scholarly journals Expression cloning of a human Fc receptor for IgA.

1990 ◽  
Vol 172 (6) ◽  
pp. 1665-1672 ◽  
Author(s):  
C R Maliszewski ◽  
C J March ◽  
M A Schoenborn ◽  
S Gimpel ◽  
L Shen
Keyword(s):  
Cell Surface ◽  
Myeloid Cell ◽  
Expression Cloning ◽  
Immunoglobulin Gene ◽  
Cell Surface Molecule ◽  
Immune Effector ◽  
Surface Receptors ◽  
Molecular Features ◽  
Myeloid Cell Line ◽  
A Cell

IgA, the predominant isotype in secretions, mediates the neutralization and removal of environmental antigens from mucosal sites. Although cell surface receptors for the Fc region of IgA (Fc alpha R) have been implicated in a variety of immune effector mechanisms, the molecular features of Fc alpha R remain only marginally characterized. In this report, we describe the isolation of a clone from a myeloid cell line cDNA library that directs the expression of a cell surface molecule with IgA binding specificity. The cDNA encodes a peptide of Mr 30,000 including a putative transmembrane region with features atypical of conventional membrane-anchored proteins. Databank searches indicate that the human myeloid cell Fc alpha R sequence is unique, is a member of the immunoglobulin gene superfamily, and is related to Fc receptors for IgG (Fc gamma RI, II, and III) and IgE (Fc epsilon RI).

scholarly journals A generic cell surface ligand system for studying cell-cell recognition

2019 ◽  
Author(s):  
Eleanor M Denham ◽  
Michael I Barton ◽  
Susannah M Black ◽  
Marcus J Bridge ◽  
Ben de Wet ◽  
...  
Keyword(s):  
Cell Surface ◽  
Surface Density ◽  
Cell Receptor ◽  
Surface Receptors ◽  
Ligand System ◽  
Ligand Interactions ◽  
A Cell ◽  
Surface Ligand ◽  
Receptor Biology ◽  
Cell Cell

AbstractDose-response experiments are a mainstay of receptor biology studies and can reveal valuable insights into receptor function. Such studies of receptors that bind cell surface ligands are currently limited by the difficulty in manipulating the surface density of ligands at a cell-cell interface. Here we describe a generic cell surface ligand system that allows precise manipulation of cell surface ligand densities over several orders of magnitude. We validate the system for a range of immunoreceptors, including the T cell receptor (TCR), and show that this generic ligand stimulates via the TCR at a similar surface density as its native ligand. This system allows the effect of surface density, valency, dimensions, and affinity of the ligand to be manipulated. It can be readily extended to other receptor-cell surface ligand interactions, and will facilitate investigation into the activation of, and signal integration between, cell surface receptors.

PECAM-1 functions as a specific and potent inhibitor of mitochondrial-dependent apoptosis

Blood ◽  
2003 ◽  
Vol 102 (1) ◽  
pp. 169-179 ◽  
Author(s):  
Cunji Gao ◽  
Weiyong Sun ◽  
Melpo Christofidou-Solomidou ◽  
Motoshi Sawada ◽  
Debra K. Newman ◽  
...  
Keyword(s):  
Cell Surface ◽  
Immunoglobulin Gene ◽  
Vascular Cells ◽  
Cytochrome C Release ◽  
Homophilic Binding ◽  
Environmental Signals ◽  
Surface Receptors ◽  
Naturally Occurring ◽  
Platelet Endothelial Cell Adhesion ◽  
Cell Adhesion Molecule 1

Abstract Programmed cell death, or apoptosis, is a tightly regulated, naturally occurring process by which damaged or unwanted cells are removed. Dysregulated apoptosis has been implicated in a variety of pathophysiological conditions, including degenerative diseases, tissue remodeling, and tumorogenesis. The decision to live or die results from integration of numerous environmental signals transmitted by specific classes of cell surface receptors that bind hormones, growth factors, or components of the extracellular matrix. Here we show that platelet endothelial cell adhesion molecule-1 (PECAM-1), a homophilic-binding member of the immunoreceptor tyrosine-based inhibitory motif (ITIM) family of inhibitory receptors, functions prominently to inhibit apoptosis in naturally occurring vascular cells subjected to apoptotic stimuli. Murine endothelial cells and human T lymphocytes lacking PECAM-1 were found to be far more sensitive than their PECAM-1—expressing counterparts to multiple death signals that stimulate Bax, a multidomain, proapoptotic member of the Bcl-2 family that plays a central role in mitochondrial dysfunction-dependent apoptosis. In addition, PECAM-1 markedly suppressed Bax overexpression—induced cytochrome c release, caspase activation, and nuclear fragmentation. Amino acid substitutions within PECAM-1's extracellular homophilic binding domain, or within its cytoplasmic ITIM, completely abolished PECAM-1—mediated cytoprotection. Taken together, these data implicate PECAM-1 as a novel and potent suppressor of Bax-mediated apoptosis and suggest that members of the immunoglobulin gene (Ig) superfamily, like cell surface integrins, may also transmit survival signals into blood and vascular cells. (Blood. 2003;102:169-179)

scholarly journals A cell surface molecule, JL1; a specific target for diagnosis and treatment of leukemias

Leukemia ◽  
1998 ◽  
Vol 12 (10) ◽  
pp. 1583-1590 ◽  
Author(s):  
WS Park ◽  
YM Bae ◽  
DH Chung ◽  
TJ Kim ◽  
EY Choi ◽  
...  
Keyword(s):  
Cell Surface ◽  
Diagnosis And Treatment ◽  
Surface Molecule ◽  
Cell Surface Molecule ◽  
Specific Target ◽  
A Cell

scholarly journals Intracellular movement of cell surface receptors after endocytosis: resialylation of asialo-transferrin receptor in human erythroleukemia cells.

1985 ◽  
Vol 100 (3) ◽  
pp. 826-834 ◽  
Author(s):  
M D Snider ◽  
O C Rogers
Keyword(s):  
Sialic Acid ◽  
Cell Surface ◽  
Golgi Complex ◽  
Transferrin Receptor ◽  
Cell Surface Receptor ◽  
Surface Receptors ◽  
Erythroleukemia Cells ◽  
Intracellular Movement ◽  
Surface Receptor ◽  
A Cell

The intracellular movement of cell surface transferrin receptor (TfR) after internalization was studied in K562 cultured human erythroleukemia cells. The sialic acid residues of the TfR glycoprotein were used to monitor transport to the Golgi complex, the site of sialyltransferases. Surface-labeled cells were treated with neuraminidase, and readdition of sialic acid residues, monitored by isoelectric focusing of immunoprecipitated TfR, was used to assess the movement of receptor to sialyltransferase-containing compartments. Asialo-TfR was resialylated by the cells with a half-time of 2-3 h. Resialylation occurred in an intracellular organelle, since it was inhibited by treatments that allow internalization of surface components but block transfer out of the endosomal compartment. Moreover, roughly half of the resialylated molecules were cleaved when cells were retreated with neuraminidase after culturing, indicating that this fraction of the molecules had returned to the cell surface. These results suggest that TfR is transported from the cell surface to the Golgi complex, the intracellular site of sialyltransferases, and then returns to the cell surface. This pathway, which has not been previously described for a cell surface receptor, may be different from the route followed by TfR in iron uptake, since reported rates of transferrin uptake and release are significantly more rapid than the resialylation of asialo-TfR.

scholarly journals May the Odds Be Ever in Your Favor: Non-deterministic Mechanisms Diversifying Cell Surface Molecule Expression

2022 ◽  
Vol 9 ◽  
Author(s):  
Donnell L. Williams ◽  
Veronica Maria Sikora ◽  
Max A. Hammer ◽  
Sayali Amin ◽  
Taema Brinjikji ◽  
...  
Keyword(s):  
Cell Surface ◽  
Molecular Mechanisms ◽  
Antigenic Variation ◽  
The Body ◽  
Allelic Exclusion ◽  
Coat Proteins ◽  
Cell Surface Molecule ◽  
Strand Breaks ◽  
Surface Receptors ◽  
Molecular Noise

How does the information in the genome program the functions of the wide variety of cells in the body? While the development of biological organisms appears to follow an explicit set of genomic instructions to generate the same outcome each time, many biological mechanisms harness molecular noise to produce variable outcomes. Non-deterministic variation is frequently observed in the diversification of cell surface molecules that give cells their functional properties, and is observed across eukaryotic clades, from single-celled protozoans to mammals. This is particularly evident in immune systems, where random recombination produces millions of antibodies from only a few genes; in nervous systems, where stochastic mechanisms vary the sensory receptors and synaptic matching molecules produced by different neurons; and in microbial antigenic variation. These systems employ overlapping molecular strategies including allelic exclusion, gene silencing by constitutive heterochromatin, targeted double-strand breaks, and competition for limiting enhancers. Here, we describe and compare five stochastic molecular mechanisms that produce variety in pathogen coat proteins and in the cell surface receptors of animal immune and neuronal cells, with an emphasis on the utility of non-deterministic variation.

scholarly journals Signaling Enzymes and Ion Channels Being Modulated by the Actin Cytoskeleton at the Plasma Membrane

2021 ◽  
Vol 22 (19) ◽  
pp. 10366
Author(s):  
Filip Vasilev ◽  
Yulia Ezhova ◽  
Jong Tai Chun
Keyword(s):  
Ion Channels ◽  
Cell Surface ◽  
Actin Cytoskeleton ◽  
Animal Species ◽  
Wide Spectrum ◽  
Cell Types ◽  
Fine Tuning ◽  
Signaling Proteins ◽  
Surface Receptors ◽  
A Cell

A cell should deal with the changing external environment or the neighboring cells. Inevitably, the cell surface receives and transduces a number of signals to produce apt responses. Typically, cell surface receptors are activated, and during this process, the subplasmalemmal actin cytoskeleton is often rearranged. An intriguing point is that some signaling enzymes and ion channels are physically associated with the actin cytoskeleton, raising the possibility that the subtle changes of the local actin cytoskeleton can, in turn, modulate the activities of these proteins. In this study, we reviewed the early and new experimental evidence supporting the notion of actin-regulated enzyme and ion channel activities in various cell types including the cells of immune response, neurons, oocytes, hepatocytes, and epithelial cells, with a special emphasis on the Ca2+ signaling pathway that depends on the synthesis of inositol 1,4,5-trisphosphate. Some of the features that are commonly found in diverse cells from a wide spectrum of the animal species suggest that fine-tuning of the activities of the enzymes and ion channels by the actin cytoskeleton may be an important strategy to inhibit or enhance the function of these signaling proteins.

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