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PubMed1998

The assessment of autonomic function in patients with systemic amyloidosis: methodological considerations.

Autonomic neuropathy is a well-known and prognostically important feature of systemic amyloidosis. In other conditions, autonomic function is commonly assessed by cardiovascular reflex tests, described by Ewing, but the feasibility of these tests has not been investigated in patients with systemic amyloidosis. We studied autonomic function in amyloidotic patients using cardiovascular tests and assessed their feasibility. Patients with AA, AL and ATTR amyloidosis participated. In all patients, cardiovascular reflex testing (mental arithmetic stress test and head-up tilting, besides the Ewing-tests) was performed. Of the 46 patients included, only 28 patients could perform all 4 Ewing-tests. In particular, patients with AA amyloidosis secondary to rheumatoid arthritis could not perform standing up and the isometric handgrip test. However, when the mental stress test replaced the handgrip test and head-up tilting replaced standing up, in 45 of the 46 patients, autonomic function could be assessed with cardiovascular reflex tests. Half of the patients with AA amyloidosis had signs of autonomic neuropathy--which was more than expected. We propose to replace the isometric handgrip test with the mental arithmetic stress test and standing up with head-up tilting if a patient is not able to perform these tests.

Adolescent↗
PubMed1998

SAA1 alleles as risk factors in reactive systemic AA amyloidosis.

SAA1 is the predominant isoform of acute phase human SAA deposited as AA amyloid fibrils in reactive systemic amyloidosis. It has recently been reported that in the Japanese population, in whom the SAA1 gamma allele occurs with a frequency of 37%, possession of, and especially, homozygosity for this allele is a significant risk factor for AA amyloidosis in adult patients with rheumatoid arthritis (RA). In contrast we report here that in a control sample of 95 healthy adult male Caucasians the SAA1 gamma allele occurs at the much lower frequency of 5.3% and that, among 41 patients with juvenile chronic arthritis (JCA) and AA amyloidosis, there was a highly significantly increased frequency of the SAA1 alpha allele (90.2%), and particularly homozygosity for this allele (80.5%), compared both to the healthy controls (75.8% and 57.9% respectively) and to 8 JCA cases without amyloid (56.3% and 12.5%). A similar trend with respect to frequency of the SAA1 alpha allele and homozygosity for it was observed among 26 adult Caucasian RA patients with AA amyloid and 26 such cases without amyloid, although it did not reach statistical significance. These results suggest that there is probably differential amyloidogenicity amongst the different SAA1 isoforms and indicate that homozygosity for SAA1 alpha and SAA1 gamma in the different populations is a significant risk factor for development of AA amyloidosis. In Caucasian patients with JCA, the presence of the homozygous SAA1 alpha genotype indicates high risk of amyloidosis and should encourage early and aggressive anti-inflammatory therapy to keep circulating SAA levels as low as possible.

Adult↗
PubMed2001

Effect of losartan treatment on the proteinuria in normotensive patients having proteinuria due to secondary amyloidosis.

Secondary amyloidosis (AA amyloidosis) is a well known cause of nephrotic syndrome and renal failure. Several studies in patients with nephrotic syndrome have suggested a beneficial effect of angiotensin-converting enzyme inhibitors (ACEI). Angiotensin II (ATII) receptor antagonists effect on the long term is not known. In this study, we intended to study the effect of losartan, as an ATII receptor antagonist, on proteinuria and renal functions in patients with normotensive secondary amyloidosis. In total 44 patients with biopsy proven AA amyloidosis associated with nephrotic proteinuria were included. The first group of patients (n=22) was treated with losartan 50 mg/day. The second group of patients (n=22) did not receive any specific antiproteinuric treatment. Urinary protein loss was effectively lowered by losartan from 4.38 +/- 1.0 to 2.8 +/- 0.61 g/day (p<0.0001), whereas the control group showed a slight fall in proteinuria as 4.21 +/- 1.06 to 4.12 +/- 1.07 g/day (p = 0.176). Hypoalbuminemia improved significantly from 2.52 +/- 0.69 to 2.78 +/- 0.46 g/dl (p = 0.004), in the losartan group, whereas serum albumin had fallen in the control group from 2.44 +/- 0.57 to 2.27 +/- 0.41 (p = 0.041). Serum creatinine increased in the control group from 1.52 +/- 0.42 to 2.39 +/- 0.51 mg/dl (p<0.0001), and in the losartan group from 1.59 +/- 0.50 to 1.84 +/- 0.6 mg/dl (p<0.001), after 24 months of treatment. The ATII receptor blocker losartan is effective in protecting against the progression of nephropathy due to AA amyloidosis. Symptomatic treatment of proteinuria with losartan is therefore to be considered, especially with severe proteinuria even in normotensive patients.

Adult↗
PubMed1988

Hepatic amyloidosis--two cases report.

Amyloidosis is classified according to the distribution pattern of amyloid deposition sites and associated diseases. Hepatic amyloidosis is not infrequent, although rarely causes clinical liver disease. We report two cases of amyloidosis diagnosed by liver biopsy. One presented with symptoms related almost to the liver disease, such as jaundice, hepatomegaly and indigestion. Echocardiogram revealed hypertrophic cardiomyopathy, suggesting cardiac involvement of the amyloidosis. The patient died of hepatic failure. The other case was found in a patient with an end stage renal disease. Features of congestive heart failure in this case may reflect cardiac involvement. The pattern of hepatic amyloid deposition in both of these cases was diffuse perisinusoidal. The predominant intralobular deposition suggests that these are amyloidosis of the secondary type.

Amyloidosis↗
PubMed2003

A case report of localized gastric amyloidosis.

AIM: To elucidate the clinical and laboratory features of localized gastric amyloidosis via a rare report along with a review of related literatures. METHODS: The clinical manifestations, laboratory results and surgical treatment of a female patient with localized gastric amyloidosis in our hospital were summarized. The relevant literatures were reviewed on the etiology, clinical features, diagnosis, treatment and prognosis of this disease. RESULTS: The patient was lack of specific clinical manifestations and positive laboratory results. Prior to the treatment, she was suspected to be of malignization from gastric ulcer by both gastroscopy and endoscopic ultrasonography, which was denied by the gastric biopsy. The patient was treated with subtotal gastrectomy and clearance of perigastric lymph nodes. The postoperative pathological diagnosis determined the lesion to be the deposition of amyloid materials in the gastric mucosa, submucosa and blood vessel walls with intestinal metaplasia and atrophy of the gastric glands, in which no malignant tumor was found. Congo red staining with prior potassium permanganate incubation confirmed the AA type of amyloid in this case. Multiple biopsies from esophagus, remnant stomach, duodenum, colon and bone marrow in the follow-up survey showed no amyloidal deposition in these tissues and organs. Up to the present, no signs of recurrence have been found in this patient. CONCLUSION: Localized gastric amyloidosis, being rare in incidence, should be considered in the differentiation of gastric tumors, in which biopsy is the only means to confirm the diagnosis. Currently, surgical resection of pathological tissue and circumambient lymph nodes may be a preferable therapeutic strategy for the localized amyloidosis to prevent possible complications. Although with a benign prognosis, gastric amyloidosis possesses a recurrent tendency as suggested by the literatures.

Amyloidosis↗
PubMed2003

Tolerability and efficacy of thalidomide for the treatment of patients with light chain-associated (AL) amyloidosis.

Thalidomide is an effective therapy for multiple myeloma, although its mechanisms of action remain unclear. Light chain-associated (AL) amyloidosis is a plasma cell disorder related to multiple myeloma, but in AL amyloidosis, fibrillar tissue deposits of clonal immunoglobulin light chains produce organ dysfunction. To test the toxicity and efficacy of thalidomide in AL amyloidosis we initiated a phase I/II trial for patients with AL amyloidosis, most of whom had failed prior therapy with high-dose melphalan and autologous stem cell transplantation. This trial was designed as an individualized 6-month dose-escalation study with reevaluation of bone marrow plasmacytosis and serum and urine monoclonal proteins after 3 and 6 months. Sixteen patients were enrolled in the study with a median age of 62 years (range, 37-70 years). Fourteen patients had renal involvement, 4 had cardiac involvement, 4 had liver involvement, and 2 had predominant soft tissue or lymph node involvement. The median maximum tolerated dose was 300 mg, with fatigue and other central nervous system side effects being the major dose-limiting toxicities. Side effects not frequently reported for other patient populations included exacerbation of peripheral and pulmonary edema and worsening azotemia. In all, 50% of patients experienced grade 3/4 toxicity, and 25% had to discontinue the study drug. No complete hematologic responses were seen, but 25% of patients had a significant reduction in Bence-Jones proteinuria. Thus, while thalidomide has activity in AL amyloidosis, it also has significant toxicity in this patient population.

Adult↗
PubMed2006

Systemic immunoglobulin light-chain amyloidosis.

Amyloidosis is a rare disease in which amyloid fibrils compromise organ function and lead to death. Systemic immunoglobulin light-chain amyloidosis, usually caused by free light chains (FLCs) made by clonal plasma cells, is the most frequent type. Hereditary and senile systemic amyloidosis are less frequent types. Rarely, a patient with a tissue diagnosis of amyloidosis might have a monoclonal gammopathy and a hereditary protein. In systemic immunoglobulin light-chain amyloidosis, circulating clonal light chains can be measured with the FLC assay and provide a target for therapy aimed at eliminating the underlying plasma cell disorder while supporting the patient. Elimination of the pathologic FLC can lead to resorption of amyloid deposits and improvement in organ function. Monthly oral melphalan and dexamethasone for 1 year is effective therapy for patients not eligible for autologous stem cell transplantation (SCT) but carries a risk of myelodysplasia. For patients with limited organ involvement, SCT is an effective approach and, when followed after SCT by adjuvant thalidomide and dexamethasone for persistent plasma cell disease, achieves a high 1-year hematologic response rate. Complete hematologic responses can be durable beyond a decade and are usually associated with organ recovery. New agents, such as bortezomib and lenalidomide, have shown promising activity, and novel monoclonal antibody approaches are also under active investigation.

Amyloidosis↗
PubMed2000

Peripheral nerve amyloidosis in sural nerve biopsies: a clinicopathologic analysis of 13 cases.

OBJECTIVE: Amyloidosis is a well-recognized but uncommon cause of peripheral neuropathy. Our objectives were to determine the overall prevalence of peripheral nerve amyloidosis in sural nerve biopsies and to evaluate the clinical and pathologic features of these lesions. METHODS: All available histologic and ultrastructural materials on biopsy tissue from 13 cases of peripheral nerve amyloidosis were examined. Muscle biopsies performed at the same time as the nerve biopsy were reviewed when available. Clinical data were collected on all patients. RESULTS: The prevalence of amyloidosis in sural nerve biopsies at our institution was 13 (1.2%) of 1098 cases over a 15.8-year period. These patients ranged in age from 41 to 82 years (median, 61 years) at initial presentation and included 10 men and 3 women. Presenting neuropathy symptoms were sensory in 6 of the 13 patients, motor in 2 cases, and mixed in 5 cases. Cardiac, renal, or gastrointestinal involvement was present in 7 of 13 cases. Two patients had myeloma and 7 had systemic autonomic symptoms. Two patients had probable familial amyloid polyneuropathy, and 1 patient demonstrated an alanine 60 point mutation. Amyloid, identified as amorphous eosinophilic extracellular deposits demonstrating apple green birefringence on Congo red stain or recognized by its characteristic fibrillar ultrastructure by electron microscopy, was identified in the endoneurium in 12 nerves, perineurium in 2 nerves, and epineurium in 9 nerves. Chronic inflammation was identified in 5 nerves. Axonal loss was recorded as mild (<25%) in 1 nerve, moderate (25% to 75%) in 8 nerves, and severe (>75%) in 4 nerves. Axonal degeneration predominated over demyelination in 8 of 10 cases that could be evaluated. Concomitant muscle biopsies contained amyloid deposits in 8 of 9 cases. CONCLUSIONS: Amyloidosis is a rare (1.2% in our series) cause of peripheral neuropathy with a distinct microscopic and ultrastructural appearance. Just over half the patients in our study had visceral organ involvement and systemic autonomic symptoms. The peripheral neuropathy was associated with axonal degeneration and a moderate to severe axonal loss in the majority of cases. Amyloid deposition was present in 8 out of 9 muscle biopsies performed at the same time.

Adult↗
PubMed2005

Primary localized laryngeal amyloidosis: report of 3 cases with long-term follow-up and review of the literature.

CONTEXT: Localized laryngeal amyloidosis is an uncommon condition with limited long-term follow-up studies. The precise etiology and pathogenesis are not entirely clear. OBJECTIVE: To further characterize the histopathologic features and possible pathogenesis of localized laryngeal amyloidosis. DESIGN: Three cases of primary localized laryngeal amyloidosis were identified at our institutions from 1980 to 2003. The clinical features and histologic and immunohistochemical patterns were evaluated. Systemic workups were pursued during the long-term follow-up. RESULTS: The common presentation of the patients was hoarseness. The lesions involved vocal cords, anterior commissure, and ventricle. Microscopically, the amyloid was present within the submucosa with an adjacent lymphoplasmacytic infiltrate. The plasma cells and amyloid demonstrated monoclonal light chain restriction in all 3 cases (2 lambda, 1 kappa). No evidence of systemic amyloidosis or an overt B-cell lymphoma was found in these patients. Two patients with long-term follow-up underwent subsequent surgical removals for multiple recurrences, which occurred within 1 year of the initial diagnosis. CONCLUSIONS: The demonstration of monoclonal light chain expression in the plasmacytic infiltrate and amyloid component in the absence of systemic lymphomas indicates that localized laryngeal amyloidosis may represent a form of benign monoclonal plasma cell dyscrasia. A close follow-up of the patients may be indicated for early detection of recurrences.

Adult↗
PubMed1989

Multiple endocrine neoplasia type 2a associated with cutaneous lichen amyloidosis.

PURPOSE: To describe and characterize the association of hereditary cutaneous lichen amyloidosis with multiple endocrine neoplasia type 2a (MEN 2a). DESIGN: Survey of a family for two diseases. SETTING: Evaluation of patients at a clinical research center. PATIENTS: Nineteen family members with MEN 2a. MEASUREMENTS AND MAIN RESULTS: In this family cutaneous lichen amyloidosis presented as multiple infiltrated papules overlying a well-demarcated plaque in the scapular area of the back (right or left). Immunohistochemical studies showed amyloid that stained for keratin but not calcitonin. Three family members had the characteristic skin lesion and also carried the gene for MEN 2a; two additional members carried the gene for MEN 2a, but did not manifest the observable skin changes associated with lichen amyloidosis. CONCLUSIONS: From the findings in this kindred and in another recently reported but unrelated family with an identical type of pruritic skin rash and MEN 2a, several conclusions can be drawn. First, the syndrome of cutaneous amyloidosis and MEN 2a is a clearly defined autosomal dominant hereditary syndrome. Second, the dermal amyloid appears to be caused by deposition of keratin-like peptides rather than by calcitonin-like peptides. Third, known families with hereditary lichen amyloidosis should be screened to determine the true frequency of this syndrome.

Adrenal Gland Neoplasms↗
PubMed1997

[Pleural amyloidosis].

OBJECTIVE: To evaluate the clinical significance of systemic amyloidosis in the differential diagnosis of pleural effusion. METHOD: Retrospective analysis of the incidence and the characteristics of pleural effusion in systemic amyloidosis. RESULTS: Seven (47%) of 15 cases of systemic amyloidosis were complicated with pleural effusion, of them 4 cases were confirmed by positive Congo red stain of percutaneous pleural biopsies specimens. CONCLUSIONS: Systemic amyloidosis involving pleura was not rare. Pleural amyloidosis should be suspected in pleural effusion complicated by multiorgan disease. Percutaneous pleural biopsy with Congo red stain can confirm the diagnosis.

Adult↗
PubMed1999

[Systemic amyloidosis with renal involvement].

Amyloidosis is a summary of a group of disorders of protein metabolism characterized by infiltration of amorphous substance into the tissues. The diagnosis can rarely be made during life. It is usually manifested by defects of the renale, cardiovascular or peripheral nervous system. Heterogenicity of clinical and histological classification of amyloidosis and clinical course in comparison with autopsy findings are presented by two cases of general amyloidosis--secondary amyloidosis of the kidneys and primary amyloidosis with a fatal prognosis.

Amyloidosis↗
PubMed2000

[Primary AA type amyloidosis of the urinary bladder: a case report].

Primary amyloidosis of the urinary bladder is a rare disease entity. A total of 61 cases have been reported in the Japanese literature, and most of them were AL type amyloidosis. We report here a case of primary AA type amyloidosis. A 52-year-old man presented with a chief complaint of asymptomatic gross hematuria. Cystoscopy revealed yellowish elevated lesions, transurethral mucosal biopsies were performed, and the histopathological diagnosis indicated a primary AA type amyloidosis of the urinary bladder. Systemic amyloidosis was clinically eliminated. The yellowish lesions in the bladder through cystoscopy disappeared spontaneously one year later without any specific treatment, but periodical work-up may be necessary to rule out recurrence of the disease or bladder tumor.

Amyloidosis↗
PubMed1999

[Secondary systemic amyloidosis A combined with primary glomerulonephritis and systemic diseases].

Amyloidosis is characterized by organic dysfunction as a result of deposition of amyloid substance in the walls of the small blood vessels and extracellularly in different organs. The involvement of the kidneys in systemic amyloidoses AL and AA has irreversible evolution to renal failure. The object of the study was to determine the prevalence of the secondary (reactive) systemic amyloidosis AA in combination with primary glomerulonephritis (PGN) and lupus nephropathy (SLE) and to create diagnostic approach for its early detection. The prevalence of amyloidosis among the renal biopsies in the Department of Nephrology by the Chair of Internal Diseases for the period 1981-1988, retrospectively, is 4% (in 11 out of 268 biopsies). For the period 1989-1996, prospectively, by directed quest, amyloid was found in 35 out of 269 renal biopsies (11%). For differentiation of AA preliminary treatment of the histologic material with KMnO4 was used. In 20 cases amyloidosis appeared as independent finding in the renal tissue, while in 15 it was combined with histologic picture of immune nephropathies: in 11 with primary glomerulonephritis (7% out of 155 PGN) and in 4 with systemic lupus erythematodes (11% out of 31 SLE). The combination of PGN with AA was almost always associated with chronic infections. It was most often observed in diffuse membranous GN or FSGSH. Our studies demonstrate increased prevalence of amyloidosis among the renal biopsies during the last years, which could be due to directed quest, but it could be a real fact, too. We suggest staining for amyloid in all renal biopsies, as well as its directed quest in mucosae of the gastro-intestinal tract and by aspiration of the abdominal subcutaneous fatty tissue in the patients with primary GN or systemic diseases.

Amyloidosis↗
PubMed2000

Amyloid goiter: the first evidence in secondary amyloidosis. Report of five cases and review of literature.

Amyloid deposition in secondary amyloidosis frequently involves thyroid gland, but rarely is responsible of a goiter. Amyloid goiter in secondary amyloidosis is characterized by deposition of amyloid A protein (AA) in the gland, associated to atrophic follicles. We identified cases of amyloid goiter in the files of our department in the period from 1985 to 1998. Five cases of amyloid goiter with ingravescent symptomatology, characterized by dyspnea, dysphagia and hoarseness were selected. In four cases of five we observed predisposing conditions as, for example, tuberculosis, Crohn's disease, or rheumatoid arthritis. In all cases the symptoms relative to thyroid enlargement preceded or, anyway, predominated over other clinical evidence of systemic amyloidosis. In one case a symptomatology of systemic amyloidosis was not evident. We would like to underline that in all cases the immunoreactivity for amyloid A in the amorphous material present in the gland permitted the diagnosis of secondary amyloidosis even in the absence of systemic symptoms.

Adult↗
PubMed1999

Systemic amyloidosis associated with hepatocellular carcinoma. Case report and literature review.

We describe the case of a male patient with biopsy-proven non-resectable liver adenoma at age 32 who presented 17 years later with hepatocellular carcinoma and nephrotic syndrome. Autopsy demonstrated systemic amyloidosis A. Review of the medical literature disclosed only three previous published cases of liver tumors associated with systemic amyloidosis. The association of non-hematologic neoplasias with systemic amyloidosis is rare and our literature review revealed only three cases of systemic amyloidosis in patients with liver tumors. We present here the case of a patient with apparent transition of liver adenoma to hepatocellular carcinoma with associated systemic amyloidosis.

Adenoma↗
PubMed2001

[Primary systemic amyloidosis presenting as polymyalgia rheumatica and giant cell arteritis].

Primary systemic amyloidosis or AL-amyloidosis is an uncommon disease characterized by the accumulation in vital organs of a fibrillar protein consisting of monoclonal light chains. It is a plasma-cell dyscrasia related to multiple myeloma where clonal plasma cells in the bone marrow produce immunoglobulins that are amyloidogenic. A monoclonal component is present in the serum or urine of 90% of patients. The presentation of most patients with AL amyloidosis is usually related to congestive heart failure, nephrotic syndrome o peripheral neuropathy, but there are unusual features suggesting giant cell arteritis (GCA) and polymyalgia rheumatic (PMR). Although in the majority of AL cases the plasma cells clone is small, the assumption is that the outcome of the disease is uniformly fatal (median survival 12-15 months) and treatment is analogous to those used in malignant proliferative disease. We describe a patient with AL amyloidosis who presented with manifestations of GCA and PMR, and we review the main characteristics of primary amyloidosis.

Aged↗
PubMed2001

Infusion of light chains from patients with cardiac amyloidosis causes diastolic dysfunction in isolated mouse hearts.

BACKGROUND: Primary (AL) amyloidosis is a plasma cell dyscrasia characterized by clonal production of immunoglobulin light chains (LC) resulting in the subsequent systemic deposition of extracellular amyloid fibrils. Cardiac involvement is marked by the hemodynamic pattern of impaired diastolic filling and restrictive cardiomyopathy. Although cardiac death in patients with AL amyloidosis is usually associated with extensive myocardial infiltration, the infiltration alone does not correlated with the degree of heart failure or survival. We hypothesized that circulating monoclonal LC may directly impair cardiac function, in addition to any mechanical effects of amyloid fibril deposition. Therefore, we examined the effects of amyloid LC proteins on diastolic and systolic cardiac function, as measured in an isolated mouse heart model. METHODS AND RESULTS: LC were obtained from patients with nonamyloid disease or from those with noncardiac, mild cardiac, and severe cardiac involved AL amyloidosis. Saline or LC (100 microgram/mL) was infused into a Langendorff-perfused, isovolumically contracting mouse heart. Saline and control, noncardiac, and mild-cardiac LC infusions did not alter ex vivo cardiac function. In contrast, infusion of sever cardiac LC resulted in marked impairment of ventricular relaxation with preservation of contractile function. CONCLUSION: These results demonstrate that infusion of LC from patients with AL amyloidosis result in diastolic dysfunction similar to that observed in patients with cardiac involved AL amyloidosis, and they suggest that amyloid LC proteins may contribute directly to the pathogenesis and the rapid progression of amyloid cardiomyopathy, independent of extracellular fibril deposition.

Amyloidosis↗