P3‐288: Antibodies in the dimer fraction of IVIG have the capacity to bind beta amyloid

Relkin, Norman; Szabo, Paul; Rotondi, Matthew L.; Mujalli, Diana

doi:10.1016/j.jalz.2009.04.959

Cited by 2 publications

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Approaches to Amyloid Therapies for the Treatment of Alzheimer's Disease

Robichaud

Kim

Jacobsen

2010

Burger's Medicinal Chemistry and Drug Discovery

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Recognized as the most common of the neurodegenerative disorders, Alzheimer's disease (AD) affects greater than 18 million people worldwide and is predicted to become the largest socioeconomic burden of the twenty‐first century. The underlying mechanism of Alzheimer's disease is as yet unknown, but the growing body of pathophysiologic evidence is beginning to point to two main causes, the formation of β‐amyloid plaques and neurofibrillary tangles. This review will cover approaches to disease modification that are based on the amyloid hypothesis; that being, the prevention of the accumulation, aggregation, and deposition of β‐amyloid peptide (Aβ) monomers, leading first to multiple oligomeric species and then to fibrils and ultimately senile plaques, is the center of focus for an approach to disease modification. There is a wealth of evidence to implicate this peptide and its subsequent aggregation in the etiology of the disease and approaches, both small molecule and biopharmaceutical, to prevent its accumulation have been the subject of much research. The vast majority of this research over the last decade has been, and continues to be, focused on these disease‐modifying, antiamyloidogenic approaches to AD. It is this subject, and the various approaches, past and present to amelioration of AD through the various agents being explored, that will be the focus of this chapter.

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Approaches to Amyloid Therapies for the Treatment of Alzheimer's Disease

Robichaud

Kim

Jacobsen

2010

Burger's Medicinal Chemistry and Drug Discovery

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On the Dark Side of Therapies with Immunoglobulin Concentrates: The Adverse Events

et al. 2015

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Therapy by human immunoglobulin G (IgG) concentrates is a success story ongoing for decades with an ever increasing demand for this plasma product. The success of IgG concentrates on a clinical level is documented by the slowly increasing number of registered indication and the more rapid increase of the off-label uses, a topic dealt with in another contribution to this special issue of Frontiers in Immunology. A part of the success is the adverse event (AE) profile of IgG concentrates which is, even at life-long need for therapy, excellent. Transmission of pathogens in the last decade could be entirely controlled through the antecedent introduction by authorities of a regulatory network and installing quality standards by the plasma fractionation industry. The cornerstone of the regulatory network is current good manufacturing practice. Non-infectious AEs occur rarely and mainly are mild to moderate. However, in recent times, the increase in frequency of hemolytic and thrombotic AEs raised worrying questions on the possible background for these AEs. Below, we review elements of non-infectious AEs, and particularly focus on hemolysis and thrombosis. We discuss how the introduction of plasma fractionation by ion-exchange chromatography and polishing by immunoaffinity chromatographic steps might alter repertoire of specificities and influence AE profiles and efficacy of IgG concentrates.

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P3‐288: Antibodies in the dimer fraction of IVIG have the capacity to bind beta amyloid

Cited by 2 publications

References 0 publications

Approaches to Amyloid Therapies for the Treatment of Alzheimer's Disease

Approaches to Amyloid Therapies for the Treatment of Alzheimer's Disease

On the Dark Side of Therapies with Immunoglobulin Concentrates: The Adverse Events

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