scholarly journals Role of the Macrophage Inflammatory Protein-1α/CC Chemokine Receptor 5 Signaling Pathway in the Neuroinflammatory Response and Cognitive Deficits Induced by β-Amyloid Peptide

2009 ◽  
Vol 175 (4) ◽  
pp. 1586-1597 ◽  
Author(s):  
Giselle Fazzioni Passos ◽  
Cláudia Pinto Figueiredo ◽  
Rui Daniel Schröder Prediger ◽  
Pablo Pandolfo ◽  
Filipe Silveira Duarte ◽  
...  
Keyword(s):  
Chemokine Receptor ◽  
Cognitive Deficits ◽  
Amyloid Peptide ◽  
Neuroinflammatory Response ◽  
Inflammatory Protein ◽  
Β Amyloid ◽  
Β Amyloid Peptide ◽  
Cc Chemokine Receptor 5 ◽  
Macrophage Inflammatory Protein

Cholesterol is essential for macrophage inflammatory protein 1β binding and conformational integrity of CC chemokine receptor 5

Blood ◽  
2002 ◽  
Vol 99 (12) ◽  
pp. 4298-4306 ◽  
Author(s):  
Dzung H. Nguyen ◽  
Dennis Taub
Keyword(s):  
Lipid Rafts ◽  
Chemokine Receptor ◽  
Membrane Microdomains ◽  
Inflammatory Protein ◽  
Immunodeficiency Virus ◽  
Chemokine Receptor Ccr5 ◽  
And Function ◽  
Cc Chemokine Receptor 5 ◽  
Macrophage Inflammatory Protein

The chemokine receptor, CCR5, is used as a human immunodeficiency virus coreceptor in combination with CD4 during transmission and early infection. CCR5 has been shown to be palmitoylated and targeted to cholesterol- and sphingolipid-rich membrane microdomains termed “lipid rafts.” However, the role of cholesterol and lipid rafts on chemokine binding and signaling through CCR5 remains unknown. We found that cholesterol extraction by hydroxypropyl-β-cyclodextrin (BCD) significantly reduced the binding and signaling of macrophage inflammatory protein 1β (MIP-1β) using CCR5-expressing CEM-NKR T cells. Reloading treated cells with cholesterol but not 4-cholesten-3-one, an oxidized form of cholesterol, restored MIP-1β binding to BCD-treated cells. Antibodies specific for distinct CCR5 epitopes lost their ability to bind to the cell surface after cholesterol extraction to varying degrees. Moreover, cells stained with fluorescently labeled MIP-1β extensively colocalized with the GM1 lipid raft marker while using anti-CCR5 antibodies; most of CCR5 on these cells only partially colocalized with GM1, suggesting that active ligand binding facilitates receptor association with lipid rafts or that raft association promotes a higher affinity conformation of CCR5. Together, these data demonstrate that cholesterol and lipid rafts are important for the maintenance of the CCR5 conformation and are necessary for both the binding and function of this chemokine receptor.

The role of β-amyloid peptide in neurodegenerative diseases

2011 ◽  
Vol 10 (4) ◽  
pp. 440-452 ◽  
Author(s):  
A.V. Maltsev ◽  
S. Bystryak ◽  
O.V. Galzitskaya
Keyword(s):  
Neurodegenerative Diseases ◽  
Amyloid Peptide ◽  
Β Amyloid ◽  
Β Amyloid Peptide

4-12-07 Ischemic animals as model in the study of the neurobiological role of human β-amyloid peptide

1997 ◽  
Vol 150 ◽  
pp. S227
Author(s):  
R. Pluta ◽  
M. Barcikowska ◽  
A. Misicka ◽  
S. Januszewski ◽  
A.W. Lipkowski
Keyword(s):  
Amyloid Peptide ◽  
Β Amyloid ◽  
Β Amyloid Peptide

scholarly journals The Characterization of the Caenorhabditis elegans Mitochondrial Thioredoxin System Uncovers an Unexpected Protective Role of Thioredoxin Reductase 2 in β-Amyloid Peptide Toxicity

2012 ◽  
Vol 16 (12) ◽  
pp. 1384-1400 ◽  
Author(s):  
Briseida Cacho-Valadez ◽  
Fernando Muñoz-Lobato ◽  
José Rafael Pedrajas ◽  
Juan Cabello ◽  
Juan Carlos Fierro-González ◽  
...  
Keyword(s):  
Caenorhabditis Elegans ◽  
Thioredoxin Reductase ◽  
Protective Role ◽  
Amyloid Peptide ◽  
Thioredoxin System ◽  
Β Amyloid ◽  
Β Amyloid Peptide
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