amyloidosis/албумин

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Human serum albumin can regulate amyloid-β peptide fiber growth in the brain interstitium: implications for Alzheimer disease.

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Alzheimer disease is a neurodegenerative disorder characterized by extracellular accumulation of amyloid-β peptide (Aβ) in the brain interstitium. Human serum albumin (HSA) binds 95% of Aβ in blood plasma and is thought to inhibit plaque formation in peripheral tissue. However, the role of albumin

Serum levels of albumin-amyloid beta complexes are decreased in Alzheimer's disease.

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OBJECTIVE Decreased amyloid β (Aβ) clearance from the brain to blood might play a key role in the development of Alzheimer's disease (AD). Aβ is normally bound to and transported by albumin in blood, thus possibly maintaining constant concentration of free Aβ in the blood. We therefore hypothesized

Therapeutic albumin binding to remove amyloid-β.

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Clearance of plasma amyloid-β (Aβ) through plasma exchange and replacement with therapeutic albumin to facilitate net Aβ efflux from the brain to plasma is a novel approach for the treatment of Alzheimer's disease. Therefore, thorough characterization of the capacity of therapeutic albumin to bind

Amyloid beta-peptide is transported on lipoproteins and albumin in human plasma.

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The amyloid beta-peptide (Abeta) is the major constituent of neuritic plaques in Alzheimer's disease and occurs as a soluble 40-42-residue peptide in cerebrospinal fluid and blood of both normal and AD subjects. It is unclear whether Abeta, once it is secreted by cells, remains free in biological

Aberrant Co-localization of Synaptic Proteins Promoted by Alzheimer's Disease Amyloid-β Peptides: Protective Effect of Human Serum Albumin.

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Amyloid-β (Aβ), Aβ40, Aβ42, and, recently, Aβ25-35 have been directly implicated in the pathogenesis of Alzheimer's disease. We have studied the effects of Aβ on neuronal death, reactive oxygen species (ROS) production, and synaptic assembling in neurons in primary culture. Aβ25-35, Aβ40, and Aβ42

Detection of β-Amyloid by Sialic Acid Coated Bovine Serum Albumin Magnetic Nanoparticles in a Mouse Model of Alzheimer's Disease.

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The accumulation and formation of β-amyloid (Aβ) plaques in the brain are distinctive pathological hallmarks of Alzheimer's disease (AD). Designing nanoparticle (NP) contrast agents capable of binding with Aβ highly selectively can potentially facilitate early detection of AD. However, a significant

[The competition of serum amyloid protein and apoprotein E for binding with human serum albumin].

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The relationship between the concentration of serum amyloid protein (SAP) isolated from human serum and the parameters of the protein elution during gel-filtration and alos with the efficiency of Ca(2+)-dependent SAP binding with sepharose 4B was studied. The dissociation of the SAP oligomeric form

The amyloid in familial amyloid cardiomyopathy of Danish origin is related to pre-albumin.

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Amyloid obtained from the myocardium of a patient (Han) with familial amyloid cardiomyopathy of Danish origin was studied. Gel filtration and electrophoresis of purified and denatured amyloid fibrils Han revealed various fractions ranging in mol. wt from 40,000 to 8,000 daltons. Amyloid Han and

The effects of chondroitin sulfate and serum albumin on the fibrillation of human islet amyloid polypeptide at phospholipid membranes.

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Glycosaminoglycans and serum albumin are important cellular components that regulate the fibril formation of proteins. Whereas the effects of cellular components on the fibrillation of amyloid proteins in bulk solution are widely studied, less attention has been paid to the effects of cellular

Insight into the inhibition effect of acidulated serum albumin on amyloid β-protein fibrillogenesis and cytotoxicity.

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Alzheimer's disease (AD) is the most prevalent form of dementia, and aggregation of amyloid β-proteins (Aβ) into soluble oligomers and fibrils has been implicated in the pathogenesis of AD. Herein we developed acidulated serum albumin for the inhibition of Aβ42 fibrillogenesis. Bovine serum albumin

Comparative toxicity of amyloid beta-peptide in neuroblastoma cell lines: effects of albumin and physalaemin.

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1. Synthetic amyloid beta-peptide was toxic to NB41A3 neuroblastoma cells in serum-free culture as judged by decreasing cell numbers and release of the cytosolic enzyme, lactic dehydrogenase. 2. Without amyloid beta-peptide, bovine serum albumin increased the number of cells surviving in culture. 3.

Serum albumin impedes the amyloid aggregation and hemolysis of human islet amyloid polypeptide and alpha synuclein.

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Protein aggregation is a ubiquitous phenomenon underpinning the origins of a range of human diseases. The amyloid aggregation of human islet amyloid polypeptide (IAPP) and alpha synuclein (αS), specifically, is a hallmark of type 2 diabetes (T2D) and Parkinson's disease impacting millions of people

[The capacity of albumin to bind to beta-amyloid].

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BACKGROUND Most plasma beta-amyloid peptide (Alphabeta) has been described to circulate bound to albumin (approx. 90%). Moreover, a balance between peripheral and brain Alphabeta seems to exist, so a reduction of Alphabeta levels in blood through plasma exchange with therapeutic albumin should

Loss of functional albumin triggers acceleration of transthyretin amyloid fibril formation in familial amyloidotic polyneuropathy.

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Transthyretin (TTR)-related familial amyloidotic polyneuropathy (FAP) is characterized by systemic accumulation of amyloid fibrils caused by a point mutation in the TTR gene. Despite the urgent need for alternative therapeutic strategies, the pathogenesis of FAP still remains elusive. In our study

Amyloid beta-peptide induces cell monolayer albumin permeability, impairs glucose transport, and induces apoptosis in vascular endothelial cells.

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Amyloid beta-peptide (A beta) is deposited as insoluble fibrils in the brain parenchyma and cerebral blood vessels in Alzheimer's disease (AD). In addition to neuronal degeneration, cerebral vascular alterations indicative of damage to vascular endothelial cells and disruption of the blood-brain

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