scholarly journals Endocytic Delivery of Vancomycin Mediated by a Synthetic Cell Surface Receptor:  Rescue of Bacterially Infected Mammalian Cells and Tissue Targeting In Vivo

2007 ◽  
Vol 129 (2) ◽  
pp. 268-269 ◽  
Author(s):  
Siwarutt Boonyarattanakalin ◽  
Jianfang Hu ◽  
Sheryl A. Dykstra-Rummel ◽  
Avery August ◽  
Blake R. Peterson
Keyword(s):  
Cell Surface ◽  
Mammalian Cells ◽  
Cell Surface Receptor ◽  
Synthetic Cell ◽  
Tissue Targeting ◽  
Surface Receptor

scholarly journals Neuropilin-1 and heparan sulfate proteoglycans cooperate in cellular uptake of nanoparticles functionalized by cationic cell-penetrating peptides

2015 ◽  
Vol 1 (10) ◽  
pp. e1500821 ◽  
Author(s):  
Hong-Bo Pang ◽  
Gary B. Braun ◽  
Erkki Ruoslahti
Keyword(s):  
Cell Surface ◽  
Heparan Sulfate ◽  
Vascular Permeability ◽  
Mammalian Cells ◽  
Cell Penetrating Peptides ◽  
Proteolytic Processing ◽  
Cell Surface Receptor ◽  
Neuropilin 1 ◽  
Cell Penetrating ◽  
Surface Receptor

Cell-penetrating peptides (CPPs) have been widely used to deliver nanomaterials and other types of macromolecules into mammalian cells for therapeutic and diagnostic use. Cationic CPPs that bind to heparan sulfate (HS) proteoglycans on the cell surface induce potent endocytosis; however, the role of other surface receptors in this process is unclear. We describe the convergence of an HS-dependent pathway with the C-end rule (CendR) mechanism that enables peptide ligation with neuropilin-1 (NRP1), a cell surface receptor known to be involved in angiogenesis and vascular permeability. NRP1 binds peptides carrying a positive residue at the carboxyl terminus, a feature that is compatible with cationic CPPs, either intact or after proteolytic processing. We used CPP and CendR peptides, as well as HS- and NRP1-binding motifs from semaphorins, to explore the commonalities and differences of the HS and NRP1 pathways. We show that the CendR-NRP1 interaction determines the ability of CPPs to induce vascular permeability. We also show at the ultrastructural level, using a novel cell entry synchronization method, that both the HS and NRP1 pathways can initiate a macropinocytosis-like process and visualize these CPP-cargo complexes going through various endosomal compartments. Our results provide new insights into how CPPs exploit multiple surface receptor pathways for intracellular delivery.

scholarly journals Minireview: A Novel Pathway of Prostacyclin Signaling—Hanging Out with Nuclear Receptors

Endocrinology ◽  
2002 ◽  
Vol 143 (9) ◽  
pp. 3207-3210 ◽  
Author(s):  
Hyunjung Lim ◽  
Sudhansu K. Dey
Keyword(s):  
Cell Surface ◽  
Nuclear Receptors ◽  
Wide Spectrum ◽  
Binding Pocket ◽  
Cell Surface Receptor ◽  
Lipoxygenase Pathway ◽  
Signaling Mechanism ◽  
Recent Developments ◽  
Surface Receptor

Abstract Prostacylin (PGI2), one of the major prostaglandins, is derived from arachidonic acid by the action of the cyclooxygenase (COX) system coupled to PGI2 synthase (PGIS). The presence of the COX-2/PGIS at the nuclear and endoplasmic reticular membrane suggests differential signaling pathways of PGI2 actions involving both cell surface and nuclear receptors. Although the signaling of PGI2 via its cell surface receptor, prostacyclin receptor (IP), is well documented in vascular biology, its action via nuclear receptors in other physiological responses is gradually being more appreciated. Peroxisomal proliferator-activated receptors (PPARs), PPARα, PPARγ, and PPARδ, though initially cloned as a family of orphan receptors, are now known for their ligand promiscuity. The ligands range from free fatty acids and their derivatives produced by the cyclooxygenase or lipoxygenase pathway to certain hypolipidemic drugs. The predisposition of PPARs to use a wide spectrum of ligands is well explained by their unusually large ligand-binding pocket. The promiscuous ligand usage by PPARs is also reflected by their involvement in various pathophysiological events. Several recent independent reports show that endogenously produced PGI2 indeed activates PPARδ in vivo, indicating that a novel signaling mechanism for this abundant eicosanoid is operative in certain systems. This review attempts to cover recent developments in nuclear actions of PGI2 in diverse biological functions.

scholarly journals Specific Capture of Mammalian Cells by Cell Surface Receptor Binding to Ligand Immobilized on Gold Thin Films

2006 ◽  
Vol 5 (7) ◽  
pp. 1580-1585 ◽  
Author(s):  
Dora Peelen ◽  
Voula Kodoyianni ◽  
Jieun Lee ◽  
Ting Zheng ◽  
Michael R. Shortreed ◽  
...  
Keyword(s):  
Thin Films ◽  
Cell Surface ◽  
Receptor Binding ◽  
Mammalian Cells ◽  
Cell Surface Receptor ◽  
Surface Receptor ◽  
Gold Thin Films

scholarly journals Effect of hyaluronic acid on neutrophil adhesion

1981 ◽  
Vol 50 (1) ◽  
pp. 329-344
Author(s):  
J.V. Forrester ◽  
J.M. Lackie
Keyword(s):  
Cell Surface ◽  
Neutrophil Migration ◽  
Interfacial Free Energy ◽  
Cell Surface Receptor ◽  
Neutrophil Adhesion ◽  
Physical Factors ◽  
Surface Receptor ◽  
Neutrophil Aggregation ◽  
Dose Dependent

The effects of hyaluronate on rabbit neutrophil adhesion were studied using a variety of techniques. Exogenous hyaluronate inhibited neutrophil aggregation under conditions of both turbulent flow and constant shear rate. Hyaluronate also inhibited neutrophil adhesion to glass. Inhibition was dose-dependent above 100 micrograms ml-1 and a minimum molecular weight for hyaluronate of 1 × 10(4) was required. These effects were not simply the result of increased bulk viscosity of the hyaluronate-containing medium, nor did they appear to be mediated by putative cell-surface receptor mechanisms. Instead, physical factors such as hindrance and/or changes in the interfacial free-energy exchange at the cell surface due to the unusual hydrodynamic properties of the hyaluronate molecule were considered to be more important. Since neutrophil migration in vivo occurs through hyaluronate-rich connective tissue matrices, the relevance of these findings for processes such as inflammation and wound healing is clear.

scholarly journals Heterobivalent ligands target cell-surface receptor combinations in vivo

2012 ◽  
Vol 109 (52) ◽  
pp. 21295-21300 ◽  
Author(s):  
L. Xu ◽  
J. S. Josan ◽  
J. Vagner ◽  
M. R. Caplan ◽  
V. J. Hruby ◽  
...  
Keyword(s):  
Cell Surface ◽  
Target Cell ◽  
Cell Surface Receptor ◽  
Surface Receptor

scholarly journals The Arabidopsis receptor kinase STRUBBELIG undergoes clathrin-dependent endocytosis

2019 ◽  
Vol 70 (15) ◽  
pp. 3881-3894 ◽  
Author(s):  
Jin Gao ◽  
Ajeet Chaudhary ◽  
Prasad Vaddepalli ◽  
Marie-Kristin Nagel ◽  
Erika Isono ◽  
...  
Keyword(s):  
Cell Surface ◽  
Fluorescent Protein ◽  
Growth Patterns ◽  
Cell Surface Receptor ◽  
Receptor Kinase ◽  
Surface Receptors ◽  
Surface Receptor ◽  
Green Fluorescent ◽  
Golgi Network

AbstractSignaling mediated by cell surface receptor kinases is central to the coordination of growth patterns during organogenesis. Receptor kinase signaling is in part controlled through endocytosis and subcellular distribution of the respective receptor kinase. For the majority of plant cell surface receptors, the underlying trafficking mechanisms are not characterized. In Arabidopsis, tissue morphogenesis requires the atypical receptor kinase STRUBBELIG (SUB). Here, we studied the endocytic mechanism of SUB. Our data revealed that a functional SUB–enhanced green fluorescent protein (EGFP) fusion is ubiquitinated in vivo. We further showed that plasma membrane-bound SUB:EGFP becomes internalized in a clathrin-dependent fashion. We also found that SUB:EGFP associates with the trans-Golgi network and accumulates in multivesicular bodies and the vacuole. Co-immunoprecipitation experiments revealed that SUB:EGFP and clathrin are present within the same protein complex. Our genetic analysis showed that SUB and CLATHRIN HEAVY CHAIN (CHC) 2 regulate root hair patterning. By contrast, genetic reduction of CHC activity ameliorates the floral defects of sub mutants. Taken together, the data indicate that SUB undergoes clathrin-mediated endocytosis, that this process does not rely on stimulation of SUB signaling by an exogenous agent, and that SUB genetically interacts with clathrin-dependent pathways in a tissue-specific manner.

scholarly journals The Cell Surface Receptor Tartan Is a Potential In Vivo Substrate for the Receptor Tyrosine Phosphatase Ptp52F

2009 ◽  
Vol 29 (12) ◽  
pp. 3390-3400 ◽  
Author(s):  
Lakshmi Bugga ◽  
Anuradha Ratnaparkhi ◽  
Kai Zinn
Keyword(s):  
Cell Surface ◽  
Axon Guidance ◽  
Motor Nerve ◽  
Tyrosine Phosphatase ◽  
Protein Tyrosine Phosphatases ◽  
Cell Surface Receptor ◽  
Wild Type ◽  
Surface Receptor

ABSTRACT Receptor-linked protein-tyrosine phosphatases (RPTPs) are essential regulators of axon guidance and synaptogenesis in Drosophila, but the signaling pathways in which they function are poorly defined. We identified the cell surface receptor Tartan (Trn) as a candidate substrate for the neuronal RPTP Ptp52F by using a modified two-hybrid screen with a substrate-trapping mutant of Ptp52F as “bait.” Trn can bind to the Ptp52F substrate-trapping mutant in transfected Drosophila S2 cells if v-Src kinase, which phosphorylates Trn, is also expressed. Coexpression of wild-type Ptp52F causes dephosphorylation of v-Src-phosphorylated Trn. To examine the specificity of the interaction in vitro, we incubated Ptp52F-glutathione S-transferase (GST) fusion proteins with pervanadate-treated S2 cell lysates. Wild-type Ptp52F dephosphorylated Trn, as well as most other bands in the lysate. GST “pulldown” experiments demonstrated that the Ptp52F substrate-trapping mutant binds exclusively to phospho-Trn. Wild-type Ptp52F pulled down dephosphorylated Trn, suggesting that it forms a stable Ptp52F-Trn complex that persists after substrate dephosphorylation. To evaluate whether Trn and Ptp52F are part of the same pathway in vivo, we examined motor axon guidance in mutant embryos. trn and Ptp52F mutations produce identical phenotypes affecting the SNa motor nerve. The genes also display dosage-dependent interactions, suggesting that Ptp52F regulates Trn signaling in SNa motor neurons.

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