Hereditary renal amyloidosis caused by a new variant lysozyme W64R in a French family

Valleix, Sophie; Drunat, Séverine; Philit, Jean‐Baptiste; Adoue, D.; Piette, Jean‐Charles; Droz, Dominique; MacGregor, Brigitte; Canet, Denis; Delpech, Marc; Grateau, Gilles

doi:10.1046/j.1523-1755.2002.00205.x

Cited by 117 publications

(86 citation statements)

References 19 publications

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“…Cardiac amyloidosis and amyloid neuropathy are associated with scores of mutations of transthyretin [42], and immunohistochemical staining with commercially available anti-transthyretin antisera [39] is specific [43]. When definitive immunohistochemical typing of amyloid cannot be achieved, specific genetic studies can be performed by polymerase chain reaction to recognize mutations in transthyretin [44,45], fibrinogen, lysozyme [46], and apolipoproteins A-I and A-II. Amyloid has been extracted successfully from fat deposits [47] for direct sequencing of the fibril protein [48].…”

Section: How Is the Amyloidosis Characterized As Al Type?mentioning

confidence: 99%

Definition of organ involvement and treatment response in immunoglobulin light chain amyloidosis (AL): A consensus opinion from the 10th International Symposium on Amyloid and Amyloidosis

et al. 2005

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Section: How Is the Amyloidosis Characterized As Al Type?mentioning

confidence: 99%

Definition of organ involvement and treatment response in immunoglobulin light chain amyloidosis (AL): A consensus opinion from the 10th International Symposium on Amyloid and Amyloidosis

et al. 2005

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“…Probing human lysozyme amyloid formation and inhibition using a camel antibody fragment. Four single-point mutants (I56T, F57I, D67H and W64R) and a double mutation (F57I/T70N) of human lysozyme are associated with systemic amyloid disease [114][115][116]. The effects of the D67H mutation on the properties of the lysozyme molecule have been studied at the molecular level using a variety of techniques including pulse labelling hydrogen/deuterium exchange analysed by mass spectrometry and NMR spectroscopy [28,117].…”

Section: Elucidation Of Misfolding Eventsmentioning

confidence: 99%

Probing the origins, diagnosis and treatment of amyloid diseases using antibodies

Dumoulin

Dobson

2004

Biochimie

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The deposition of proteins in the form of amyloid fibrils is the characteristic feature of more than 20 medical conditions affecting the central nervous system or a variety of peripheral tissues. These disorders, which include Alzheimer's disease, the prion diseases and type II diabetes, are of enormous importance in the context of present-day human health and welfare. Extensive research is therefore being carried out to define the molecular details of the mechanism of the pathological conversion of amyloidogenic proteins from their soluble forms into fibrillar structures. This review focuses on recent studies that demonstrate the power of using antibodies or antibody fragments to probe the process of fibril formation, and discusses the emerging potential of these species as diagnostic and therapeutic agents.

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“…1 Since 1993, six naturally occurring lysozyme variants associated with amyloid disease (I56T, F57I, F57I/T70N, W64R, D67H and T70N/W112R), [2][3][4][5] and one non-amyloidogenic variant (T70N), 6 have been discovered. In-depth characterization of two of the disease-associated variants, I56T and D67H, as well as the non-diseaserelated T70N variant, has been performed using a variety of biophysical techniques.…”

Section: Introductionmentioning

confidence: 99%

The Extracellular Chaperone Clusterin Potently Inhibits Human Lysozyme Amyloid Formation by Interacting with Prefibrillar Species

Kumita

Poon

Caddy

et al. 2007

Journal of Molecular Biology

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We have studied the effects of the extracellular molecular chaperone, clusterin, on the in vitro aggregation of mutational variants of human lysozyme, including one associated with familial amyloid disease. The aggregation of the amyloidogenic variant I56T is inhibited significantly at clusterin to lysozyme ratios as low as 1:80 (i.e. one clusterin molecule per 80 lysozyme molecules). Experiments indicate that under the conditions where inhibition of aggregation occurs, clusterin does not bind detectably to the native or fibrillar states of lysozyme, or to the monomeric transient intermediate known to be a key species in the aggregation reaction. Rather, it seems to interact with oligomeric species that are present at low concentrations during the lag (nucleation) phase of the aggregation reaction. This behavior suggests that clusterin, and perhaps other extracellular chaperones, could have a key role in curtailing the potentially pathogenic effects of the misfolding and aggregation of proteins that, like lysozyme, are secreted into the extracellular environment.

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Hereditary renal amyloidosis caused by a new variant lysozyme W64R in a French family

Cited by 117 publications

References 19 publications

Definition of organ involvement and treatment response in immunoglobulin light chain amyloidosis (AL): A consensus opinion from the 10th International Symposium on Amyloid and Amyloidosis

Definition of organ involvement and treatment response in immunoglobulin light chain amyloidosis (AL): A consensus opinion from the 10th International Symposium on Amyloid and Amyloidosis

Probing the origins, diagnosis and treatment of amyloid diseases using antibodies

The Extracellular Chaperone Clusterin Potently Inhibits Human Lysozyme Amyloid Formation by Interacting with Prefibrillar Species

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