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PubMed2002

Hereditary renal amyloidosis caused by a new variant lysozyme W64R in a French family.

BACKGROUND: The number of proteins with mutations resulting in amyloidosis has continued to increase. Five proteins--transthyretin, fibrinogen alpha-A chain, apolipoprotein AI, lysozyme, apolipoprotein AII, cystatin C and gelsolin--can be associated with hereditary amyloidosis involving the kidney. METHODS: A French family with a history of autosomal dominant hereditary amyloidosis with early sicca syndrome and nephropathy leading to renal failure after the fifth to the seventh decade was studied. Several tissue specimens obtained from the proband and his relatives were examined. Immunohistochemistry was performed on paraffin embedded sections using the indirect immunoperoxidase technique. We searched for mutations in the five exons and flanking introns of the lysozyme gene. RESULTS: Amyloid deposits from the bowel, labial salivary gland and kidney were intensively stained by anti-lysozyme antibody. Sequence analysis of lysozyme exon 2 from the affected individuals revealed a nucleotide substitution predicting a substitution of the amino acid at position 64 in the mature protein from tryptophane, an aromatic residue to the cationic residue arginine (W64R). CONCLUSION: We report a novel mutation (W64R) of the lysozyme that is associated with hereditary amyloidosis and prominent nephropathy. Since the treatment of hereditary amyloidosis greatly varies with the nature of the amyloid protein, thorough characterization of the latter is crucial for the management of the disease.

Aged↗
PubMed2001

Localized amyloidosis and extramedullary plasmacytoma involving the larynx of a child.

Extramedullary plasmacytoma of the larynx and localized laryngeal amyloidosis are 2 uncommon disease entities that are exceedingly rare in children. We report a case of a 12-year-old girl presenting with progressive hoarseness who was subsequently found to have extramedullary plasmacytoma coexisting with localized amyloidosis involving the larynx. Results from the immunohistochemical and molecular studies showed that the tumor cells of the plasmacytoma were monoclonal (kappa-restricted), strongly supporting their neoplastic nature. The biochemical nature of the amyloid deposits was also shown to be of kappa immunoglobulin light chain, suggesting the pathogenetic relationship between the plasmacytoma and amyloid deposition in the larynx of this patient. There was no other evidence of malignancy or amyloidosis elsewhere. On a follow-up period of 4 years, this patient was well and asymptomatic. We believe that this represents the first case in the literature showing the coexistence of extramedullary plasmacytoma and localized amyloidosis of the larynx in children. This case also supports the concept that localized laryngeal amyloidosis may be a manifestation of low-grade B-cell neoplasms.

Amyloidosis↗
PubMed2001

Subcutaneous nodular amyloidosis: a case report and review of the literature.

Amyloidosis typically manifests with disseminated infiltration of multiple organ systems. Rarely, amyloidosis may be localized. We report a patient with localized subcutaneous nodular amyloidosis, without systemic amyloid involvement or myeloma, whose presenting symptom was multiple discrete neck nodules. Immunohistochemical analysis showed the amyloid deposits to be derived from lambda light chains. Twenty-four month follow-up showed minimal disease progression. A literature review showed only 5 reported cases of subcutaneous nodular amyloidosis. This is the first description of a patient with subcutaneous nodular amyloidosis derived from lambda light chains. HUM PATHOL 32:346-348.

Adult↗
PubMed2006

AH amyloidosis associated with lymphoplasmacytic lymphoma secreting a monoclonal gamma heavy chain carrying an unusual truncated D segment.

To date, the presence of amyloidosis associated with immunoglobulin heavy chain (AH amyloidosis) was reported in only 7 cases. Although AH amyloidosis is caused mainly by plasma cell dyscrasia, as in AL amyloidosis, we report a 61-year-old patient who presented with nephrotic syndrome caused by AH amyloidosis associated with lymphoplasmacytic lymphoma. Biochemical and molecular analyses of the deposited amyloid fibrils and heavy-chain genes of lymphocytes showed that proliferative lymphoma cells produced a gamma heavy chain, not a mu heavy chain, which carried an unusual truncated diversity (D) segment of the variable region. Our results indicate that production of the abnormal heavy chain caused by the partially deleted D segment gene is responsible for gamma heavy-chain-related amyloid fibril formation in this patient.

Amyloidosis↗
PubMed1998

[Surgical ENT therapy of oropharyngeal amyloidosis].

BACKGROUND: The term "amyloidosis" refers to a disturbance of metabolism with a pathological deposit of extracellular protein. There are two types of amyloidosis, both of which can have oropharyngeal manifestations. The amyloid deposits cause dysfunction of affected tissues and could result in a life-threatening obstruction of neighbouring organs or the upper aerodigestive tract. CASE REPORT: The present paper reports about the symptoms, diagnosis, and surgical treatment of oropharyngeal amyloidosis. The possible life-threatening obstruction of the upper aerodigestive tract by amyloidosis is illustrated in a case report. CONCLUSIONS: Surgical treatment is indicated in cases of amyloid caused obstruction of the upper aerodigestive tract. The transoral approach combined with a laser surgical tissue resection is often not efficient where diffuse amyloid muscular deposits are present in the form of macroglossia with induration of the floor of the mouth. An effective surgical treatment of oropharyngeal amyloidosis consists of suprahyoid pharyngotomy with a partial tongue resection and a supplementary reduction of the induration of the floor of the mouth.

Airway Obstruction↗
PubMed1990

Evaluation of systemic amyloidosis by scintigraphy with 123I-labeled serum amyloid P component.

BACKGROUND: In systemic amyloidosis the distribution and progression of disease have been difficult to monitor, because they can be demonstrated only by biopsy. Serum amyloid P component (SAP) is a normal circulating plasma protein that is deposited on amyloid fibrils because of its specific binding affinity for them. We investigated whether labeled SAP could be used to locate amyloid deposits. METHODS: Purified human SAP labeled with iodine-123 was given intravenously to 50 patients with biopsy-proved systemic amyloidosis--25 with the AL (primary) type and 25 with the AA (secondary) type--and to 26 control patients with disease and 10 healthy subjects. Whole-body images and regional views were obtained after 24 hours and read in a blinded fashion. RESULTS: In the patients with amyloidosis the 123I-SAP was localized rapidly and specifically in amyloid deposits. The scintigraphic images obtained were characteristic and appeared to identify the extent of amyloid deposition in all 50 patients. There was no uptake of the 123I-SAP by the control patients and the healthy subjects. In all patients with AA amyloidosis the spleen was affected, whereas the scans showed uptake in the heart, skin, carpal region, and bone marrow only in patients with the AL type. Positive images were seen in six patients in whom biopsies had been negative or unsuccessful; in all six, amyloid was subsequently found on biopsy or at autopsy. Progressive amyloid deposition was observed in 9 of 11 patients studied serially. CONCLUSIONS: Scintigraphy after the injection of 123I-SAP can be used for diagnosing, locating, and monitoring the extent of systemic amyloidosis.

Adult↗
PubMed2002

Amyloidosis of the tongue as a paraneoplastic marker of plasma cell dyscrasia.

OBJECTIVE: Our objective was to study the results of the medical workup in patients with amyloidosis of the oral cavity. STUDY DESIGN: Patients diagnosed with amyloidosis of the oral cavity during the period from January 1971 to January 2001 at the Departments of Oral and Maxillofacial Surgery/Oral Pathology and Dermatology of the VU University Medical Center, Amsterdam, The Netherlands, were included in this retrospective case study. In total, this series comprised 11 patients, 9 women and 2 men. The patients' medical workup and final diagnoses were traced by means of the medical records. RESULTS: All but one patient presented with amyloidosis of the tongue, most of them manifesting as macroglossia. In 7 of the 11 included patients a diagnosis of myeloma could be established shortly after their referral to the above-stated departments. Three of the 4 remaining patients appeared to have a monoclonal gammopathy of undetermined significance, and 1 patient was diagnosed with a lymphoplasmacytoid non-Hodgkin lymphoma (immunocytoma). CONCLUSIONS: Amyloidosis of the oral cavity predominantly involves the tongue, mainly manifesting as macroglossia. Amyloidosis of the tongue is associated with an occult underlying plasma cell dyscrasia, in particular myeloma, and, therefore, should be regarded as a paraneoplastic phenomenon of these hematologic diseases.

Aged↗
PubMed1990

Immunoglobulin heavy-chain-associated amyloidosis.

Immunoglobulin- or multiple myeloma-associated amyloidosis has been distinguished by the tissue deposition of Congophilic, fibrillar protein consisting of light chains or light-chain fragments (AL amyloidosis). We now report the isolation and characterization of another form of immunoglobulin-associated amyloid obtained from a patient who had extensive systemic amyloidosis and in whom the amyloid deposits consisted not of light chains but rather of an unusual form of heavy chain. This component, isolated from splenic amyloid extracts, represented an internally deleted IgG1 heavy chain as evidenced by immunochemical, electrophoretic, and amino acid sequence analyses. A comparable immunoglobulin-related monoclonal protein, consisting only of IgG heavy chains, was present in the patient's urine. Based on serologic reactivity with a battery of anti-immunoglobulin antisera, these two immunoglobulin-related components were antigenically identical; however, when compared to normal IgG, both were deficient in Fc-associated gamma-chain determinants. The structural abnormality of the amyloid gamma-chain protein was further evidenced by SDS/PAGE and immuno-blotting analyses: An unusually low molecular mass of approximately 22 kDa was found for this material vs. the expected value of approximately 55 kDa for a normal gamma heavy chain. Despite the lack of certain Fc determinants, the amyloid and urinary heavy-chain proteins expressed the IgG1 subclass allotype marker G1m(a) located on the third constant region (CH3) domain of the internally deleted IgG1 heavy chains. That the amyloid protein contained an intact CH3 domain was established through amino acid sequence analyses of cyanogen bromide fragments and peptides generated by a lysine-specific protease. These studies also revealed that the gamma-chain amyloid protein contained the complete heavy-chain variable (VH) domain [including the diversity (DH) and joining (JH) segments] that was contiguous with the CH3 domain. The low molecular mass of the protein resulted from the total absence of the first (CH1), hinge, and second (CH2) heavy-chain constant regions. Such extensive CH deletions and the presence of a complete VH distinguish this amyloid-associated heavy chain from all other heretofore characterized gamma-heavy-chain disease proteins. This heavy-chain-related form of immunoglobulin-associated amyloidosis is tentatively designated AH amyloidosis.

Aged↗
PubMed1980

A chemical classification of amyloid. Correlation with different clinical types of amyloidosis.

Results of recent research have made it possible to classify amyloidosis by means of the chemical and antigenic characteristics of the amyloid fibrils. The chemical classification of amyloid correlates quite well with the various clinical types of amyloidosis. Monoclonal immunoglobulins constitute a major part of primary amyloid fibrils, while amyloid protein AA plays a similar role in secondary amyloidosis. In addition, structural properties of amyloid fibril proteins derived from medullary carcinoma of the thyroid and from senile cardiac amyloidosis respectively, have been shown to be unique for these clinical types of localized amyloidosis. A protein identical or similar to prealbumin appears to constitute an amyloid fibril subunit in familial amyloidotic polyneuropathy. However, the mechanisms by which the various amyloid precursor proteins are converted to fibrils and deposited in the tissues are still not clear.

Amyloid↗
PubMed1998

Treatment of amyloidosis and the rheumatologist. State of the art and perspectives for the future.

The rheumatologist must be prepared to face diagnostic and therapeutic problems related to different categories of amyloidosis. This applies to the systemic AA amyloidosis that complicates chronic inflammatory arthropathies like adult and juvenile rheumatoid arthritis, causing nephropathy and various internal manifestations. Other types of amyloidosis are essential because they may localize to structures of the locomotor system and cause rheumatic complaints. At present, there is no cure for amyloidosis. But adequate and especially early therapeutic intervention is helpful in many cases. This review focuses on treatment of the categories of amyloidosis which are most relevant to the rheumatologist. In addition to treatments that are available today, more effective therapeutic modalities which hopefully will be available in the near future are also reviewed.

Amyloidosis↗
PubMed2005

Quantitative serum free light chain assay in the diagnostic evaluation of AL amyloidosis.

We compared a new serum immunoassay for quantitation of serum free light chains (FLC) with the conventional tests for clonal immunoglobulin production: bone marrow immunohistochemistry, serum immunofixation electrophoresis, and urine immunofixation electrophoresis. Serum samples from 169 patients with AL amyloidosis and 20 controls were examined. Elevated levels of kappa-FLC and lambda-FLC were found in 94% and 93% of patients with the respective clonal disease. However, false positive elevations of kappa-FLC and lambda-FLC were found in 30% and 44% of patients with clonal disease of the other light chain subtype. We found that the FLC level was a reliable test for the diagnosis of clonal disease when the FLC kappa:lambda ratio was abnormal and was comparable to the conventional tests in patients with AL amyloidosis. After a histologic tissue diagnosis of amyloidosis, determining the type as AL amyloidosis relies on a panel of hematologic tests to determine light chain clonality and the exclusion other forms of amyloidosis.

Adult↗
PubMed2005

Acceleration of murine amyloidosis by implantation of amyloid-containing grafts.

We examined the transmissibility of amyloidosis by the implantation of amyloid-containing tissue. If the transmissibility similar to prion diseases is applicable, using amyloid-containing tissue for transplantation in humans might be a risk factor. In this study, AA amyloidosis occurred in mice that underwent implantation of AA amyloid-containing grafts to the liver and subsequent inflammatory stimulation. AApoAII amyloidosis occurred after implantation of AApoAII amyloid-containing grafts to the liver or to the subcutaneous space without inflammatory stimulation. Both types of amyloidoses occurred in the recipient mice sooner than expected. Moreover, AA and AApoAII amyloid deposits were found at 12 weeks after implantation in mice given AApoAII amyloid-containing grafts and inflammatory stimulation. These results suggest that implanted amyloid deposits have an AEF effect and that implanted amyloid-containing tissue can promote and accelerate a different type of amyloidosis. In another experiment, mice received amyloid-containing or normal tissue grafts. The degree of amyloid deposition was compared after 6 days and 5 weeks of inflammatory stimulation and when the mice were killed. There was no obvious difference in the degree of amyloid deposition between each group, indicating that the lag-time is shortened by implantation of amyloid-containing tissue, resulting in severe amyloidosis in the short term.

Amyloid↗
PubMed2002

Cholestasis and renal failure in a patient with secondary amyloidosis.

Amyloid, was first described in the 19th century by Virchow, which means starch or cellulose. Extracellular deposition of this unique protein fibrils in tissues, often leading organ dysfunction is known as amyloidosis. In systemic amyloidosis, amyloid fibrils may deposit in different organs including kidneys, heart and liver. Although liver is effected frequently, clinical liver disease is rare. There are a few cases that secondary amyloidosis presented with hepatic involvement and cholestasis which seems to be limited to primary amyloidosis. Hepatic amyloidosis with cholestasis may be a predictor of involvement of other organs and thus of poor prognosis. We report a case of a 67 year old man with renal failure and prominent cholestasis due to AA amyloid deposition in the liver.

Aged↗
PubMed2005

Tissue Doppler is a more reliable method in early detection of cardiac dysfunction in patients with AA amyloidosis.

OBJECTIVE: Cardiac deposition of AA amyloidosis may result in increasing left ventricular mass and systolic and diastolic dysfunction (DD). The aim of this study was to investigate the left ventricular systolic and diastolic functions by both tissue Doppler imaging (TDI) and pulsed wave Doppler echocardiography (PWD) in patients with AA amyloidosis without congestive heart failure symptoms or arrthymia. METHODS AND RESULTS: Twenty-four patients with AA amyloidosis without congestive heart failure symptoms or arrthymia (15 men and nine women; mean age 44.3 +/- 16.7 years) and 25 healthy subjects (19 men and six women; mean age 43.1 +/- 9.2 years) as controls were included in the study. M-mode, two-dimensional, PWD, and TDI were performed. Peak transmitral filling velocity (E wave), peak transmitral atrial filling velocity (A wave), deceleration time, and isovolumic relaxation time were measured by PWD recordings. Peak myocardial systolic velocity (Sm), peak myocardial early (Em), and late diastolic velocities (Am) were also recorded by TDI. E/A ratio less than one was accepted as DD for both methods. Ejection fraction (EF) was calculated by Teicholtz method. The subjects were divided into three groups as follows: healthy controls (group 1), patients without DD (group 2), and patients with DD (group 3) according to the PWD findings. PWD echocardiography showed that DD was present in 50% of the patients, whereas TDI showed DD in 66% of such cases. In subgroup analysis, Sm wave as a systolic function index was lower in group 3 than in groups 1 and 2, whereas mean EF values were similar in all groups. CONCLUSION: Although AA amyloidosis uncommonly causes cardiac symptoms and findings, according to our results, patients with AA amyloidosis may have systolic and diastolic dysfunction eventhough they are asymptomatic. Also, tissue Doppler imaging is a more reliable method in the early detection of cardiac dysfunction in such patients.

Adult↗
PubMed2001

Amyloid goiter as the initial manifestation of systemic amyloidosis due to familial mediterranean fever with homozygous MEFV mutation.

We describe a case of amyloid goiter revealing a systemic amyloidosis secondary to familial Mediterranean fever (FMF) with homozygous MEFV mutation, and we review the literature. A 45-year-old euthyroid Sephardic man, known to suffer from FMF, developed a goiter with cold nodule, after which a subtotal thyroidectomy was performed. Histologic evaluation revealed diffuse AA amyloid deposition without any associated thyroid neoplasia. At that time, no other organ was found to be affected by amyloidosis. Colchicine and levothyroxine were prescribed. Eight years later, the patient presented with a rapidly growing neck enlargement. He reported that he had discontinued colchicine therapy 2 years earlier. The serum thyrotropin (TSH) and calcitonin levels were normal. Renal, digestive, and salivary gland biopsies confirmed the presence of systemic AA amyloidosis. Despite the reintroduction of colchicine, the onset of compressive symptoms led to the completion of the total thyroidectomy. The histopathology again demonstrated amyloid deposition, and excluded a malignant neoplasm. Nine cases of amyloid goiter associated with FMF have been reported in the literature; none of them had an amyloid goiter as the first manifestation of systemic amyloidosis. To our knowledge, this is the first case of FMF in which an amyloid goiter preceded the development of secondary systemic amyloidosis. The cessation of colchicine therapy may have played a role in local relapse and the secondary spread of amyloid deposits.

Amyloidosis↗
PubMed2006

Nutritional status of outpatients with systemic immunoglobulin light-chain amyloidosis 1.

BACKGROUND: Maintenance of a good nutritional status is associated with prolonged survival in many chronic diseases. To date, the nutritional status of outpatients with immunoglobulin light-chain (AL) amyloidosis has not been evaluated. OBJECTIVE: The aims of this study were to obtain information regarding the nutritional status of AL amyloidosis outpatients and to investigate its prognostic role. DESIGN: One hundred six consecutive patients with histologically confirmed AL amyloidosis were enrolled. Anthropometric, biochemical, and clinical variables were measured. The Kaplan-Meier method was used to calculate survival. A Cox proportional hazard model was constructed to evaluate the prognostic effect of the nutritional variables. RESULTS: Unintentional weight loss (median: 11.3%; range: 2.6-34% of usual nonedematous body weight) was documented in 58 subjects (54.7%). Body mass index (BMI; in kg/m2) was <22 in 25 subjects (23.6%). Serum prealbumin was <200 mg/L (lower reference limit) in 26 patients (24.5%). A multivariate analysis showed that the percentage weight loss was significantly greater in patients with than in those without cardiac involvement (P = 0.03), and it also differed significantly by New York Heart Association class (P = 0.02) and Eastern Cooperative Oncology Group performance status (P = 0.001). Cardiac involvement (P = 0.008), hematologic response to therapy (P = 0.013), BMI (P = 0.001) and serum prealbumin (P = 0.001) were independent predictors of survival. CONCLUSIONS: Malnutrition is a prominent clinical feature of patients with AL amyloidosis. Appropriate nutritional evaluation that comprises the easily measurable nutritional variables associated with survival should be an integral part of the clinical assessment of AL amyloidosis outpatients.

Adult↗
PubMed1993

Tumoral presentation of amyloidosis (amyloidomas) in soft tissues. A report of 14 cases.

Amyloidosis in its diverse types (immunocytic dyscrasia-associated, reactive, or heredofamilial) most often presents in a systemic form. Localized amyloidosis is uncommon in general and is exceedingly rare in the soft tissues. The authors discuss the cases of 14 patients in whom amyloidosis manifested as a localized mass ("amyloidoma") in the soft tissues (mostly mediastinal and retroperitoneal), leading to a clinical diagnosis of neoplasm in most cases. On the basis of the associated morphologically atypical and phenotypically monoclonal cell population, the resistance to potassium permanganate pretreatment, and the lack of reactivity with anti-AA antisera, 10 cases could be classified as immunocytic dyscrasia-associated AL-amyloidosis. However, four cases had histopathologic and histo- and immunohistochemical characteristics of reactive ("secondary") AA-amyloidosis. This proportion (28.5%) was higher than that suggested by the sporadic AA-amyloidomas reported in the literature. The pathologic distinction between these two categories is important because patients with AA-amyloidomas of the soft tissues appear to have a better prognosis.

Adult↗
PubMed1993

Localized pleural microdeposition of type A amyloid in a patient with rheumatoid pleuritis. Histologic distinction from pleural involvement in systemic amyloidosis.

Decorticated pleural tissue from a 74-year-old man with rheumatoid arthritis, an exudative pleural effusion, and normal left ventricular function contained microscopic deposits of amyloid A protein, localized to the interface between a deep layer of dense fibrocollagen and a layer of granulation tissue beneath a surface fibrin exudate. Previously reported instances of pleural amyloid deposition have occurred in patients with presumed systemic amyloidosis, and most such effusions are the result of congestive heart failure. This patient had no evidence of systemic amyloidosis, and this case appeared to be an example of an unusual form of localized amyloidosis, so-called periinflammatory amyloidosis A. These observations suggest that amyloid in a pleural biopsy should not be construed per se to be diagnostic of systemic amyloidosis.

Aged↗