Development and Characterization of a High-Throughput System for Assessing Cell-Surface Receptor−Ligand Engagement

Langmuir ◽  
2005 ◽  
Vol 21 (18) ◽  
pp. 8374-8384 ◽  
Author(s):  
G. M. Harbers ◽  
L. J. Gamble ◽  
E. F. Irwin ◽  
D. G. Castner ◽  
K. E. Healy
Keyword(s):  
Cell Surface ◽  
High Throughput ◽  
Cell Surface Receptor ◽  
Receptor Ligand ◽  
Surface Receptor

scholarly journals Synthesis of end-labeled multivalent ligands for exploring cell-surface-receptor–ligand interactions

2000 ◽  
Vol 7 (1) ◽  
pp. 9-16 ◽  
Author(s):  
Eva J Gordon ◽  
Jason E Gestwicki ◽  
Laura E Strong ◽  
Laura L Kiessling
Keyword(s):  
Cell Surface ◽  
Cell Surface Receptor ◽  
Receptor Ligand ◽  
Multivalent Ligands ◽  
Ligand Interactions ◽  
Surface Receptor

scholarly journals The Cell Surface Receptor CD44: NMR-Based Characterization of Putative Ligands

ChemMedChem ◽  
2016 ◽  
Vol 11 (10) ◽  
pp. 1097-1106 ◽  
Author(s):  
Carlo Baggio ◽  
Elisa Barile ◽  
Gianluigi Di Sorbo ◽  
Thomas J. Kipps ◽  
Maurizio Pellecchia
Keyword(s):  
Cell Surface ◽  
Cell Surface Receptor ◽  
Surface Receptor

scholarly journals Isolation of an adhesion-mediating protein from chick neural retina adherons.

1985 ◽  
Vol 101 (3) ◽  
pp. 1071-1077 ◽  
Author(s):  
D Schubert ◽  
M LaCorbiere
Keyword(s):  
Cell Surface ◽  
Heparan Sulfate ◽  
Cultured Cells ◽  
Cell Types ◽  
Neural Retina ◽  
Cell Surface Receptor ◽  
Isolation And Characterization ◽  
Surface Receptor ◽  
Adhesive Interactions

Adherons are high molecular weight glycoprotein complexes which are released into the growth medium of cultured cells. They mediate the adhesive interactions of many cell types, including those of embryonic chick neural retina. The cell surface receptor for chick neural retina adherons has been purified, and shown to be a heparan sulfate proteoglycan (Schubert, D., and M. LaCorbiere, 1985, J. Cell Biol., 100:56-63). This paper describes the isolation and characterization of a protein in neural retina adherons which interacts specifically with the cell surface receptor. The 20,000-mol-wt protein, called retinal purpurin (RP), stimulates neural retina cell-substratum adhesion and prolongs the survival of neural retina cells in culture. The RP protein interacts with heparin and heparan sulfate, but not with other glycosaminoglycans. Monovalent antibodies against RP inhibit RP-cell adhesion as well as adheron-cell interactions. The RP protein is found in neural retina, but not in other tissues such as brain and muscle. These data suggest that RP plays a role in both the survival and adhesive interactions of neural retina cells.

Characterization of the Strongylocentrotus Purpuratus Egg Cell Surface Receptor for Sperm

1986 ◽  
pp. 293-313 ◽  
Author(s):  
Norka Ruiz-Bravo ◽  
Daniel P. Rossignol ◽  
Glenn L. Decker ◽  
Lawrence I. Rosenberg ◽  
William J. Lennarz
Keyword(s):  
Cell Surface ◽  
Strongylocentrotus Purpuratus ◽  
Cell Surface Receptor ◽  
Egg Cell ◽  
Surface Receptor

scholarly journals Evidence that the thyrotropin-releasing hormone receptor and its ligand are recycled dissociated from each other

1995 ◽  
Vol 306 (1) ◽  
pp. 107-113 ◽  
Author(s):  
C P Petrou ◽  
A H Tashjian
Keyword(s):  
Cell Surface ◽  
Hormone Receptor ◽  
Thyrotropin Releasing Hormone ◽  
Cell Surface Receptor ◽  
Acidic Ph ◽  
Receptor Recycling ◽  
Bafilomycin A1 ◽  
Receptor Ligand ◽  
Surface Receptor ◽  
Receptor Pool

We have examined the trafficking of the thyrotropin-releasing hormone receptor (TRHR) and its ligand, after TRHR-TRH internalization in rat pituitary GH4C1 cells. After rapid ligand-induced receptor sequestration, the cell surface receptor pool was replenished. Replenishment was insensitive to inhibition of protein synthesis and was dependent on the duration of internalization; therefore, the replenished receptors were not newly synthesized but recycled. The total amount of recycled receptors decreased with increasing internalization time, resulting in only partial replenishment of the cell-surface receptor pool after prolonged incubation with ligand. Thus, in addition to a receptor recycling pathway, a non-cycling route exists for TRHR sorting; this route became dominant with increasing internalization periods. TRHR entry into these pathways was not determined by the affinity of the receptor-ligand interaction, because the extent of receptor recycling was similar after TRH- and methyl-TRH (MeTRH)-induced internalization. Unlike results with the TRHR, the TRH recycling pool was not depleted by the noncycling pathway. After multiple rounds of [3H]MeTRH internalization, the amount of cell-associated radioactivity increased with increasing internalization time due to accumulation of the ligand or its metabolites in a non-cycling pathway, but the absolute amount of recycled ligand remained constant after short or long internalization times. The difference in the proportion of TRHR and MeTRH that were diverted into a noncycling pathway indicated intracellular dissociation of the internalized TRHR-TRH complex. Dissociation of the internalized TRHR-TRH complex was dependent on the acidic pH in an intracellular compartment. Although extracellular acidic pH did not enhance cell-surface receptor-ligand (RL) dissociation, bafilomycin A1 inhibited both receptor and ligand recycling. We conclude that the TRHR-TRH system is unique among recycling receptors because, after RL sequestration, the TRHR-TRH complex becomes dissociated intracellularly via a bafilomycin A1-sensitive, acidic pH-dependent mechanism, and both the unoccupied TRHR and TRH recycle disassociated from each other.

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