Search results for " Lipid raft"

showing 4 items of 4 documents

Linoleic acid: Is this the key that unlocks the quantum brain? Insights linking broken symmetries in molecular biology, mood disorders and personalis…

2017

Abstract In this paper we present a mechanistic model that integrates subneuronal structures, namely ion channels, membrane fatty acids, lipid rafts, G proteins and the cytoskeleton in a dynamic system that is finely tuned in a healthy brain. We also argue that subtle changes in the composition of the membrane’s fatty acids may lead to down-stream effects causing dysregulation of the membrane, cytoskeleton and their interface. Such exquisite sensitivity to minor changes is known to occur in physical systems undergoing phase transitions, the simplest and most studied of them is the so-called Ising model, which exhibits a phase transition at a finite temperature between an ordered and disorde…

0301 basic medicinePhase transitionLinoleic acidMood DisorderModels NeurologicalPhysical systemAntidepressantContext (language use)MicrotubuleReviewlcsh:RC321-57103 medical and health sciencesCellular and Molecular Neuroscience0302 clinical medicineAntidepressants; Cytoskeleton; Depression; Ion channels; Ising model; Linoleic acid; Lipid raft; Microtubule; Mood disorders; Quantum states; Linoleic Acid; Mood Disorders; Brain; Models Neurological; Neuroscience (all); Cellular and Molecular NeuroscienceIsing modelCytoskeletonlcsh:Neurosciences. Biological psychiatry. NeuropsychiatryLipid raftQuantumIon channelCytoskeletonNeuroscience (all)ChemistryDepressionGeneral Neurosciencelcsh:QP351-495BrainQuantum statesMood disorders Linoleic acid Ion channels Cytoskeleton Microtubule Lipid raft Depression Antidepressants Ising model Quantum statesAntidepressantsQuantum stateLipid raftlcsh:Neurophysiology and neuropsychology030104 developmental biologyIon channelsMood disordersIsing modelIon channelNeuroscience030217 neurology & neurosurgery
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CD95 death-inducing signaling complex formation and internalization occur in lipid rafts of type I and type II cells

2004

We investigated the membrane localization of CD95 in type I and type II cells, which differ in their ability to recruit and activate caspase-8. We found that CD95 was preferentially located in lipid rafts of type I cells, while it was present both in raft and non-raft plasma membrane sub-domains of type II cells. After stimulation, CD95 located in phospholipid-rich plasma membrane was recruited to lipid rafts in both types of cells. Similarly, CD95 cross-linking resulted in caspase-independent translocation of FADD/MORT1 and caspase-8 to the lipid rafts, which was prevented by a death domain-defective receptor. CD95 internalization was then rapid in type I and delayed in type II cells and s…

Death Domain Receptor Signaling Adaptor ProteinsEndosomeT-Lymphocytesmedia_common.quotation_subjectImmunologyApoptosisReceptors Tumor Necrosis FactorCell LineMembrane MicrodomainsSettore MED/04 - PATOLOGIA GENERALECell Line TumorReceptorsHumansImmunology and Allergyfas ReceptorFADDInternalizationLipid raftLipid raftsDeath domainmedia_commonTumorbiologyVesicleFas receptorEndocytosisCell biologyProtein TransportCholesterolCD95 death-inducing signaling complexCaspasesCD95biology.proteinlipids (amino acids peptides and proteins)biological phenomena cell phenomena and immunityCaspase-8Tumor Necrosis FactorCaspase-8; CD95; Lipid rafts; Apoptosis; Caspases; Cell Line Tumor; Cholesterol; Death Domain Receptor Signaling Adaptor Proteins; Humans; Membrane Microdomains; Protein Binding; Protein Transport; Receptors Tumor Necrosis Factor; T-Lymphocytes; fas Receptor; Endocytosis; Signal Transduction; Immunology and Allergy; ImmunologyProtein BindingSignal TransductionEuropean Journal of Immunology
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Plant lipid rafts : from proteic composition to physiological roles

2007

International audience; A large body of evidence supports the existence, in membrane from animal and yeast cells, of functional microdomains playing important roles in protein sorting, signal transduction, or infection by pathogens (1). We demonstrated the presence, in plants, of detergent resistant fractions isolated from plasma membrane, with a lipidic composition similar to animal microdomains (2). Electrophoresis experiments indicated that these fractions were able to recruit a specific set of plasma membrane proteins and exclude others. We used mass spectrometry to give an extensive description of a tobacco plasma membrane microdomains. This led to the identification of 145 proteins wh…

[SDV] Life Sciences [q-bio]PLANT LIPID RAFTS[SDV]Life Sciences [q-bio]
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Hsp60 from cancer cells can reach near and distant targets: A proposal for a multistage pathway

2011

Cancer cells have means to influence other cells in their vicinity and distant, and in this signal-delivering mechanisms the chaperonin Hsp60 plays a role, which is currently being recognized as potentially crucial for the growth and dissemination of at least certain types of tumors. In order to arrive at its destination, Hsp60, a typical resident of mitochondria in normal and tumor cells, leaves the organelle and reaches the blood. In the latter, Hsp60 can travel and arrive at targets situated far away from its origin. The details of the route followed by Hsp60 and their molecular mechanisms have not yet been fully elucidated. We investigated Hsp60 levels and secretion in normal and tumor …

chaperonins; cellular secretion; exosomes; lipid rafts; multivesicular bodies; cell membraneHsp60 cancer
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