scholarly journals Cyclic Mechanical Reinforcement of Integrin–Ligand Interactions

2013 ◽  
Vol 49 (6) ◽  
pp. 1176 ◽  
Author(s):  
Fang Kong ◽  
Zhenhai Li ◽  
William M. Parks ◽  
David W. Dumbauld ◽  
Andrés J. García ◽  
...  
Keyword(s):  
Mechanical Reinforcement ◽  
Ligand Interactions ◽  
Integrin Ligand

scholarly journals Cyclic Mechanical Reinforcement of Integrin–Ligand Interactions

2013 ◽  
Vol 49 (6) ◽  
pp. 1060-1068 ◽  
Author(s):  
Fang Kong ◽  
Zhenhai Li ◽  
William M. Parks ◽  
David W. Dumbauld ◽  
Andrés J. García ◽  
...  
Keyword(s):  
Mechanical Reinforcement ◽  
Ligand Interactions ◽  
Integrin Ligand

scholarly journals Binding of Anthrax Toxin to Its Receptor Is Similar to α Integrin-Ligand Interactions

2003 ◽  
Vol 278 (49) ◽  
pp. 49342-49347 ◽  
Author(s):  
Kenneth A. Bradley ◽  
Jeremy Mogridge ◽  
G. Jonah ◽  
A. Rainey ◽  
Sarah Batty ◽  
...  
Keyword(s):  
Anthrax Toxin ◽  
Ligand Interactions ◽  
Integrin Ligand

scholarly journals Vimentin filaments regulate integrin–ligand interactions by binding to the cytoplasmic tail of integrin β3

2016 ◽  
Vol 129 (10) ◽  
pp. 2030-2042 ◽  
Author(s):  
Jiyoon Kim ◽  
Chansik Yang ◽  
Eun Jin Kim ◽  
Jungim Jang ◽  
Se-Jong Kim ◽  
...  
Keyword(s):  
Cytoplasmic Tail ◽  
Integrin Β3 ◽  
Ligand Interactions ◽  
Integrin Ligand ◽  
Vimentin Filaments

scholarly journals Shining a Light on Intestinal Traffic

2012 ◽  
Vol 2012 ◽  
pp. 1-14 ◽  
Author(s):  
Carola T. Murphy ◽  
Kenneth Nally ◽  
Fergus Shanahan ◽  
Silvia Melgar
Keyword(s):  
Leukocyte Migration ◽  
Clinical Aspects ◽  
Leukocyte Trafficking ◽  
Ligand Interactions ◽  
Inflammatory Bowel ◽  
Integrin Ligand ◽  
Major Target

Inflammatory bowel disease (IBD), encompassing Crohn's disease and ulcerative colitis, is associated with enhanced leukocyte infiltration to the gut, which is directly linked to the clinical aspects of these disorders. Thus, leukocyte trafficking is a major target for IBD therapy. Past and emerging techniques to study leukocyte trafficking bothin vitroandin vivohave expanded our knowledge of the leukocyte migration process and the role of inhibitors. Various strategies have been employed to target chemokine- and integrin-ligand interactions within the multistep adhesion cascade and the S1P/S1PR1 axis in leukocyte migration. Though there is an abundance of preclinical data demonstrating efficacy of leukocyte trafficking inhibitors, many have yet to be confirmed in clinical studies. Vigilance for toxicity and further research is required into this complex and emerging area of IBD therapy.

scholarly journals Cellular Entry of Hantaviruses Which Cause Hemorrhagic Fever with Renal Syndrome Is Mediated by β3 Integrins

1999 ◽  
Vol 73 (5) ◽  
pp. 3951-3959 ◽  
Author(s):  
Irina N. Gavrilovskaya ◽  
Eric J. Brown ◽  
Mark H. Ginsberg ◽  
Erich R. Mackow
Keyword(s):  
New York ◽  
Endothelial Cells ◽  
Umbilical Vein ◽  
Hemorrhagic Fever ◽  
Common Elements ◽  
Fab Fragment ◽  
Ligand Interactions ◽  
Cellular Entry ◽  
Umbilical Vein Endothelial Cells ◽  
Integrin Ligand

ABSTRACT Hantaviruses replicate primarily in the vascular endothelium and cause two human diseases, hemorrhagic fever with renal syndrome (HFRS) and hantavirus pulmonary syndrome (HPS). In this report, we demonstrate that the cellular entry of HFRS-associated hantaviruses is facilitated by specific integrins expressed on platelets, endothelial cells, and macrophages. Infection of human umbilical vein endothelial cells and Vero E6 cells by the HFRS-causing hantaviruses Hantaan (HTN), Seoul (SEO), and Puumala (PUU) is inhibited by antibodies to αvβ3 integrins and by the integrin ligand vitronectin. The cellular entry of HTN, SEO, and PUU viruses, but not the nonpathogenic Prospect Hill (PH) hantavirus (i.e., a virus with no associated human disease), was also mediated by introducting recombinant αIIbβ3 or αvβ3 integrins into β3-integrin-deficient CHO cells. In addition, PH infectivity was not inhibited by αvβ3-specific sera or vitronectin but was blocked by α5β1-specific sera and the integrin ligand fibronectin. RGD tripeptides, which are required for many integrin-ligand interactions, are absent from all hantavirus G1 and G2 surface glycoproteins, and GRGDSP peptides did not inhibit hantavirus infectivity. Further, a mouse-human hybrid β3integrin-specific Fab fragment, c7E3 (ReoPro), also inhibited the infectivity of HTN, SEO, and PUU as well as HPS-associated hantaviruses, Sin Nombre (SN) and New York-1 (NY-1). These findings indicate that pathogenic HPS- and HFRS-causing hantaviruses enter cells via β3 integrins, which are present on the surfaces of platelets, endothelial cells, and macrophages. Since β3integrins regulate vascular permeability and platelet function, these findings also correlate β3 integrin usage with common elements of hantavirus pathogenesis.

Epitopes of adhesion-perturbing monoclonal antibodies map within a predicted alpha-helical domain of the integrin beta 1 subunit

1997 ◽  
Vol 110 (20) ◽  
pp. 2619-2628
Author(s):  
D.T. Shih ◽  
D. Boettiger ◽  
C.A. Buck
Keyword(s):  
Ligand Binding ◽  
Critical Role ◽  
Alpha Helix ◽  
Cation Binding ◽  
Affinity Column ◽  
Integrin Subunit ◽  
Amino Acid Residues ◽  
Helix Formation ◽  
Ligand Interactions ◽  
Integrin Ligand

Several recent studies have demonstrated the involvement of various domains of the beta 1 integrin subunit in ligand binding. Thus, specific amino acids have been shown to be important in divalent cation binding, and others have been implicated by peptide crosslinking to play an intimate role in integrin-ligand interactions. Added to these data are previous observations that a group of adhesion-blocking anti-chicken beta 1 antibodies mapped within the first 160 amino acid residues of the subunit. These observations suggested that this region plays a critical role in integrin ligand recognition. In order to further define the domain in which the epitopes for these antibodies are clustered, a series of mouse/chicken chimeric beta 1 constructs were examined for their reactivity with each of these antibodies. Most of the antibodies recognize a region between residues 124 to 160 of the chicken beta 1 subunit. Computer modeling predicted a possible amphipathic alpha-helical configuration for the region between residues 141 to 160. Consistent with this prediction, circular dichroism and NMR analysis revealed a tendency for a synthetic peptide containing these residues to form an alpha-helix. The significance of this structural characteristic was demonstrated by a mutation at residue 149 that disrupted the alpha-helix formation and resulted in a loss of the ability to form heterodimers with alpha subunits, localize to focal contacts, or be transported to the cell surface. The direct involvement of residues 141 to 160 in ligand binding was supported by the ability of a peptide with this sequence to elute integrins from a fibronectin affinity column. Thus, our data suggest that residues 141 to 160 of the integrin beta 1 subunit, when arranged in an alpha-helix configuration, participate in ligand binding.

scholarly journals Membrane Targeting and Coupling of NHE1-IntegrinαIIbβ3-NCX1 by Lipid Rafts following Integrin-Ligand Interactions Trigger Ca2+Oscillations

2008 ◽  
Vol 284 (6) ◽  
pp. 3855-3864 ◽  
Author(s):  
Yung-Hsiang Yi ◽  
Pei-Yun Ho ◽  
Tung-Wei Chen ◽  
Wen-Jie Lin ◽  
Vladimir Gukassyan ◽  
...  
Keyword(s):  
Lipid Rafts ◽  
Membrane Targeting ◽  
Ligand Interactions ◽  
Integrin Ligand

scholarly journals Integrin-Ligand Interactions in Inflammation, Cancer, and Metabolic Disease: Insights Into the Multifaceted Roles of an Emerging Ligand Irisin

2020 ◽  
Vol 8 ◽  
Author(s):  
Eun Jeong Park ◽  
Phyoe Kyawe Myint ◽  
Atsushi Ito ◽  
Michael G. Appiah ◽  
Samuel Darkwah ◽  
...  
Keyword(s):  
Metabolic Disease ◽  
Ligand Interactions ◽  
Integrin Ligand
Sign in / Sign up

Export Citation Format

Share Document