Antiproteases and Cells in the Pathogenesis of β&lt;sub&gt;2&lt;/sub&gt;-Microglobulin Amyloidosis: Role of α&lt;sub&gt;2&lt;/sub&gt;-Macroglobulin and Macrophages

Argilés, Àngel; Mourad, Georges; Gouin-Charnet, Annie; Schmitt-Bernard, Clair-Florent

doi:10.1159/000045707

Cited by 10 publications

(8 citation statements)

References 107 publications

(137 reference statements)

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“…The other protein components of~2-microglobulin amyloidosis may also play a role in the pathogenesis of this disease. Particularly important would be a 2macroglobulin (66), glucosaminoglycans (67-70) and amyloid P component (71)(72)(73)(74).…”

Section: A) Low Molecular Weight Proteins In General (We)mentioning

confidence: 99%

Uremic Toxicity: Present State of the Art

Vanholder

Argilés

Baurmeister³

et al. 2001

Int J Artif Organs

248

198

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The uremic syndrome is a complex mixture of organ dysfunctions, which is attributed to the retention of a myriad of compounds that under normal condition are excreted by the healthy kidneys (uremic toxins). In the area of identification and characterization of uremic toxins and in the knowledge of their pathophysiologic importance, major steps forward have been made during recent years. The present article is a review of several of these steps, especially in the area of information about the compounds that could play a role in the development of cardiovascular complications. It is written by those members of the Uremic Toxins Group, which has been created by the European Society for Artificial Organs (ESAO). Each of the 16 authors has written a state of the art in his/her major area of interest.

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Section: A) Low Molecular Weight Proteins In General (We)mentioning

confidence: 99%

Uremic Toxicity: Present State of the Art

Vanholder

Argilés

Baurmeister³

et al. 2001

Int J Artif Organs

248

198

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“…Recently, we reported a new simple formic acid microextraction technique allowing the recovery and chemical typing of amyloid in small formalin-fixed biopsy specimens. 15,16 Application of this microtechnique in the present study, together with our small-scale amyloid purification method, 22 made possible the first biochemical characterization of the intestinal amyloid deposits in dialysis-related amyloidosis. Our study was based on previous findings 39,40 showing that amyloid, in contrast to many other proteins, is not affected by formalin fixation, probably because beta-pleated sheet conformation of amyloid prevents formalin infiltration.…”

Section: Discussionmentioning

confidence: 87%

“…33 The immunohistochemical amyloid typing methods are used routinely to provide this information, but in some instances, the obtained results can be inconclusive, especially in relation to AL proteins. 35 In this respect, our biochemical micromethods 15,16 applied in this study were helpful in identifying unequivocally the chemical nature of the deposited amyloid. (Figures 7 and 8).…”

Section: Discussionmentioning

confidence: 97%

“…15 The importance of the b 2 M structure-unrelated factors in the pathogenesis of dialysis-related amyloidosis has been proposed by implying the role of other proteins and cells under chronic inflammatory stress conditions and by raising questions of bioincompatibility of membranes or insufficient purity of water used for dialysis. 16,17 Thus, the existence of the diseasespecific modifications of b 2 M structure and their role in the pathogenesis of amyloid disease remain questionable.…”

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confidence: 99%

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Gastrointestinal β2microglobulin amyloidosis in hemodialysis patients: biochemical analysis of amyloid proteins in small formalin-fixed paraffin-embedded tissue specimens

et al. 2005

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We present here a first report on the biochemical analysis of intestinal amyloid deposits found in two cases of hemodialysis-related amyloidosis. A new microtechnique was applied for extraction and immunochemical/ chemical characterization of amyloid proteins in small amounts of fixed tissue, thus allowing precise identification of b 2 microglobulin amyloid (Ab 2 M) in both cases studied. The molecular mass of the identified amyloid b 2 M was close to that of intact b 2 M (12 kDa), with no evidence of the products of proteolytic fragmentation of these molecules. The isoelectrofocusing of the purified Ab 2 M demonstrated a shift to more acidic pI as compared to the normal b 2 M analyzed under the same experimental conditions. The obtained data suggest that the intestinal amyloid deposits in dialysis-related amyloidosis contain disease-specific b 2 M isoforms, which could play a role in the pathogenesis of amyloid disease. The new methodology used might be useful in obtaining precise diagnosis of amyloidosis that is necessary for appropriate therapy, and also provide new important information on the chemical structure of amyloid proteins.

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“…Subsequently, b 2 -microglobulin (b 2 m), a precursor protein of DRA, has been reported to form a complex with a 2 M [9]. On the basis of this evidence, the "a 2 M hypothesis" has been forwarded by Argil és et al [10] as an interesting mechanism to account for the pathogenesis of DRA. Based on this complex-mediated promotion concept, we established an assay system using the enzyme immunoassay method for a 2 M-b 2 m complex and measured its serum level in 137 hemodialysis patients as well as 11 prehemodialysis patients.…”

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confidence: 99%