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PubMed1979

Localized conjunctival amyloidosis.

We treated a patient with localized amyloidosis of the bulbar conjunctiva, which strongly resembled a neoplastic growth. Although the patient suffered from a long-standing, debilitating rheumatoid arthritis, suggesting the possibility of a secondary systemic amyloidosis caused by the chronic effusive process, no specific clinical evidence of systemic amyloidosis was noted. The ocular lesion was, therefore, classified as a primary localized amyloidosis. However, the simple recognition of amyloid in the ocular adnexa should not be considered a complete diagnosis. For such cases in which a prominent underlying systemic disease is present, a thorough medical evaluation and future follow-up should be ensured to rule out the possibility that this represents the initial manifestation of a potentially life-threatening secondary systemic amyloidosis caused by rheumatoid arthritis.

Aged↗
PubMed1984

Immunocytochemical demonstration of prealbumin in the vitreous in heredofamilial amyloidosis.

Vitreous material obtained at pars plana vitrectomy from a patient with heredofamilial amyloidosis with vitreous involvement and control vitreous from a patient without amyloidosis were subjected to immunocytochemical studies. P component (AP), a minor constituent of all amyloid deposits, was found in trace amounts in the familial amyloid vitreous, but other amyloid proteins, which occur in secondary amyloidosis or in primary amyloidosis, were not found. The major amyloid protein in the vitreous in heredofamilial amyloidosis (but not control vitreous) was found to be prealbumin.

Adult↗
PubMed1990

Finnish hereditary amyloidosis is caused by a single nucleotide substitution in the gelsolin gene.

The amyloid protein in Finnish hereditary amyloidosis is a fragment of the actin-filament binding region of a variant gelsolin molecule. Here we demonstrate, using polymerase chain reaction and allele-specific oligonucleotide hybridization analyses of genomic DNA, a single base mutation (G654----A654) in the gelsolin gene segment encoding the amyloid protein. The mutation is responsible for the expression of the variant (Asn187) gelsolin molecule in Finnish hereditary amyloidosis. The nucleotide substitution was found in all five unrelated patients with Finnish amyloidosis studied, but not in 45 unrelated control subjects. The mutation co-segregated with the disease phenotype in a family with Finnish amyloidosis. The results show that a single substitution in the gelsolin gene causes Finnish hereditary amyloidosis. The allele-specific oligonucleotide hybridization method provides a simple and accurate means of detecting this mutation.

Amyloidosis↗
PubMed1993

Low diagnostic yield of sural nerve biopsy in patients with peripheral neuropathy and primary amyloidosis.

Patients with primary amyloidosis may develop peripheral neuropathy as an early feature. Sural nerve biopsy is reported to be a sensitive method for diagnosing amyloidosis in such patients. We identified nine patients, ultimately diagnosed as having amyloidosis, who were referred for peripheral neuropathy of undetermined etiology. In six, a sural nerve biopsy demonstrated no amyloid. Subsequent examination of other tissue or of the contralateral sural nerve eventually resulted in the correct diagnosis. We conclude that sural nerve biopsy may be less sensitive than previously believed for the diagnosis of amyloidosis in patients with peripheral neuropathy secondary to amyloid. When the clinical suspicion of amyloidosis is high, a nondiagnostic sural nerve biopsy should not discourage the performance of further investigative studies.

Aged↗
PubMed1991

Imaging of haemodialysis-associated amyloidosis with 123I-serum amyloid P component.

Long-term haemodialysis is frequently complicated by amyloid deposition in which the fibrils consist of beta 2-microglobulin. Dialysis-related amyloid disease causes extensive morbidity and has been associated with deaths in some cases. All amyloid deposits contain amyloid P component that is derived from the normal circulating protein, serum amyloid P component (SAP). We have used scintigraphic imaging after injection of 123I-labelled SAP to assess the distribution of amyloidosis in 38 patients receiving long-term haemodialysis for end-stage renal failure. There was focal localisation of tracer at all sites where histological examination confirmed amyloid deposition. Splenic uptake was seen in 12 patients, indicating splenic amyloidosis, but there was no evidence of other visceral involvement. 6 control subjects who had been dialysed for under 1.5 years showed no localisation of tracer, nor was there any uptake of 123I-labelled human serum albumin in 3 long-term dialysis patients with histologically confirmed amyloidosis and positive 123I-SAP images. Negative scans were also obtained in 5 patients who had been transplanted 0.8-2.4 years previously, despite past evidence of dialysis arthropathy (5) and histologically proven amyloidosis (4). 123I-SAP scintigraphy may be helpful as a non-invasive method for both the diagnosis and monitoring of dialysis-associated amyloidosis.

Amyloidosis↗
PubMed1995

[Systemic amyloidosis in the elderly: diagnostic value of the test of subcutaneous abdominal fat and the labial salivary glands. Prospective study in 100 aged patients].

Primary and secondary amyloidosis are not uncommon in aging but the diagnosis is rarely made on account of the risk of bleeding in the site of biopsies and the difficulty to distinguish senile from systemic amyloidosis on the biopsy samples. We have studied the frequency of amyloid deposition in the abdominal fat aspirate (AFA), the labial salivary gland (LSG), the temporal arteries (four cases), bone marrow (two cases), digestive tract (four cases) in 100 elderly patients (aged 80 or greater). AFA was positive in 15 percent of the patients and LSG in 5%; both samples were positive in 4%. Four cases of systemic amyloidosis were found (two of the AL and two of the AA type). Sensitivity of AFA was 75%, specificity was 87% and the positive predictive value was 20%. The values were respectively 100%, 99%, 100% for LSG. In 11 patients whose AFA biopsies samples were singly positive, amyloid deposits were found in temporal arteries in four of four cases. We conclude that AFA is too sensitive for the diagnosis of systemic amyloidosis in aging. The responsibility of senile amyloid deposition on AFA should require further investigations. LSG biopsies seem to be a more reliable test for the diagnosis of primary and secondary amyloidosis in elderly.

Abdomen↗
PubMed1989

Doppler characterization of left ventricular diastolic function in cardiac amyloidosis.

Sixty-four patients with primary systemic amyloidosis-53 with two-dimensional echocardiographic features of cardiac involvement (Group I) and 11 without cardiac involvement (Group II)--underwent Doppler echocardiographic assessment of left ventricular diastolic function. Pulsed wave Doppler recordings of left ventricular inflow velocities and pulmonary vein flow velocities with respiratory monitoring in these patients were compared with findings in a normal group. Patients in Group I showed striking abnormalities of left ventricular diastolic filling when classified into subgroups by mean left ventricular wall thickness: early greater than 12 but less than 15 mm; advanced greater than or equal to 15 mm. In early amyloidosis, relaxation was abnormal, with decreased peak early velocity (75 +/- 20 versus 86 +/- 16 cm/s; p less than 0.01), increased late velocity (71 +/- 22 versus 56 +/- 13 cm/s; p less than 0.01), decreased early to late velocity ratio (1.2 +/- 0.6 versus 1.6 +/- 0.5; p less than 0.01) and prolonged isovolumic relaxation time (87 +/- 15 versus 73 +/- 13 ms; p less than 0.01) compared with normal values. In advanced amyloidosis, there was a restrictive filling pattern with a markedly shortened deceleration time (148 +/- 50 versus 199 +/- 32 ms; p less than 0.001), decreased pulmonary vein peak systolic flow velocity (34 +/- 16 versus 54 +/- 12 cm/s; p less than 0.01) and increased diastolic flow velocity (55 +/- 20 versus 44 +/- 12 cm/s; p less than 0.01) compared with normal values. Group and the subgroup with early amyloidosis had similar flow velocity patterns. Thus, this study documents that in cardiac amyloidosis, a spectrum of diastolic filling abnormalities exists; the restrictive filling pattern is seen only in the advanced stages.

Amyloidosis↗
PubMed2006

[Gastric amyloidosis mimicking malignancy. A case report].

Amyloidosis is an abnormal extracellular deposition of insoluble proteins, which is associated with an involvement of the gastrointestinal tract in 50 to 70% of cases. In primary amyloidosis (light chain amyloidosis), localized gastric involvement is a rare finding which can mimic malignancy. We report the case of a 56-year-old man, admitted with upper digestive outlet obstruction. Linitis plastica with lymph node involvement was suspected by gastroscopy, barium meal and endoscopic ultrasonography but was not confirmed by gastric biopsies. The patient was treated with total gastrectomy with lymph node dissection. Pathological examination demonstrated gastric and lymph nodes amyloidosis and no malignant tumor was found. The patient died 9 months later from cardiac failure due to amyloidosis.

Amyloidosis↗
PubMed2006

Fulminant hepatic failure due to secondary amyloidosis.

Systemic amyloidosis frequently involves liver, however, clinically apparent liver disease is rare and, if observed, is usually mild. Rarely, primary amyloidosis may present with evidence of portal hypertension or hepatic failure. Although secondary amyloidosis may involve the liver and rarely causes liver pathologies such as cholestatic hepatitis and portal hypertension, to our knowledge, hepatic failure due to secondary amyloidosis has been reported once before. Herein, we presented a woman with subacute fulminant hepatic failure who had no known history of a chronic disease other than episodes of urinary tract infection, and secondary amyloidosis was diagnosed with post-mortem liver biopsy.

Amyloidosis↗
PubMed2005

Noninvasive etiologic diagnosis of cardiac amyloidosis using 99mTc-3,3-diphosphono-1,2-propanodicarboxylic acid scintigraphy.

OBJECTIVES: We investigated the diagnostic accuracy of 99mTc-3,3-diphosphono-1,2-propanodicarboxylic acid (99mTc-DPD) scintigraphy for differentiation of monoclonal immunoglobulin light-chain (AL) and transthyretin (TTR)-related cardiac amyloidosis. BACKGROUND: Differential diagnosis between TTR-related and AL amyloidosis is often complex and time-consuming. METHODS: Patients under routine observation with TTR-related/AL systemic amyloidosis and echocardiographic evidence of cardiac involvement were studied with 99mTc-DPD scintigraphy. RESULTS: Patients with cardiac involvement of TTR-related (group A; n = 15) and AL (group B; n = 10) etiology were comparable for left ventricular mass and renal function. Heart and heart/whole-body tracer retention were significantly higher (p < 0.05) in group A as compared with group B and with 10 unaffected controls. At visual scoring, cardiac 99mTc-DPD uptake was present in all group A patients and absent in all group B patients; thus, using genotyping/immunohistochemistry as the reference technique, the accuracy of 99mTc-DPD scintigraphy for distinction of TTR-related and AL etiology was 100%. Cardiac 99mTc-DPD uptake was also absent among unaffected controls. Using echocardiography as the reference standard for recognition of cardiac involvement, sensitivity and specificity of scintigraphy were both 100% for group A patients; in group B, sensitivity was 0% and specificity was 100% (accuracy, 50%). Eleven patients with myocardial 99mTc-DPD uptake underwent 99mTc-methylene diphosphonate (99mTc-MDP) scintigraphy; all patients showed a 99mTc-MDP myocardial visual score of 0. CONCLUSIONS: Etiology is a third major cause--in addition to type of organ-involved (soft-tissue/heart) and tracer type--of scintigraphic variability in cardiac amyloidosis. This is a highly relevant consideration for future studies. We conclude that 99mTc-DPD scintigraphy is a useful step in the workup of the differential diagnosis of TTR versus AL etiology in patients with documented cardiac amyloidosis.

Aged↗
PubMedDate not supplied

Renal amyloidosis followed more than 5 years: report of 12 cases.

Renal involvement with amyloidosis is common but causes patient survival to be poor, rarely reaching 5 years. In this study, we retrospectively reviewed clinical and biological characteristics as well as treatments and outcomes of patients with renal amyloidosis followed for more than 5 years. Between 1975 and 2003, 485 patients were diagnosed with renal amyloidosis including only 12 patients who were followed more than 5 years. The six men and six women of mean age 42.4 years (range 18 to 66 years) displayed renal signs of lower limb edema in all cases; hypertension in four cases, proteinuria on urinalysis in all cases with microscopic hematuria in five cases. Biological tests showed nephrotic syndrome in 11 patients, normal renal function in nine patients, and renal failure in three patients whose mean creatinine was 481.6 micromol/L (range 294 to 726). The amyloidosis was AA type in 11 cases and non-AA in one case. An etiologic survey revealed spondylarthropathy in one patient, pulmonary tuberculosis in two patients, chronic bronchitis in three patients, hepatic hydatic cyst in one patient, Mediterranean familial fever in two patients, Crohn's disease in one patient, Hodgkin's lymphoma in one patient, and multiple myeloma in one patient. Specific treatment was initiated with colchicine in seven patients. At a 110-month mean follow-up (range 53 to 153 months), remission of nephrotic syndrome was observed in four cases, progression to chronic renal failure in two patients, and to end-stage renal failure in five cases (range 53 to 196 months), with stabilization of renal function in seven patients. In conclusion, primary amyloid disease should be optimally suppressed in patients with renal involvement. The role of this treatment in remission of renal amyloidosis is not well established. This efficacy of the treatment has been demonstrated in some patients with improved survival.

Adult↗
PubMed2005

Effect of amyloidosis on long-term survival in kidney transplantation.

Amyloidosis is characterized by the accumulation of an amorphous material in various organs and tissues secondary to a variety of inflammatory, immune, infectious, and hereditary diseases. Since 1975, our transplantation team has performed 1470 renal transplantations. Between 1985 and July 2004, among 1159 kidney transplantations, 953 (82.3%) were from living donors and 206 (17.7%) from cadaveric donors. There were 32 recipients (28 men, 4 women; mean age, 31.4 +/- 1.7 years; range, 21 to 48 years) with amyloidosis, including, 28 (87.5%) who received grafts from living donors and 4 (12.5%) from cadaveric donors. Amyloidosis was secondary to familial Mediterranean fever in 22 (68.7%) patients and rheumatoid arthritis in 1 (3.1%). The remaining 9 (28.1%) patients had primary amyloidosis. The mean follow-up time was 51.2 +/- 5.7 months (range, 2-124 months). Mean HLA mismatch rate was 2.2 +/- 1. Twenty-six (81.2%) patients are alive at this time with functioning grafts, and a mean serum creatinine value of 2.1 +/- 1.5 ng/dL. The 1- and 5-year patient and graft survival rates were 90.6% and 84.3%, and 81.2% and 68.7%, respectively. We conclude that patients with amyloidosis may undergo kidney transplantation safely expecting outcomes similar to those patients who receive transplantations for other reasons.

Adult↗
PubMed2006

Outcome of kidney transplantation for renal amyloidosis:a single-center experience.

The aim of this retrospective study was to investigate the results of kidney transplantation in patients with renal amyloidosis. We analyzed the results of renal transplantation in 13 amyloidotic transplant recipients compared with those in a control group of 13 nonamyloidotic patients. While the etiology of amyloidosis was rheumatoid arthritis in one patient, in all of the others it was secondary to familial Mediterranean fever. Acute rejection episodes developed once in six and twice in one patient. The renal function in these patients was improved by antirejection treatment. Chronic rejection did not develop in any patient. However six patients (46%) died due to various complications despite functional grafts. The others are still being followed with well-functioning grafts. Among the control group, acute and chronic rejection were diagnosed in three and two patients, respectively: one patient returned to hemodialysis after 26 months of transplantation, while the others are still alive with functional grafts. There was no death in the control group. The 5- and 10-year actuarial patient survival rates of the amyloidosis and control groups were 52.2%, 26.6%, and 100%, 100%, respectively (P = .002). However, the graft survivals of the amyloidosis versus control groups were 100%, 100%, versus 87.5%, 87.5, respectively (P = .47). In conclusion, we observed a high rate of early mortality among recipients with amyloidosis associated with infectious complications. Moreover, patient survivals were lower among amyloidotic renal recipients.

Actuarial Analysis↗
PubMed2000

Systemic amyloidosis presenting as a mass of the conjunctival semilunar fold.

PURPOSE: To report a case of systemic amyloidosis that presented as a mass of the plica semilunaris (semilunar fold) of the conjunctiva. METHODS: Case report. RESULTS: A healthy 56-year-old man developed a fleshy, hemorrhagic lesion of the semilunar fold of the left conjunctiva. Excisional biopsy revealed an acellular lesion of the conjunctival stroma that stained positively for Congo red and showed apple-green birefringence and dichroism with polarization microscopy. The diagnosis was amyloidosis of the semilunar fold of the conjunctiva. Subsequent evaluation disclosed systemic amyloidosis. The patient remains asymptomatic. CONCLUSIONS: Although conjunctival amyloidosis usually occurs as a localized lesion without systemic involvement, it can be the initial sign of systemic amyloidosis.

Amyloidosis↗
PubMedDate not supplied

Ocular amyloidosis, with special reference to the hereditary forms with vitreous involvement.

The complex of diseases referred to as amyloidosis is characterized by the deposition of amyloid substance in various tissues. The amyloid protein differs in the various forms of amyloidosis. This variation is the basis of the differences in affected tissues and subsequent clinical dissimilarities. Vitreous involvement in amyloidosis seems to be especially linked to some of the hereditary neuropathies associated with the amyloid protein transthyretin. Characterization of the amyloid proteins during recent decades has allowed a chemical and immunologic classification of amyloid fibrils. This paper presents the basis for classification of amyloidosis, reviews the literature on ocular amyloidosis, with special reference to vitreous involvement, and summarizes clinical findings and frequency of vitreous amyloid involvement in Swedish patients with familial amyloidotic polyneuropathy.

Adolescent↗
PubMed1988

Morphologic differences in the pattern of liver infiltration between systemic AL and AA amyloidosis.

Biopsy and necropsy tissue from 31 unselected patients with systemic amyloidosis, in which there was histologic evidence of liver involvement, were reviewed with reference to the location and pattern of amyloid deposition in the liver. Amyloidosis was classified into AA and AL types on the basis of immunohistochemistry and permanganate reaction of the amyloid deposits. Nineteen were categorized as AA (secondary) and 12 as AL (primary) amyloidosis. Deposition of AA amyloid was limited to the walls of vessels in the portal tract, constituting a "vascular" pattern. In AL amyloidosis, the deposits exhibited a "sinusoidal" pattern in that they were seen along hepatic sinusoids as well as in vessel walls. This difference was statistically significant (P less than .001). The histologic pattern of liver infiltration offers a valuable clue in the classification of systemic amyloidosis and provides information that may be useful in the selection of patients for therapy.

Amyloid↗
PubMed2001

Amyloid load and clinical outcome in AA amyloidosis in relation to circulating concentration of serum amyloid A protein.

BACKGROUND: Reactive systemic (AA, secondary) amyloidosis occurs in chronic inflammatory diseases, and most patients present with nephropathy. The amyloid fibrils are derived from the circulating acute-phase reactant serum amyloid A protein (SAA), but the relation between production of fibril precursor protein, amyloid load, and clinical outcome in AA and other types of amyloidosis is unclear. METHODS: We studied amyloidotic organ function and survival prospectively for 12-117 months in 80 patients with systemic AA amyloidosis in whom serum SAA concentration was measured monthly and visceral amyloid deposits were assessed annually by serum amyloid P component scintigraphy. Underlying inflammatory diseases were treated as vigorously as possible. FINDINGS: Amyloid deposits regressed in 25 of 42 patients whose median SAA values were within the reference range (<10 mg/L) throughout follow-up, and amyloidotic organ function stabilised or improved in 39 of these cases. Outcome varied substantially among patients whose median SAA concentration exceeded 10 mg/L, but amyloid load increased and organ function deteriorated in most of those whose SAA was persistently above 50 mg/L. Estimated survival at 10 years was 90% in patients whose median SAA was under 10 mg/L, and 40% among those whose median SAA exceeded this value (p=0.0009). INTERPRETATION: Although isolated amyloid fibrils are stable in vitro, AA amyloid deposits exist in a state of dynamic turnover, and outcome is favourable in AA amyloidosis when the SAA concentration is maintained below 10 mg/L. The potential for amyloid to regress and for the function of amyloidotic organs to recover support therapeutic strategies to decrease the supply of amyloid fibril precursor proteins in amyloidosis generally.

Adolescent↗
PubMed1987

A genetic marker for systemic amyloidosis in juvenile arthritis.

A genetic marker of susceptibility to systemic amyloidosis has been identified. A DNA polymorphic site, 5' to the serum amyloid P component gene, has been found to be significantly associated with amyloidosis in juvenile arthritic patients. When genomic DNA was cut with the restriction enzyme MspI and probed with the cDNA for serum amyloid P component, homozygosity for the 5.6 kb restriction fragment length polymorphic (RFLP) band was absent in all 28 amyloid patients. Furthermore, the proportion who were homozygous for the 8.8 kb RFLP band was greater (p = 0.008) than that among 89 normal subjects. The distribution of this polymorphic site among 19 juvenile arthritic patients without amyloidosis was the same as that in the normal group. Thus the 8.8 kb RFLP band represents a genetic predisposition to reactive amyloidosis in juvenile arthritis and may apply to amyloidosis associated with more common inflammatory conditions.

Adult↗