Visceral Involvement of Dialysis Amyloidosis

Campistol, Josep M.; Cases, Aleix; Torrás, A; Solèr, M.; J, Muñoz-Gomez; Montolíu, J; Lopez-Pedret, Josep; Revert, L

doi:10.1159/000167505

Cited by 61 publications

(36 citation statements)

References 14 publications

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“…One question about hemodialysis-associated amyloidosis raised is: Are the (^m-associated amyloid deposits localized to articu lar and bone areas or systemic? Some reports (rectum [11], heart, liver [16] different organs [17,18] and spleen, jejunum and duodenum [personal observations]) seem to confirm the presence of amyloid in sites other than bones and synovia in long-term hemodialysis pa tients; amyloid deposits were observed in small vessels and were not identifiable in skin and fat tissue [16]. Our results concerning fat aspirates in hemodialysis patients do not allow us to define the abdominal fat localization of this type of amyloidosis.…”

Section: Discussionmentioning

confidence: 99%

Unsuitable Value of Abdominal Fat Tissue Aspirate Examination for the Diagnosis of Amyloidosis in Long-Term Hemodialysis Patients

et al. 1988

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Abdominal fat tissue aspiration was used in 22 long-term hemodialysis patients (5–17 years). Fourteen of these patients had carpal tunnel syndrome and amyloid deposits of β₂-microglobulin in the synovium. One patient had a spontaneous rupture of the spleen with amyloid deposits in spleen vessels. Seven other patients presented carpal tunnel syndrome and/or articular pains, and radiological lytic lesions in bone, strongly suggesting an amyloid origin. As a control group, in 22 patients with biopsy-proven amyloidosis, abdominal fat tissue aspirates were performed and were studied under the same conditions: by light microscopy these tissues were stained with Congo red and examined with a polarizing microscope; these specimens were also studied by electron microscopy. In all hemodialyzed patients, no amyloid deposit was present in fat tissue with Congo red staining and by electron microscopy. On the contrary, amyloid was observed in 17 of 22 cases in other types of amyloidosis. It seems that this method which has been proved to be simple and sensitive for the diagnosis of systemic amyloidosis is not a good marker for the presence of amyloid in long-term hemodialysis patients.

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Section: Discussionmentioning

confidence: 99%

Unsuitable Value of Abdominal Fat Tissue Aspirate Examination for the Diagnosis of Amyloidosis in Long-Term Hemodialysis Patients

et al. 1988

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“…The major constituent protein in this hemodialysis-related amyloidosis has been identified as β 2 -microglobulin (β2m) [3]. This form of amyloidosis has a preferred tissue distribution involving the synovia, ligaments, articular cartilage and intervertebral discs [2, 4], but it also affects visceral organs [5], especially in patients with prolonged hemodialysis [6]. …”

Section: Introductionmentioning

confidence: 99%

Affinity Binding of Glycosaminoglycans with β2-Microglobulin

Ohashi

Kisilevsky²,

Yanagishita³

2002

Nephron

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Background: A constant finding in β₂-microglobulin (β2m) amyloidosis is an increase in tissue heparan sulfate (HS) and chondroitin sulfate (CS) proteoglycans (PGs) at sites of amyloid deposits. However, the binding characteristics of PGs with β2m have not been elucidated yet. Methods: Using affinity retardation chromatography, β2m- and glycosaminoglycan (GAG)-anchored columns, an affinity between β2m and GAGs was analyzed. Five peptides which spanned the entire β2m amino acid sequence were prepared, and an affinity between these peptides and heparin (HP) was examined. Furthermore, the specific binding of biotinylated β2m peptide for AA amyloid deposits via GAGs was examined on tissue sections. Results: Using β2m-anchored column, HP showed the smallest dissociation constant (K_d), i.e. the strongest affinity, among the GAGs examined. At 0.4 M NaCl, the K_ds of β2m relative to BSA-anchored columns for HP, HS, CS-A, CS-B, and CS-C were 94, 620, 130, 660 and 190 µM, respectively. Using GAG-anchored columns, at 0.15 M NaCl, pH 7.4, β2m also showed an affinity for HP, with the K_d relative to a reference column being 370 µM. Under the latter conditions, no β2m affinity for CSA was demonstrated. Among the five peptides, peptide-1, which is composed of residues 1–24, showed the highest affinity for HP, the K_d being 190 µM. Peptides analogous to peptide-1, in which each basic amino acid was individually replaced by alanine, showed a remarkable decrease in affinity for HP. The specific binding of biotinylated β2m peptide for AA amyloid deposits via HS and CS was confirmed in situ by pretreatment with heparitinase and chondroitinase ABC. Conclusion: The present data indicate that HP/HS is effective in the binding of the β2m monomer, and the anatomic localization of β2m amyloid precursor protein.

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“…Although β 2 -microglobulin amyloidosis can have a systemic involvement [11, 12, 13, 14, 15, 16], it has a marked predilection for bone, tendons, and joints. Bone lesions, radiologically identified as radiolucent cysts, are frequently observed in carpal as well as in long bones.…”

Section: Introductionmentioning

confidence: 99%