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PubMed1986

Primary amyloidosis (AL) in families.

We report the occurrence of immunoglobulin-related amyloidosis (AL) in three separate families, each family having two members affected. None of the six patients had evidence to suggest the presence of familial amyloidosis (AF). Previously, immunoglobulin-related amyloidosis (AL) was considered to be a sporadic disease process. Because of the occasional familial occurrence of other monoclonal gammopathies such as monoclonal gammopathy of undetermined significance, multiple myeloma, and macroglobulinemia of Waldenström, amyloidosis (AL) should be added to the list of immunopathies with a familial predisposition.

Adult↗
PubMed1991

Cranial neuropathy associated with primary amyloidosis.

We report 6 patients for whom cranial neuropathy was a major manifestation of primary amyloidosis. In 3 of the 6, multiple cranial nerves were involved. All had tissue biopsy documentation of amyloidosis. In 2, nerve biopsy also confirmed amyloidosis. All had renal involvement manifested by proteinuria. Primary systemic amyloidosis must be considered in the differential diagnosis of cranial neuropathy, especially when proteinuria is present.

Amyloidosis↗
PubMed2002

Fenofibrate inhibits reactive amyloidosis in mice.

OBJECTIVE: To examine the effects of the lipid-lowering agent fenofibrate on experimental AA amyloidosis and on serum amyloid A (SAA) levels. METHODS: Fenofibrate was administered orally in a mouse model of amyloidosis, which is induced by injections of amyloid-enhancing factor and Freund's complete adjuvant. Fenofibrate was given for 3 weeks, including a 1-week course before induction of amyloidosis. Splenic amyloid deposits were evaluated histologically, and SAA levels were measured. RESULTS: Fenofibrate inhibited the formation of splenic amyloid deposits and suppressed the elevation of SAA levels. CONCLUSION; Fenofibrate inhibits experimental amyloidosis by reducing levels of the precursor SAA.

Acute-Phase Proteins↗
PubMed1992

Utility of high-resolution ultrasound for the diagnosis of dialysis-related amyloidosis.

OBJECTIVE: To evaluate the utility of real-time, high-resolution ultrasound of the shoulder in the diagnosis of dialysis-related amyloidosis. METHODS: We performed a case series study of 2 groups of patients seen at a referral-based clinic in a tertiary care hospital. The shoulders of 13 patients with normal renal function and of 38 patients receiving long-term hemodialysis were studied by real-time, high-resolution ultrasound. All hemodialysis patients were evaluated clinically for the presence of dialysis-related amyloidosis. Surgical specimens of joints were available for all 13 patients with normal renal function and for 17 of the 38 hemodialysis patients. These specimens were evaluated for the presence of beta 2-microglobulin (beta 2m) amyloid by Congo red and immunohistochemical staining. RESULTS: Two ultrasonographic findings were selectively observed in the dialysis patients with clinical and histologic evidence of beta 2m amyloid in comparison with patients with normal renal function and no evidence of amyloid: rotator cuffs greater than 8 mm in thickness and echogenic pads between muscle groups of the rotator cuff. The presence of at least 1 of these 2 findings corresponded to the presence of clinically and histologically evident beta 2m amyloid with a sensitivity of 79% and a specificity of 100%. When additional patients without surgical specimens for histologic confirmation of amyloidosis were included, the sensitivity of these 2 sonographic findings was 72% and the specificity was 97%. CONCLUSION: Real-time, high-resolution ultrasound is a relatively sensitive and highly specific noninvasive adjunct to the clinical diagnosis of beta 2m amyloidosis in patients receiving long-term hemodialysis.

Adult↗
PubMed1995

Regression of the nephrotic syndrome in rheumatoid arthritis and amyloidosis treated with azathioprine. A case report.

Secondary or reactive (AA) amyloidosis is a well-known complication of certain rheumatic diseases, particularly rheumatoid arthritis (RA). This case report describes a patient with RA complicated by amyloidosis and the nephrotic syndrome, which regressed after treatment with azathioprine. The AA amyloidosis was documented by renal and lymph node biopsies and by the presence of proteinuria. Evaluation for other etiologies of proteinuria was negative. After treatment with azathioprine, the proteinuria resolved and the serum albumin level increased from 1.9 mg/dl to normal. This is the first published report of azathioprine therapy resulting in a reversal of the nephrotic syndrome in a patient with RA and secondary amyloidosis.

Amyloidosis↗
PubMed1997

Nonsecretory immunoglobulin-derived amyloidosis of the heart: diagnosis by immunohistochemistry of the endomyocardium.

Primary amyloid light chain (AL) amyloidosis of the heart is a rare cause of congestive heart failure. Approximately 15% of patients with primary AL amyloidosis demonstrate no monoclonal proteins on serum or urine immunoelectrophoresis:(so-called nonsecretory immunoglobulin-derived amyloidosis). The histologic findings of endomyocardial biopsy from these patients may be indistinguishable from those with senile cardiac amyloidosis. However, the AL type may respond favourably to chemotherapy while the latter type does not. The prognosis is also better in the senile cardiac amyloid type. The precise diagnosis in the present case was made by applying immunohistochemical techniques on cardiac tissues.

Amyloid↗
PubMedDate not supplied

Hypothyroidism in association with systemic amyloidosis.

BACKGROUND: Systemic amyloidosis leads to functional compromise of various organs through infiltration of these tissues by amyloid protein. The majority of affected patients develop infiltration of the thyroid gland; yet thyroid dysfunction rarely occurs. METHODS AND RESULTS: Described herein is a case of hypothyroidism occurring in a patient with amyloid goiter. An alternative explanation for her hypothyroidism could not be determined by histologic or serologic evaluation. Hormonal assays were consistent with progressive hypothyroidism in spite of oral and, finally, parenteral replacement therapy. A review of the literature describes other cases of thyroid dysfunction reported in patients with systemic amyloidosis. CONCLUSIONS: This case illustrates how amyloid infiltration may be a cause of hypothyroidism in patients with systemic amyloidosis. Therefore, all patients who develop a goiter, including those with systemic amyloidosis, must be screened for thyroid dysfunction. When a physician diagnoses the patient with hypothyroidism, that physician must be aware of potential pitfalls in the administration of thyroxine replacement as outlined below.

Adult↗
PubMed2006

ALys amyloidosis caused by compound heterozygosity in exon 2 (Thr70Asn) and exon 4 (Trp112Arg) of the lysozyme gene.

Hereditary amyloidoses are caused by germline mutations, which increase the propensity of a protein to form cross-beta aggregates and deposit as amyloid. Hereditary amyloidoses are particularly interesting as they help to understand how changes in the primary structure of an otherwise non-amyloidogenic protein contribute to amyloidogenesis. Here we report on a novel form of systemic ALys amyloidosis, caused by compound heterozygosity in exon 2 (p.T70N) and exon 4 (p.W112R) of the lysozyme gene (LYZ), with both mutations being present on the same allele. This type of hereditary ALys amyloidosis is characterized by extended amyloid deposits in the upper gastrointestinal tract, entire colon, and kidney, leading to gastrointestinal bleeding. Both mutations are probably effective in disease manifestation. The novel mutation at position 112 in the mature protein is located within the alpha-helical domain of the protein and therefore outside the cluster of residues that has so far been implicated in ALys amyloidosis. Taken together with the p.T70N mutation, this results in a lysozyme species where the correct folding of various protein domains is probably impaired and increases the propensity of amyloid fibril formation. Interestingly, this form of ALys amyloidosis is also characterized by the occurrence of proteolytic fragments of lysozyme in the amyloid deposits.

Adult↗
PubMed1987

The pathogenesis and biochemistry of amyloidosis.

The transformation of serum proteins into Congo red-sensitive fibrillar material is requisite for the onset and progression of amyloid disease. All the mechanisms which lead to the disease itself have not been elucidated, but our knowledge has increased significantly. It is apparent that in all types of amyloid fibrils, three common features are displayed by the major protein constituents. These are that the fibril protein has a serum precursor, a high degree of anti-parallel beta-sheet conformation and a distinctive ultrastructure on electron microscopy. In the AL and AA forms of amyloidosis, the putative precursors appear to undergo limited degradation to form the protein component of amyloid fibrils. It has been suggested that there may be certain primary structural characteristics inherent in precursor molecules which make them amyloidogenic, thus predisposing them to amyloid fibril formation. This would include certain subtypes of immunoglobulin light chains, possibly kappa I and lambda VI, in the AL type of amyloidosis and one of the polymorphic SAA species, SAA2, which has been identified as the predominating isotype found in AA amyloid fibrils. In AH amyloidosis, the mechanism of amyloid fibril formation appears to be simply a concentration phenomenon where elevated concentrations of B2-M are not handled normally and amyloid deposition is the result. Amyloidogenesis in the hereditary form of systemic amyloidosis may involve other factors in addition to the presence of a variant precursor prealbumin as indicated by the delayed onset of the disease. It is evident that the elucidation of the mechanism(s) which governs the onset and progression of the amyloidoses will allow future regulation and treatment of these all too often complex disorders.

Amyloid↗
PubMed1997

Oxidative stress is found in amyloid deposits in systemic amyloidosis.

Oxidative stress in human amyloid deposits from patients with systemic amyloidosis, such as familial amyloidotic polyneuropathy (FAP), primary amyloidosis, and secondary amyloidosis, was examined immunohistochemically by means of an affinity purified anti-hydroxynonenal (HNE) antibody to HNE, a marker of lipid peroxidation. Furthermore, the levels of thiobarbituric acid reactive substances (TBARS), which is another marker of lipid peroxidation, and the levels of protein carbonyl, a maker of protein modifications by free radicals, were determined in FAP patients and healthy controls. Affinity purified anti-HNE antibody reacted with amyloid deposits in all types of amyloid tissues examined. Significantly higher levels of TBARS and protein carbonyl were found in amyloid rich tissues of FAP patients compared with those in the control subjects. These results verify that lipid peroxidation via free radical injury occurs in amyloid deposits in systemic amyloidosis. The protein modifying properties of free radicals increase the likelihood that they play an important role in the amyloid formation process.

Adult↗
PubMed1994

Preferential expression of human lambda-light-chain variable-region subgroups in multiple myeloma, AL amyloidosis, and Waldenström's macroglobulinemia.

We have compared the distribution of lambda-light-chain variable-region (V lambda) subgroups among Ig lambda molecules found in the serum of normal individuals with that of monoclonal Ig lambda components obtained from patients with plasma cell and related immunoproliferative disorders. A panel of monoclonal antibodies specific for each of the major human V lambda subgroups--V lambda I, V lambda II, V lambda III, V lambda IV, V lambda VI, and V lambda VIII--was used in a highly sensitive enzyme-linked immunosorbent assay (ELISA) to quantitate each of these populations. The mean distribution of Ig lambda I, Ig lambda II, Ig lambda III, Ig lambda IV, Ig lambda VI, and Ig lambda VIII molecules in serum specimens collected from 20 normal adults was approximately 40, 3, 43, 5, 5, and 3% of the total Ig lambda population, respectively. In contrast, that of monoclonal IgG, IgA, and IgD proteins and Bence Jones proteins obtained from patients with multiple myeloma and related gammopathies (n = 196) was approximately 27, 28, 39, 5, 0, and 1%, respectively. The percentage of monoclonal Ig lambda II components found in individuals with AL lambda amyloidosis (n = 41) was comparably increased to that seen in multiple myeloma and was even higher in patients with Waldenström's macroglobulinemia (n = 16), in whom 63% of the IgM lambda proteins were of the V lambda II subgroup. Also evidenced were differences in the distribution of other V lambda subgroups in the disease states: Most striking was the predominance (41%) of the V lambda VI subgroup among monoclonal lambda chains obtained from patients with AL amyloidosis and that this subgroup was found exclusively on amyloidosis-associated proteins. No Ig lambda VI-type myeloma- or macroglobulinemia-related proteins were identified. The observed alterations in V lambda subgroup distribution among "pathologic" monoclonal Igs were attributed to the particular disease and not related to the heavy-chain class. Our finding that certain V lambda subgroups are nonstochastically expressed in lambda-type multiple myeloma, AL amyloidosis, and Waldenström's macroglobulinemia provides evidence for abnormal VL gene usage in these disorders and, thus, furnishes new insight into their pathogenesis.

Amyloid↗
PubMed1994

Primary systemic amyloidosis leading to advanced renal and cardiac involvement in a 30-year old man.

The case of a 30-year-old man with primary systemic amyloidosis is reported. Three months prior to admission the patient developed fever, night sweats, dyspnea, and bilateral ankle swelling. Recurrent left-sided pleural effusion led to further investigation when massive proteinuria with free monoclonal lambda chains in the urine became evident. Abdominal subcutaneous fat aspiration and renal biopsy confirmed the diagnosis of amyloidosis. Bone marrow biopsy and bone scan did not reveal multiple myeloma. Echocardiography showed a sparkling texture of the interventricular septum. Pulsed-wave Doppler recording of the left ventricular inflow profile showed the pattern of advanced cardiac amyloidosis consistent with markedly impaired diastolic heart function. Electrocardiogram-gated magnetic resonance imaging was carried out for noninvasive evaluation of cardiac function. The patient was started on repeated courses of melphalan, prednisone, and colchicine therapy. Despite increasing deterioration of renal function the therapy was tolerated quite well, and the patient is still alive 10 months after initial diagnosis. Although very rare in this age, primary systemic amyloidosis should be considered as a cause of pleural effusion, proteinuria, and congestive heart failure and should lead to further investigation.

Adult↗
PubMed1995

Transthyretin Ser 6 gene frequency in individuals without amyloidosis.

Transthyretin (TTR) Ser 6 was originally described in a Scottish kindred without amyloidosis. This variant, arising from a G-->A transition in codon 6 that destroys an MspI site and creates a BsrI site, was present in none of 50 controls, and was therefore thought to be rare. This variant has subsequently been found in a normal human cDNA liver library and in two unrelated patients with familial amyloidosis and other TTR variants, raising the question whether it is actually a common polymorphism. To address this question, we performed PCR and restriction digestion of 574 DNA samples from people without evidence of amyloidosis or a known family history of amyloidosis. The TTR Ser 6 allele frequency was 33/558 (.060) in Caucasians (including 8/192 (.04) in North American Ashkenazic Jews, 16/218 (.07) in North American non-Jews, and 9/148 (.06) in Portuguese), 3(242 (.01) in African Americans, 0/140 in Africans, and 0/208 in Asians. These data are most suggestive of a single Caucasian founder and the known 25% admixture of "Caucasian" genes in the African-American population. Alternatively, as this variant arose from a transition at a CG dinucleotide "hot spot," it may have arisen on multiple occasions. These data indicate that TTR Ser 6 is a common non-amyloidogenic population polymorphism in Caucasians.

Amyloidosis↗
PubMed1978

Correlations between the morphological and clinical findings in a patient recovering from secondary generalised amyloidosis with renal involvement. Light- and electron microscopic investigations on serial biopsies.

We report light- and electron microscopic findings in glomerular amyloidosis (secondary amyloidosis), which occurred after recurrent empyema of the pleura. After healing of the empyema, the clinical symptoms disappeared, over a period of eight years. During the acute stage of the disease (grade II-III amyloidosis) when the nephrotic syndrome was present, amyloid deposits were seen in the mesangium and on both sides of the basement membrane of the glomerular capillaries. Furthermore, denuded basement membrane areas showing the passage of amyloid into the urinary space, and invaginations of the podocyte by straightened amyloid fibrils were found. After clinical recovery (except for a trace of proteinuria), the renal amyloidosis had electronmicroscopically transformed from an active into an inactive or resting form, while the amount of amyloid present was almost the same. In the areas of amyloid deposits, reparative changes were observed, espcially in the area of the mesangial cells and of the podocytes. The podocytes were separated from the persisting amyloid deposits by newly formed basement membrane material.

Adult↗
PubMed1975

Morphological and clinical features of renal amyloidosis.

The morphological and clinical findings in 122 patients with renal amyloidosis proved by renal biopsy were studied. A higher incidence of amyloidosis occurred in males than females. Coexisting disorders in addition to amyloidosis were present in 80% of the patients. The nephrotic syndrome was a main clinical feature. No significant differences were observed in the manifestations of amyloid renal disease among patients with primary and secondary amyloidosis. Amyloid deposition was present in the mesangium and along the basement membrane. The glomerular basement membrane was damaged by the accumulation of amyloid. The amounts of amyloid in the glomeruli correlated roughly with the clinical manifestations of the disease. The formation of new basement membrane-like substance and the occurrence of granulomatous reaction against amyloid deposits were discussed in relation to the course of hte disease.

Adolescent↗
PubMed1975

Mast cells in the islets of Langerhans. A study of their behaviour in connection with diabetes and with insular amyloidosis.

The number of mast cells in the islets of Langerhans in 60 cases was determined in an autopsy study. The 60 patients were divided into 4 groups, distinguishing between those with diabetes, insular amyloidosis, those with both these pathological conditions and those with neither diabetes nor insular amyloidosis. As compared with the control group, it was discovered that there was a sharp increase in mast cells in the group with insular amyloidosis and in the group with diabetes; the number of mast cells tended to increase even more in the presence of both pathological conditions. With these data in hand, it is assumed that the increase in mast cells in the islets of Langerhans is not only due to the presence of amyloidosis, but that it is also brought about as a direct consequence of diabetes.

Age Factors↗
PubMed1975

[The influence of dyes with special affinity to amyloid on the resorption of casein-induced amyloidosis in mice (author's transl)].

1. The influence of dyes with special affinity to amyloid on the resorption of experimental amyloidosis was studied in mice (A/J/Bom). 2. The amyloidosis was produced by injections of 5% casein over a period of seven weeks. After an interval of six weeks the animals received 0.5 ml of a 0.01% dye solution intraperitoneally (congo red, diamine green, Evans blue) or 0.9% NaCl (controls) every seventh day over a period of 22 weeks. 10, 17, and 22 weeks after the dye treatment was started 3-4 animals of each group were sacrificed and studied histologically. 3. In contrast to the in vitro findings of Shirahama et al. (1971), in vivo there is no acceleration of amyloid resorption by congo red. In the same way diamine green does not accelerate the resorption of amyloid. Evans blue produces a decrease in the amount of amyloid, but at the same time it causes wasting in the animals. Moreover, congo red and diamine green produce amyloidosis by themselves. 4. From our findings neither congo red nor the other amyloidaffine dyes studied, diamine green and Evans blue, are suitable for a therapy of amyloidosis.

Amyloid↗
PubMed1977

Amyloidosis and inflammatory bowel disease.

Surprisingly little has been written about the association of amyloidosis with inflammatory bowel disease. On reviewing the literature it appears that there is a correlation between amyloidosis and Crohn's disease, but little definitive evidence of such a relationship with ulcerative colitis could be found. No specific features emerge as aetiological factors in the amyloidosis of inflammatory bowel disease. The amyloidosis may arise after only a short duration of bowel disease, and there is evidence that the association may be commoner than is realized. The need for a prospective systematic search in a large number of patients with inflammatory bowel disease is emphasized.

Adolescent↗