A novel immunoglobulin superfamily receptor (19A) related to CD2 is expressed on activated lymphocytes and promotes homotypic B-cell adhesion

2002 ◽  
Vol 361 (3) ◽  
pp. 431-436 ◽  
Author(s):  
John J. MURPHY ◽  
Paul HOBBY ◽  
Juan VILARINO-VARELA ◽  
Benjamin BISHOP ◽  
Panagiota IORDANIDOU ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
B Cell ◽  
Molecular Model ◽  
Immunoglobulin Superfamily ◽  
Activated Lymphocytes ◽  
Lymphocyte Adhesion ◽  
Cell Line Model ◽  
Specific Immunoglobulin ◽  
Immunoglobulin Superfamily Protein

A novel lymphocyte-specific immunoglobulin superfamily protein (19A) has been cloned. The predicted 335-amino-acid sequence of 19A represents a Type 1 membrane protein with homology with the CD2 family of receptors. A molecular model of the two predicted extracellular immunoglobulin-like domains of 19A has been generated using the crystal structure of CD2 as a template. In isolated lymphocytes, expression of 19A is induced by various activation stimuli, and enforced expression of the 19A gene promotes homotypic cell adhesion in a B-cell-line model. Collectively these data imply that the 19A protein plays a role in regulation of lymphocyte adhesion.

scholarly journals A novel immunoglobulin superfamily receptor (19A) related to CD2 is expressed on activated lymphocytes and promotes homotypic B-cell adhesion

2002 ◽  
Vol 361 (3) ◽  
pp. 431 ◽  
Author(s):  
John J. MURPHY ◽  
Paul HOBBY ◽  
Juan VILARINO-VARELA ◽  
Benjamin BISHOP ◽  
Panagiota IORDANIDOU ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
B Cell ◽  
Immunoglobulin Superfamily ◽  
Activated Lymphocytes

scholarly journals CD22, a B cell-specific immunoglobulin superfamily member, is a sialic acid-binding lectin.

1993 ◽  
Vol 268 (10) ◽  
pp. 7011-7018
Author(s):  
D. Sgroi ◽  
A. Varki ◽  
S. Braesch-Andersen ◽  
I. Stamenkovic
Keyword(s):  
Sialic Acid ◽  
B Cell ◽  
Immunoglobulin Superfamily ◽  
Sialic Acid Binding ◽  
Specific Immunoglobulin ◽  
Binding Lectin

scholarly journals Distinct Roles of ICOS and CD40L in Human T-B Cell Adhesion and Antibody Production

2021 ◽  
pp. 104420
Author(s):  
Zhicui Liu ◽  
Shuai Liu ◽  
Yan Zhang ◽  
Weihong Zeng ◽  
Shujun Wang ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
B Cell ◽  
Antibody Production

scholarly journals Cell surface anchorage and ligand-binding domains of the Saccharomyces cerevisiae cell adhesion protein alpha-agglutinin, a member of the immunoglobulin superfamily.

1993 ◽  
Vol 13 (4) ◽  
pp. 2554-2563 ◽  
Author(s):  
D Wojciechowicz ◽  
C F Lu ◽  
J Kurjan ◽  
P N Lipke
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Adhesion ◽  
Amino Acid ◽  
Cell Surface ◽  
Consensus Sequence ◽  
Binding Domain ◽  
Immunoglobulin Superfamily ◽  
Cell Contact ◽  
Amino Acid Residues ◽  
Adhesion Proteins

alpha-Agglutinin is a cell adhesion glycoprotein expressed on the cell wall of Saccharomyces cerevisiae alpha cells. Binding of alpha-agglutinin to its ligand a-agglutinin, expressed by a cells, mediates cell-cell contact during mating. Analysis of truncations of the 650-amino-acid alpha-agglutinin structural gene AG alpha 1 delineated functional domains of alpha-agglutinin. Removal of the C-terminal hydrophobic sequence allowed efficient secretion of the protein and loss of cell surface attachment. This cell surface anchorage domain was necessary for linkage to a glycosyl phosphatidylinositol anchor. A construct expressing the N-terminal 350 amino acid residues retained full a-agglutinin-binding activity, localizing the binding domain to the N-terminal portion of alpha-agglutinin. A 278-residue N-terminal peptide was inactive; therefore, the binding domain includes residues between 278 and 350. The segment of alpha-agglutinin between amino acid residues 217 and 308 showed significant structural and sequence similarity to a consensus sequence for immunoglobulin superfamily variable-type domains. The similarity of the alpha-agglutinin-binding domain to mammalian cell adhesion proteins suggests that this structure is a highly conserved feature of adhesion proteins in diverse eukaryotes.

scholarly journals Changes in J chain and mu chain RNA expression as a function of B cell differentiation.

1984 ◽  
Vol 160 (3) ◽  
pp. 877-892 ◽  
Author(s):  
G Lamson ◽  
M E Koshland
Keyword(s):  
B Cell ◽  
Time Course ◽  
Rna Synthesis ◽  
Rna Expression ◽  
B Cell Differentiation ◽  
Activated Lymphocytes ◽  
J Chain ◽  
Pattern Characteristic ◽  
Kinetics Of ◽  
Lymphoid Cell Lines

The time course of differentiative events in the pentamer IgM response was examined by following the expression of J chain and mu chain RNA and their protein products in mitogen-stimulated lymphocytes. The analyses showed that the shift to mus RNA synthesis begins shortly after stimulation and precedes proliferation of the cells and any increase in mu RNA levels. In contrast, expression of J chain RNA and the amplification of J chain and mus message are late events that coincide with a phase of rapid proliferation and with the secretion of pentamer IgM antibody. The kinetics of J and mu chain RNA expression observed in normal lymphocytes were supported by analyses of lymphoid cell lines. B lymphomas were found to display the RNA pattern characteristic of early-activated lymphocytes, i.e., a partial shift to mus RNA production and no J chain RNA, whereas IgM-secreting lines resembled late-activated lymphocytes in their expression of high levels of both mus and J chain mRNA. Moreover, the kinetics of J and mus chain RNA expression correlates with the sequential action of B cell lymphokines in the induction of the pentamer IgM response. This correlation suggests that the successive differentiative changes are triggered by successive membrane stimuli.

scholarly journals Human immunodeficiency virus type-1 induces a regulatory B cell-like phenotype in vitro

2017 ◽  
Vol 15 (10) ◽  
pp. 917-933 ◽  
Author(s):  
Jacobo Lopez-Abente ◽  
Adrián Prieto-Sanchez ◽  
Maria-Ángeles Muñoz-Fernandez ◽  
Rafael Correa-Rocha ◽  
Marjorie Pion
Keyword(s):  
Human Immunodeficiency Virus ◽  
B Cell ◽  
Human Immunodeficiency Virus Type ◽  
Virus Type ◽  
Regulatory B Cell ◽  
Immunodeficiency Virus

scholarly journals A single antigen-specific B cell can conjugate to either a type 1 or a type 2 helper T cell.

1988 ◽  
Vol 85 (20) ◽  
pp. 7724-7728 ◽  
Author(s):  
V. M. Sanders ◽  
R. Fernandez-Botran ◽  
R. L. Coffman ◽  
T. R. Mosmann ◽  
E. S. Vitetta
Keyword(s):  
T Cell ◽  
B Cell ◽  
Helper T Cell ◽  
Single Antigen

scholarly journals Paracrine Regulation of Germinal Center B Cell Adhesion through the c-Met–Hepatocyte Growth Factor/Scatter Factor Pathway

1997 ◽  
Vol 185 (12) ◽  
pp. 2121-2131 ◽  
Author(s):  
Robbert van der Voort ◽  
Taher E.I. Taher ◽  
Robert M.J. Keehnen ◽  
Lia Smit ◽  
Martijn Groenink ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
T Cell ◽  
B Cells ◽  
Growth Factor ◽  
Hepatocyte Growth Factor ◽  
Tyrosine Kinase ◽  
B Cell ◽  
Germinal Center ◽  
Scatter Factor ◽  
Hepatocyte Growth

T cell–dependent humoral immune responses are initiated by the activation of naive B cells in the T cell areas of the secondary lymphoid tissues. This primary B cell activation leads to migration of germinal center (GC) cell precursors into B cell follicles where they engage follicular dendritic cells (FDC) and T cells, and differentiate into memory B cells or plasma cells. Both B cell migration and interaction with FDC critically depend on integrin-mediated adhesion. To date, the physiological regulators of this adhesion were unkown. In the present report, we have identified the c-met–encoded receptor tyrosine kinase and its ligand, the growth and motility factor hepatocyte growth factor/scatter factor (HGF/SF), as a novel paracrine signaling pathway regulating B cell adhesion. We observed that c-Met is predominantly expressed on CD38+CD77+ tonsillar B cells localized in the dark zone of the GC (centroblasts). On tonsil B cells, ligation of CD40 by CD40-ligand, induces a transient strong upregulation of expression of the c-Met tyrosine kinase. Stimulation of c-Met with HGF/SF leads to receptor phosphorylation and, in addition, to enhanced integrin-mediated adhesion of B cells to both VCAM-1 and fibronectin. Importantly, the c-Met ligand HGF/SF is produced at high levels by tonsillar stromal cells thus providing signals for the regulation of adhesion and migration within the lymphoid microenvironment.

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