface Immunoglobulin

scholarly journals A pathway for cell wall anchorage of Saccharomyces cerevisiae alpha-agglutinin.

1994 ◽  
Vol 14 (7) ◽  
pp. 4825-4833 ◽  
Author(s):  
C F Lu ◽  
J Kurjan ◽  
P N Lipke
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Wall ◽  
Plasma Membrane ◽  
Cell Surface ◽  
Soluble Form ◽  
Gpi Anchor ◽  
Glycosyl Phosphatidylinositol ◽  
Experimental Support ◽  
Cell Biol ◽  
A Cell

Saccharomyces cerevisiae alpha-agglutinin is a cell wall-anchored adhesion glycoprotein. The previously identified 140-kDa form, which contains a glycosyl-phosphatidylinositol (GPI) anchor (D. Wojciechowicz, C.-F. Lu, J. Kurjan, and P. N. Lipke, Mol. Cell. Biol. 13:2554-2563, 1993), and additional forms of 80, 150, 250 to 300, and > 300 kDa had the properties of intermediates in a transport and cell wall anchorage pathway. N glycosylation and additional modifications resulted in successive increases in size during transport. The 150- and 250- to 300-kDa forms were membrane associated and are likely to be intermediates between the 140-kDa form and a cell surface GPI-anchored form of > 300 kDa. A soluble form of > 300 kDa that lacked the GPI anchor had properties of a periplasmic intermediate between the plasma membrane form and the > 300-kDa cell wall-anchored form. These results constitute experimental support for the hypothesis that GPI anchors act to localize alpha-agglutinin to the plasma membrane and that cell wall anchorage involves release from the GPI anchor to produce a periplasmic intermediate followed by linkage to the cell wall.

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