The TolC protein of Escherichia coli serves as a cell-surface receptor for the newly characterized TLS bacteriophage 1 1Edited by B. Holland

2001 ◽  
Vol 308 (4) ◽  
pp. 579-585 ◽  
Author(s):  
Greg J German ◽  
Rajeev Misra
Keyword(s):  
Escherichia Coli ◽  
Cell Surface ◽  
Cell Surface Receptor ◽  
Surface Receptor ◽  
A Cell ◽  
Tolc Protein

P4-054: KLOTHO ENHANCES NEURONAL ACTIVITY THROUGH INTERACTION WITH A CELL-SURFACE RECEPTOR

2006 ◽  
Vol 14 (7S_Part_27) ◽  
pp. P1453-P1454
Author(s):  
Nicola J. Corbett ◽  
Kate Fisher ◽  
Helen A. Rowland ◽  
Alys C. Jones ◽  
Nigel M. Hooper
Keyword(s):  
Cell Surface ◽  
Neuronal Activity ◽  
Cell Surface Receptor ◽  
Surface Receptor ◽  
A Cell

230. Megalin, RAP and Nkx3.1 expression in the developing reproductive tract of a marsupial, the tammar wallaby

2008 ◽  
Vol 20 (9) ◽  
pp. 30
Author(s):  
M. Gamat ◽  
M. B. Renfree ◽  
A. J. Pask ◽  
G. Shaw
Keyword(s):  
Cell Surface ◽  
Reproductive Tract ◽  
Tammar Wallaby ◽  
Cell Surface Receptor ◽  
Urogenital Sinus ◽  
Receptor Associated Protein ◽  
Wide Range ◽  
Surface Receptor ◽  
A Cell ◽  
Strong Staining

Androgens induce the differentiation of the urogenital sinus (UGS) to form a prostate. An early marker of this response is upregulation of the transcription factor Nkx3.1 in the urogenital epithelium in the precursors of prostatic buds. In tammars, prostate differentiation begins ~3 weeks after birth and after the time the testis starts to secrete androgens, and 2 weeks after androgen stimulated Wolffian duct differentiation. The reason for this delay in prostate differentiation is unexplained. Androgen receptors are present in the UGS, and the potent androgen, androstanediol, induces prostatic development in females. Whilst androgens may diffuse into cells by across the cell membrane, there is increasing evidence that steroids are also internalised actively via the cell-surface transport molecule Megalin. We are exploring the possibility that the delay may be related to the establishment of a Megalin-mediated pathway. Megalin is a cell surface receptor expressed on epithelia and mediates the endocytosis of a wide range of ligands, including SHBG-bound sex steroids. Megalin action is regulated by Receptor Associated Protein (RAP), which acts as an antagonist to Megalin action. This study cloned partial sequences of Megalin, RAP and Nkx3.1 and examined their expression in the developing urogenital sinus of the tammar wallaby using RT–PCR. The cellular distribution of Megalin protein in the developing UGS was examined using immunohistochemistry. Megalin, RAP and Nkx3.1 in the tammar were all highly conserved with eutherian orthologueues. Megalin and Nkx3.1 transcripts were detected in the liver, kidney, ovary, testis and developing urogenital sinus of male and female tammars. In the developing UGS of the tammar, there was strong staining for Megalin protein in the urogenital epithelium with some diffuse staining in the surrounding mesenchyme. Together, these results suggest that Megalin could be a key gene in the mediation of androgen action in prostatic development in the tammar wallaby.

The T4 Glycoprotein Is a Cell-surface Receptor for the AIDS Virus

1986 ◽  
Vol 51 (0) ◽  
pp. 703-711 ◽  
Author(s):  
J.S. McDougal ◽  
P.J. Maddon ◽  
A.G. Dalgleish ◽  
P.R. Clapham ◽  
D.R. Littman ◽  
...  
Keyword(s):  
Cell Surface ◽  
Cell Surface Receptor ◽  
Aids Virus ◽  
Surface Receptor ◽  
A Cell

Membrane guanylate cyclase is a cell-surface receptor with homology to protein kinases

Nature ◽  
1988 ◽  
Vol 334 (6184) ◽  
pp. 708-712 ◽  
Author(s):  
Sujay Singh ◽  
David G. Lowe ◽  
David S. Thorpe ◽  
Henry Rodriguez ◽  
Wun-Jing Kuang ◽  
...  
Keyword(s):  
Cell Surface ◽  
Protein Kinases ◽  
Guanylate Cyclase ◽  
Cell Surface Receptor ◽  
Membrane Guanylate Cyclase ◽  
Surface Receptor ◽  
A Cell

scholarly journals Membrane Protein 4F2/CD98 Is a Cell Surface Receptor Involved in the Internalization and Trafficking of Human β-Defensin 3 in Epithelial Cells

2015 ◽  
Vol 22 (2) ◽  
pp. 217-228 ◽  
Author(s):  
Irene Colavita ◽  
Ersilia Nigro ◽  
Daniela Sarnataro ◽  
Olga Scudiero ◽  
Vincenzo Granata ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Membrane Protein ◽  
Cell Surface ◽  
Cell Surface Receptor ◽  
Surface Receptor ◽  
A Cell

scholarly journals Acting via a Cell Surface Receptor, Thyroid Hormone Is a Growth Factor for Glioma Cells

2006 ◽  
Vol 66 (14) ◽  
pp. 7270-7275 ◽  
Author(s):  
Faith B. Davis ◽  
Heng-Yuan Tang ◽  
Ai Shih ◽  
Travis Keating ◽  
Lawrence Lansing ◽  
...  
Keyword(s):  
Growth Factor ◽  
Thyroid Hormone ◽  
Cell Surface ◽  
Glioma Cells ◽  
Cell Surface Receptor ◽  
Surface Receptor ◽  
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.

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