scholarly journals Erratum: Corrigendum: Metabolic biotinylation of cell surface receptors for in vivo imaging

2006 ◽  
Vol 3 (8) ◽  
pp. 657-657
Author(s):  
Bakhos A Tannous ◽  
Jan Grimm ◽  
Katherine F Perry ◽  
John W Chen ◽  
Ralph Weissleder ◽  
...  
Keyword(s):  
Cell Surface ◽  
In Vivo Imaging ◽  
Cell Surface Receptors ◽  
Surface Receptors

Metabolic biotinylation of cell surface receptors for in vivo imaging

2006 ◽  
Vol 3 (5) ◽  
pp. 391-396 ◽  
Author(s):  
Bakhos A Tannous ◽  
Jan Grimm ◽  
Katherine F Perry ◽  
John W Chen ◽  
Ralph Weissleder ◽  
...  
Keyword(s):  
Cell Surface ◽  
In Vivo Imaging ◽  
Cell Surface Receptors ◽  
Surface Receptors

scholarly journals 1001. Metabolic Biotinylation of Cell Surface Receptors for In Vivo Imaging

2006 ◽  
Vol 13 ◽  
pp. S386
Author(s):  
Bakhos A. Tannous ◽  
Jan Grimm ◽  
Katherine F. Perry ◽  
John W. Chen ◽  
Weissleder Ralph ◽  
...  
Keyword(s):  
Cell Surface ◽  
In Vivo Imaging ◽  
Cell Surface Receptors ◽  
Surface Receptors

scholarly journals Redirecting Retroviral Tropism by Insertion of Short, Nondisruptive Peptide Ligands into Envelope

2002 ◽  
Vol 76 (7) ◽  
pp. 3558-3563 ◽  
Author(s):  
Timothy J. Gollan ◽  
Michael R. Green
Keyword(s):  
Cell Surface ◽  
Leukemia Virus ◽  
Envelope Proteins ◽  
Peptide Ligands ◽  
Viral Envelope ◽  
Moloney Murine Leukemia Virus ◽  
Cell Surface Receptors ◽  
Wild Type ◽  
Surface Receptors

ABSTRACT A potentially powerful approach for in vivo gene delivery is to target retrovirus to specific cells through interactions between cell surface receptors and appropriately modified viral envelope proteins. Previously, relatively large (>100 residues) protein ligands to cell surface receptors have been inserted at or near the N terminus of retroviral envelope proteins. Although viral tropism could be altered, the chimeric envelope proteins lacked full activity, and coexpression of wild-type envelope was required for production of transducing virus. Here we analyze more than 40 derivatives of ecotropic Moloney murine leukemia virus (MLV) envelope, containing insertions of short RGD-containing peptides, which are ligands for integrin receptors. In many cases pseudotyped viruses containing only the chimeric envelope protein could transduce human cells. The precise location, size, and flanking sequences of the ligand affected transduction specificity and efficiency. We conclude that retroviral tropism can be rationally reengineered by insertion of short peptide ligands and without the need to coexpress wild-type envelope.

scholarly journals Sulfated polysaccharides identified as inducers of neuropilin-1 internalization and functional inhibition of VEGF165 and semaphorin3A

Blood ◽  
2008 ◽  
Vol 111 (8) ◽  
pp. 4126-4136 ◽  
Author(s):  
Masashi Narazaki ◽  
Marta Segarra ◽  
Giovanna Tosato
Keyword(s):  
Cell Surface ◽  
Dextran Sulfate ◽  
Receptor Internalization ◽  
Sulfated Polysaccharides ◽  
Cell Surface Receptors ◽  
Ligand Interaction ◽  
Surface Receptors ◽  
Neuropilin 1

Abstract Neuropilin-1 (NRP1) and NRP2 are cell surface receptors shared by class 3 semaphorins and vascular endothelial growth factor (VEGF). Ligand interaction with NRPs selects the specific signal transducer, plexins for semaphorins or VEGF receptors for VEGF, and promotes NRP internalization, which effectively shuts down receptor-mediated signaling by a second ligand. Here, we show that the sulfated polysaccharides dextran sulfate and fucoidan, but not others, reduce endothelial cell-surface levels of NRP1, NRP2, and to a lesser extent VEGFR-1 and VEGFR-2, and block the binding and in vitro function of semaphorin3A and VEGF165. Administration of fucoidan to mice reduces VEGF165-induced angiogenesis and tumor neovascularization in vivo. We find that dextran sulfate and fucoidan can bridge the extracellular domain of NRP1 to that of the scavenger receptor expressed by endothelial cells I (SREC-I), and induce NRP1 and SREC-I coordinate internalization and trafficking to the lysosomes. Overexpression of SREC-I in SREC-I–negative cells specifically reduces cell-surface levels of NRP1, indicating that SREC-I mediates NRP1 internalization. These results demonstrate that engineered receptor internalization is an effective strategy for reducing levels and function of cell-surface receptors, and identify certain sulfated polysaccharides as “internalization inducers.”

In Vivo Internalization of the Somatostatin sst2A Receptor in Rat Brain: Evidence for Translocation of Cell-Surface Receptors into the Endosomal Recycling Pathway

2001 ◽  
Vol 17 (4) ◽  
pp. 646-661 ◽  
Author(s):  
Zsolt Csaba ◽  
Véronique Bernard ◽  
Lone Helboe ◽  
Marie-Thérèse Bluet-Pajot ◽  
Bertrand Bloch ◽  
...  
Keyword(s):  
Cell Surface ◽  
Rat Brain ◽  
Cell Surface Receptors ◽  
Surface Receptors ◽  
Endosomal Recycling ◽  
Recycling Pathway

scholarly journals Membrane-Tethered Ligands: Tools for Cell-Autonomous Pharmacological Manipulation of Biological Circuits

Physiology ◽  
2013 ◽  
Vol 28 (3) ◽  
pp. 164-171 ◽  
Author(s):  
Charles Choi ◽  
Michael N. Nitabach
Keyword(s):  
Cell Surface ◽  
Biological Significance ◽  
Cell Surface Receptors ◽  
Surface Receptors ◽  
Membrane Tethering ◽  
A Cell ◽  
Cellular Circuits ◽  
Communication Pathway ◽  
Tethered Ligands

Detection of secreted signaling molecules by cognate cell surface receptors is a major intercellular communication pathway in cellular circuits that control biological processes. Understanding the biological significance of these connections would allow us to understand how cellular circuits operate as a whole. Membrane-tethered ligands are recombinant transgenes with structural modules that allow them to act on cell-surface receptors and ion channel subtypes with pharmacological specificity in a cell-autonomous manner. Membrane-tethered ligands have been successful in the specific manipulation of ion channels as well as G-protein-coupled receptors, and, in combination with cell-specific promoters, such manipulations have been restricted to genetically defined subpopulations within cellular circuits in vivo to induce specific phenotypes controlled by those circuits. These studies establish the membrane-tethering approach as a generally applicable method for dissecting neural and physiological circuits.

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