scholarly journals Cellular distribution, regulation, and biochemical nature of an Fc alpha receptor in humans.

1990 ◽  
Vol 171 (3) ◽  
pp. 597-613 ◽  
Author(s):  
R C Monteiro ◽  
H Kubagawa ◽  
M D Cooper
Keyword(s):  
Cell Lines ◽  
Receptor Expression ◽  
Cell Surface Receptor ◽  
Ligand Specificity ◽  
Transmembrane Glycoprotein ◽  
Human Granulocytes ◽  
Surface Receptor ◽  
Igg Receptors ◽  
Monocyte Cell ◽  
Distinctive Role

In these studies, we characterize an Fc receptor (FcR) for IgA that is present on human granulocytes, monocyte/macrophages, and their corresponding cell lines. Receptor expression appears to be constitutive but can be selectively upregulated on monocyte cell lines by stimulation with a phorbol ester and polymeric IgA. Both the induction requirements and ligand specificity of the IgA receptor differ from the IgG receptors, Fc gamma R I, II, and III, that are also expressed on monocytes and granulocytes. IgA binding to the cell surface receptor is mediated via the Fc alpha region. The Fc alpha R is a heterogenously charged, approximately 60-kD molecule with an isoelectric point of 4.5-5.6 that binds monomeric or polymeric IgA1 and IgA2 molecules. This transmembrane glycoprotein appears to be composed of 32- and 36-kD protein cores with multiple N-linked carbohydrate moieties. We conclude that this Fc alpha R represents a novel member of the FcR family that may have a distinctive role in host defense.

scholarly journals Porcine Breast Extracellular Matrix Hydrogel for Spatial Tissue Culture

2018 ◽  
Vol 19 (10) ◽  
pp. 2912 ◽  
Author(s):  
Girdhari Rijal ◽  
Jing Wang ◽  
Ilhan Yu ◽  
David Gang ◽  
Roland Chen ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Human Mammary Epithelial Cell ◽  
Tumor Formation ◽  
Receptor Expression ◽  
Cell Surface Receptor ◽  
Breast Diseases ◽  
Porous Scaffolds ◽  
Ecm Proteins ◽  
Surface Receptor

Porcine mammary fatty tissues represent an abundant source of natural biomaterial for generation of breast-specific extracellular matrix (ECM). Here we report the extraction of total ECM proteins from pig breast fatty tissues, the fabrication of hydrogel and porous scaffolds from the extracted ECM proteins, the structural properties of the scaffolds (tissue matrix scaffold, TMS), and the applications of the hydrogel in human mammary epithelial cell spatial cultures for cell surface receptor expression, metabolomics characterization, acini formation, proliferation, migration between different scaffolding compartments, and in vivo tumor formation. This model system provides an additional option for studying human breast diseases such as breast cancer.

scholarly journals Drebrin 1 in dendritic cells regulates phagocytosis and cell surface receptor expression through recycling for efficient antigen presentation

Immunology ◽  
2018 ◽  
Vol 156 (2) ◽  
pp. 136-146 ◽  
Author(s):  
Diana M. Elizondo ◽  
Temesgen E. Andargie ◽  
Naomi L. Haddock ◽  
Thomas A. Boddie ◽  
Michael W. Lipscomb
Keyword(s):  
Dendritic Cells ◽  
Cell Surface ◽  
Antigen Presentation ◽  
Receptor Expression ◽  
Cell Surface Receptor ◽  
Surface Receptor

scholarly journals Selective inhibition of the growth of human erythroid bursts by monoclonal antibodies against transferrin or the transferrin receptor

Blood ◽  
1986 ◽  
Vol 67 (6) ◽  
pp. 1631-1638 ◽  
Author(s):  
KM Shannon ◽  
JW Larrick ◽  
SA Fulcher ◽  
KB Burck ◽  
J Pacely ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Transferrin Receptor ◽  
Thymidine Incorporation ◽  
Selective Inhibition ◽  
Receptor Expression ◽  
Cell Surface Receptor ◽  
Transferrin Receptors ◽  
Human Erythropoietin ◽  
Surface Receptor ◽  
Transferrin Receptor Expression

Abstract The relative requirements of colonies derived from erythroid (BFU-E) and myeloid (CFU-c) progenitors for transferrin were examined using monoclonal antibodies directed against the transferrin molecule (TF-6) or its cell surface receptor (TFR-A12, TFR1–2B). Growth of erythroid bursts was profoundly reduced at concentrations of all three antibodies that had no effect on CFU-c-derived colonies. When TFR1–2B was layered over cultures established one to seven days previously, further burst development was inhibited, and degeneration of early erythroid colonies was observed. Addition of erythropoietin augmented transferrin receptor expression on cells harvested after 1 to 2 weeks in culture and analyzed by flow cytometry. Recombinant human erythropoietin gave results comparable to those obtained in experiments using human urinary erythropoietin. Analysis of erythroblasts plucked directly from culture plates confirmed the presence of transferrin receptors on BFU-E-derived colonies. Thymidine incorporation was maximal early in the second week of culture and coincided with high transferrin receptor expression. These data demonstrate that transferrin must be available into the second week of culture to support the growth and differentiation of BFU- E-derived erythroid bursts, that the generation of erythroid colonies from BFU-E is more dependent on transferrin than myeloid colony formation from CFU-c, and that erythropoietin modulates the expression of transferrin receptors on growing bursts.

MONOCYTE CELL SURFACE RECEPTOR UPREGULATION IN RESPONSE TO STIMULATION WITH LIPOPOLYSACCHARIDE AND PEPTIDOGLYCAN

Shock ◽  
2004 ◽  
Vol 21 (Supplement) ◽  
pp. 21
Author(s):  
J S HADLEY ◽  
J E WANG ◽  
S J FOSTER ◽  
C THIEMERMANN ◽  
C J HINDS
Keyword(s):  
Cell Surface ◽  
Cell Surface Receptor ◽  
Surface Receptor ◽  
Monocyte Cell ◽  
Receptor Upregulation

Increased cell-surface receptor expression on U-937 cells induced by 1-O-octadecyl-2-O-methyl-sn-glycero-3-phosphocholine

2000 ◽  
Vol 48 (10) ◽  
pp. 569-578 ◽  
Author(s):  
Marina Y. Pushkareva ◽  
Sharon L. Wannberg ◽  
Andrew S. Janoff ◽  
Eric Mayhew
Keyword(s):  
Cell Surface ◽  
Receptor Expression ◽  
Cell Surface Receptor ◽  
Surface Receptor

scholarly journals Identification of Molecular Phenotypes and Biased Signaling Induced by Naturally Occurring Mutations of the Human Calcium-Sensing Receptor

Endocrinology ◽  
2012 ◽  
Vol 153 (9) ◽  
pp. 4304-4316 ◽  
Author(s):  
Katie Leach ◽  
Adriel Wen ◽  
Anna E. Davey ◽  
Patrick M. Sexton ◽  
Arthur D Conigrave ◽  
...  
Keyword(s):  
Amino Acid ◽  
Receptor Expression ◽  
Cell Surface Receptor ◽  
Receptor Coupling ◽  
Calcium Sensing ◽  
Naturally Occurring ◽  
Molecular Determinant ◽  
Biased Signaling ◽  
Surface Receptor ◽  
Molecular Phenotypes

More than 200 naturally occurring mutations have been identified in the human CaSR, which have been linked to diseases involving dysregulation of extracellular Ca2+ homeostasis. These mutations have classically been termed “loss-” or “gain-of-function” mutations, which is an oversimplification given that amino acid changes can alter numerous molecular properties of a receptor. We thus sought to characterize the effects of 21 clinically relevant mutations, the majority located in the heptahelical domains and extracellular loop regions of the CaSR, using flow cytometry to measure cell surface receptor expression levels, and measurements of intracellular Ca2+ mobilization and ERK1/2 phosphorylation to monitor receptor signaling. We identified distinct molecular phenotypes caused by these naturally occurring amino acid substitutions, which included combinations of loss- and gain-of-expression and changes in intrinsic signaling capacity. Importantly, we also identified biased signaling in the response of the CaSR to different mutations across the two pathways, indicating that some mutations resulted in receptor conformations that differentially altered receptor-coupling preferences. These findings have important implications for understanding the causes of diseases linked to the CaSR. A full appreciation of the molecular effects of these amino acid changes may enable the development of therapeutics that specifically target the molecular determinant of impairment in the receptor.

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