Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “AMYLOIDOSIS”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 181 records · Page 10Linked to original sources
PubMed2002

Comparison of gastroduodenal, renal and abdominal fat biopsies for diagnosing amyloidosis in rheumatoid arthritis.

The aim of the study was to determine the frequency of amyloidosis detected by gastroduodenal biopsy in rheumatoid arthritis (RA) patients, and to investigate correlations between the results of gastroduodenal biopsy and abdominal fat and renal biopsies. A total of consecutive 1006 RA patients underwent gastroduodenal biopsy. The 71 patients who tested positive for gastrointestinal (GI) amyloidosis were asked to undergo renal and abdominal fat biopsies, and 21 did so. Renal biopsies were also performed on 12 patients with no amyloidosis but indicators of drug-induced renal damage, and abdominal fat biopsies were performed on 50 RA patients with no indication of amyloidosis. The prevalence of GI amyloidosis was 7.1%. Urinary abnormalities and GI symptoms were common in GI amyloidisis, and inflammatory markers were elevated. Sixty-one (86%) had either depressed creatinine clearance or urinary symptoms. Nineteen of the 21 patients (91%) with GI amyloidosis who underwent renal biopsies also had renal amyloid deposits. Eleven of the 21 (52%) had amyloidosis on abdominal fat biopsy. None of the 12 patients without GI amyloidosis had renal amyloidosis on renal biopsy, and none of the 50 patients without GI amyloidosis had amyloidosis on abdominal fat biopsy. Gastroduodenal biopsy reveals a high prevalence of amyloidosis in RA patients. Amyloidosis is often associated with signs of renal impairment. Results of GI biopsy are highly correlated with those of renal biopsy, but the results of fat biopsy are not. We recommend GI biopsy for RA patients for the screening of systemic amyloidosis.

Abdominal Wall↗
PubMed2006

Lysozyme amyloidosis: report of 4 cases and a review of the literature.

Autosomal dominant hereditary amyloidosis represents not 1 disease but a group of diseases, each the result of mutations in a specific protein. The most common form is transthyretin amyloidosis, which has been recognized clinically for over 50 years as a familial polyneuropathy. Nonneuropathic amyloidoses (Ostertag type amyloidosis) include those due to abnormalities in lysozyme, fibrinogen Aalpha-chain, and apolipoprotein A-I and A-II. The role of lysozyme in amyloid-related human disorders was first described in 1993; to date, there have been only 9 publications describing this disorder, which is a nonneuropathic form of hereditary amyloidosis. Reported cases have involved 7 unrelated families. We describe here our own experience with 4 families suffering from lysozyme amyloidosis: the first had prominent renal manifestations with sicca syndrome, the second and third had prominent gastrointestinal symptoms, and the fourth had a dramatic bleeding event due to rupture of abdominal lymph nodes. To our knowledge, this last symptom has not been reported previously, but is reminiscent of the hepatic hemorrhage seen in a previously reported case of a patient with lysozyme amyloidosis. To characterize the manifestations of this disorder, we performed an exhaustive literature review.Although hereditary amyloidosis is thought to be a rare disease, it is probably not as rare as we think and may well be underdiagnosed. Moreover, some cases of lysozyme amyloidosis are probably confused with acquired monoclonal immunoglobulin light-chain (AL) amyloidosis, formerly known as primary amyloidosis, which is the most frequent type of amyloidosis. Because treatment for each type of amyloidosis is different, and because therapy directed at 1 type may worsen symptoms of the other types, it is important to determine precisely the nature of the amyloid protein. Thus, hereditary lysozyme amyloidosis should be considered in all patients with systemic amyloidosis, particularly in patients who present with renal, gastrointestinal, or bleeding complications without evidence of AL or AA (secondary) amyloidoses.

Adult↗
PubMed2006

Unique type of isolated cardiac valvular amyloidosis.

BACKGROUND: Amyloid deposition in heart is a common occurrence in systemic amyloidosis. But localised valvular amyloid deposits are very uncommon. It was only in 1922 that the cases of valvular amyloidosis were reported. Then in 1980, Goffin et al reported another type of valvular amyloidosis, which he called the dystrophic valvular amyloidosis. We report a case of aortic valve amyloidosis which is different from the yet described valvular amyloidosis. CASE PRESENTATION: A 72 years old gentleman underwent urgent aortic valve replacement. Intraoperatively, a lesion was found attached to the inferior surface of his bicuspid aortic valve.Histopathology examination of the valve revealed that the lesion contained amyloid deposits, identified as AL amyloidosis. The serum amyloid A protein (SAP) scan was normal and showed no evidence of systemic amyloidosis. The ECG and echocardiogram were not consistent with cardiac amyloidosis. CONCLUSION: Two major types of cardiac amyloidosis have been described in literature: primary-myelomatous type (occurs with systemic amyolidosis), and senile type(s). Recently, a localised cardiac dystrophic valvular amyloidosis has been described. In all previously reported cases, there was a strong association of localised valvular amyloidosis with calcific deposits.Ours is a unique case which differs from the previously reported cases of localised valvular amyloidosis. In this case, the lesion was not associated with any scar tissue. Also there was no calcific deposit found. This may well be a yet unknown type of isolated valvular amyloidosis.

Aged↗
PubMedDate not supplied

[Senile amyloidosis: from the Schwartz tetrad to the present].

Senile amyloidosis can be systemic (generalized) or local, this being determined by the protein precursor of the amyloid fibrils. Systemic cardiovascular amyloidosis should be distinguished from AL-amyloidosis. Senile amyloidosis is represented by both endocrine and nonendocrine forms. Endocrine forms include isolated auricular amyloidosis and amyloidosis of the Langerhans islands, while non-endocrine forms include aortic amyloidosis, cerebral amyloidosis, eye amyloidosis and amyloidosis of the prostate and/or seminal vesicles. Most frequent are combinations of the endocrine with aortic amyloidosis or Langerhand island amyloidosis with cerebral amyloidosis and eye amyloidosis. These data reject the Schwarts tetrad as necessary manifestation of senility.

Aged↗
PubMedDate not supplied

Nasopharyngeal amyloidosis.

PURPOSE: To discuss the presentation of localized amyloidosis affecting the nasopharynx and discuss the management options. Amyloidosis in the head and neck is a rare and benign condition that usually takes the form of localized amyloidosis. Because systemic amyloidosis markedly shortens life expectancy owing to its involvement with vital organs, rectal biopsy or fat aspiration of the anterior abdominal wall must be carried out to exclude systemic involvement. Localized amyloidosis in the head and neck can involve the orbit, sinuses, nasopharynx, oral cavity, salivary glands, and larynx. METHODS: We present the case of a patient with conductive hearing loss and serous otitis media with effusion secondary to nasopharyngeal amyloidosis, as well as present a review of the literature. RESULTS: Only a few cases of nasopharyngeal amyloidosis have thus far been reported. Patients with this disease can also present with recurrent epistaxis, postnasal drip, nasal obstruction, and eustachian tube dysfunction. Localized amyloidosis of the nasopharynx, which is slow growing, has proved difficult to treat because it can persist or recur despite surgical treatment. Furthermore, bleeding may be a major complication in treating patients with nasopharyngeal amyloidosis by transpalatal excision because the amyloid deposits cause vascular wall fragility. Finally, there is no evidence that surgical treatment of nasopharyngeal amyloidosis can prolong survival or that localized amyloidosis can progress to systemic amyloidosis. For these reasons, we elected to treat our patient with a tympanostomy tube and observation. CONCLUSION: In the absence of systemic disease, localized amyloidosis of the nasopharynx may be treated conservatively.

Aged↗
PubMed2005

Significance of SAA1.3 allele genotype in Japanese patients with amyloidosis secondary to rheumatoid arthritis.

OBJECTIVE: To clarify the clinical significance of the SAA1.3 allele in the development and outcome of AA amyloidosis in Japanese patients with rheumatoid arthritis (RA). METHODS: One hundred and twenty RA patients (60 alive and 60 dead) fulfilling the 1987 ACR criteria and 62 RA patients with biopsy-confirmed amyloid A (AA) amyloidosis (36 alive and 26 dead) were enrolled. The SAA1 genotypes were determined by PCR-based restriction fragment length polymorphism. To predict the clinical outcome of AA amyloidosis, we investigated characteristics and survival, focusing on the SAA1.3 allele retrospectively. RESULTS: The SAA1.3 allele genotype was not only a risk factor for the association of AA amyloidosis but also a poor prognostic factor for the development of AA amyloidosis (P=0.015). Both the association of AA amyloidosis arising early in the RA disease course and symptomatic variety and severity were found in amyloidotic patients with the SAA1.3 allele. The presenting factors adversely influenced were age (P=0.001), lowered serum albumin (P=0.001) and creatinine concentration (P=2.14 x 10(-5)). Renal involvement was associated with poor survival in patients with AA amyloidosis (P=0.011) and the presence of cardiac involvement was likely to be a risk factor for survival (P=0.062). The rate of the causes of death in respect to the category of infection, gastrointestinal diseases, and renal failure was higher in patients with AA amyloidosis than in those without amyloidosis, gastrointestinal diseases and renal failure. Cyclophosphamide was found to be superior to methotrexate in the management of RA patients with AA amyloidosis. CONCLUSION: Our data support the fact that homozygosity for the SAA1.3 allele is a univariate predictor of survival in addition to a risk factor for the association of AA amyloidosis adversely influencing the outcome in Japanese RA patients. Renal involvement is a pivotal clinical manifestation in the development of AA amyloidosis, as is likely to be cardiac involvement in AA amyloidosis secondary to RA.

Amyloidosis↗
PubMed1997

Thoracic cross-sectional imaging of amyloidosis.

OBJECTIVE: Our objective was to determine the thoracic manifestations on cross-sectional imaging of patients with tissue-proven amyloidosis. MATERIALS AND METHODS: We reviewed the records of 300 patients with the diagnosis of amyloidosis on whom cross-sectional imaging was done at our institution between 1985 and 1995. After exclusions, 19 patients with tissue-proven amyloidosis and cervicothoracic cross-sectional imaging were included. Seven patients had localized amyloidosis and 12 patients had systemic amyloidosis. Eighteen patients underwent CT scans and the remaining patient, MR imaging. RESULTS: Two patients with systemic amyloidosis had widespread noncalcified adenopathy. A third patient had an infiltrative soft-tissue process in the mediastinum and axillae containing thick linear and focal calcifications. Five patients with localized amyloidosis had pulmonary nodules: Three patients had solitary nodules, one patient had two nodules, and one patient had 10 nodules. Nodules ranged in size from 8 mm to 3 cm. Eight patients with systemic amyloidosis had diffuse lung disease. One patient with systemic amyloidosis had recurrent right pleural effusions. Two patients with localized amyloidosis had laryngotracheobronchial amyloidosis. One of the two patients had focal thickening of the right aryepiglottic fold. The other patient had diffuse concentric soft-tissue thickening within the trachea. CONCLUSIONS: Localized amyloidosis can occur in patients as pulmonary nodules or as laryngotracheobronchia involvement. Nodules are typically solitary (60%) with a smooth or lobular contour and are frequently in a subpleural or peripheral location. Calcification is not common (20%). Systemic amyloidosis can occur in patients as a combination of adenopathy (75%), multiple pulmonary nodules (50%), and diffuse irregular lines or interlobular septal thickening (50%).

Aged↗
PubMed2005

Respiratory manifestations in amyloidosis.

BACKGROUND: Amyloidosis is a collection of diseases in which different proteins are deposited. Amyloid deposits occur in systemic and organ-limited forms. In both systemic and localized forms of the disease, lung can be involved. The aim of this study was to explore the different respiratory manifestations of amyloidosis. METHODS: Chest radiology, clinical presentations, bronchoscopic/laryngoscopic findings and lung function data of 59 patients with amyloidosis involving respiratory tract collected during January 1986 to March 2005, were analysed. RESULTS: Of the 16 cases with localized respiratory tract amyloidosis, 8 had the lesions in the trachea and the bronchi, 2 in the larynx and the trachea, 5 in the larynx and/or the pharynx, and 1 in the lung parenchyma. Of 43 systemic amyloidosis with respiratory tract involvement, 3 had the lesions in bronchi, 13 in lung parenchyma, 33 in pleura, 8 in mediastina, 1 in nose and 1 in pharynx. Chest X-rays were normal in most cases of tracheobronchial amyloidosis. CT, unlike chest X-rays, showed irregular luminal narrowing, airway wall thickening with calcifications and soft tissue shadows in airway lumen. Localized lung parenchymal amyloidosis presented as multiple nodules. Multiple nodular opacities, patch shadows and reticular opacities were the main radiological findings in systemic amyloidosis with lung parenchymal involvement. In pleural amyloidosis, pleural effusions and pleural thickening were detected. Mediastinal and/or hilar adenopathy were also a form of lung involvement in systemic amyloidosis. The major bronchoscopic findings of tracheobronchial amyloidosis were narrowing of airway lumen, while nodular, 'tumour like' or 'bubble like' masses, with missing or vague cartilaginous rings, were detected in about half of the patients. CONCLUSIONS: Localized respiratory tract amyloidosis mostly affects the trachea and the bronchi. Chest X-rays are not sensitive to detect these lesions. Systemic amyloidosis often involves lung parenchyma and the pleura. Open lung biopsy or pleural biopsy should be performed for the diagnosis.

Adolescent↗
PubMed1996

[Clinical characteristics and genetic background of secondary amyloidosis associated with rheumatoid arthritis in Japanese].

In order to examine the clinical characteristics and genetic background of secondary amyloidosis associated with rheumatoid arthritis, we analyzed clinical features and HLA typing of 85 patients in a multicenter study. Eighty-five patients with secondary amyloidosis associated RA were studied. The diagnosis of secondary amyloidosis were made on histological findings by biopsy or autopsy. The most common biopsy site was gastrointestinal tract (79.5%). Clinical symptom and the frequency at the time of diagnosis were; diarrhea (35 cases), abdominal pain (22 cases) and vomiting and nausea (16 cases). Abnormalities and the frequency in a laboratory test included proteinuria (49 cases), increased serum creatinine (32 cases), anemia (30 cases) and hematuria (15 cases). Twenty-eight patients were dead and 57 patients were alive at the time of the study. The average duration between diagnosis of amyloidosis and death was 19.4 +/- 18.5 (SD) months among the dead patients. The average duration after diagnosis of amyloidosis was 24.2 +/- 19.5 (SD) months in surviving patients. The causes of death were renal failure complicated with heart failure (6 patients), heart failure alone (3 patients) and renal failure alone (2 patients). Fifty-nine patients in the control group who were negative to amyloid deposition on biopsies at more than one site in the gastrointestinal tract, were clinically compared with patients in the amyloidosis group. No difference were noted in the age of RA occurrence and the stage between the two groups. As to the class, however, the number of patients with severe functional disorder (class 3 or severe) was larger in the amyloidosis group. There were no significant difference between the two groups in Lansbury's activity index. On hematology, biochemistry and urinalysis, the incidences of increased white blood cell count, anemia, increased platelet count, increased serum creatinine, hypoproteinemia, hypoalbuminemia, increased IgA, and increased urine and blood BMG were statistically significantly higher in the amyloidosis group than in the control group. HLA-A, -B, -C, and DR-locus antigens were compared in the 53 patients in the amyloidosis group and in the 59 subjects in the control group. There were no significant differences in frequency of HLA-A, and -B antigens between two groups. Frequency of CW7 antigen was significantly decreased in the amyloidosis group (13.2%) than in the control group (39.0%). Frequency of DR1 antigen was decreased in the amyloidosis group (3.8%) than in the control group (22.0%), although the difference was not significant. These findings suggest the possible involvement of genetic factors in the occurrence of amyloidosis. It is suggested that the occurrence of amyloidosis is suppressed by some genes which are linked with CW7 antigen.

Adolescent↗
PubMed2006

Current treatment in cardiac amyloidosis.

Involvement of the heart is a common finding in amyloidosis. The heart is usually infiltrated by amyloid fibrils in primary amyloidosis and age-related forms of amyloidosis, less commonly in transthyretin familial amyloidosis, and rarely in secondary amyloidosis. The most common clinical presentation is restrictive cardiomyopathy with right-sided heart failure. The second most frequent presentation is congestive heart failure due to systolic dysfunction, followed by arrhythmias and orthostatic hypotension. The diagnosis of amyloidosis requires tissue sample confirmation; at present, Congo red staining in polarized light is the diagnostic method of choice. The characterization of protein fibril type by immunohistochemistry or biochemistry is essential for patient prognosis and treatment. The therapeutic approach consists of specific treatment of amyloidosis and supportive treatment for cardiac-related symptoms. The treatment depends on the type of amyloidosis and the stage of disease. The mainstay of supportive treatment of cardiac failure is diuretic therapy. Primary amyloidosis treatment protocol includes melphalan and prednisone chemotherapy. Heart transplantation is only a palliative treatment. Stem cell transplantation is an emerging treatment alternative. Combination therapy of melphalan and stem cell transplantation has been shown to be a promising treatment strategy. Secondary amyloidosis requires aggressive treatment of the associated inflammatory and neoplastic process. Age-related (senile) amyloidosis benefits from supportive cardiac treatment when applicable. Transthyretin amyloidosis, the most common cardiac hereditary amyloidosis, is treated by liver or combined liver-heart transplantation. New therapies based on chemical and immunologic reaction with amyloid or its precursor are under intensive development.

Journal Article↗
PubMed1996

Prospective and serial study of primary amyloidosis with serum amyloid P component scintigraphy: from diagnosis to prognosis.

OBJECTIVE: The purpose of this study was to assess the value of the serum amyloid P (SAP) component scintigraphy in patients with primary amyloidosis (AL). MATERIAL AND METHODS: Pure human SAP labeled with iodine-123 (123I-SAP) was given intravenously to 24 patients with biopsy-proven systemic amyloidosis (15 without multiple myeloma = group 1, and 9 with multiple myeloma = group 2) and to 6 patients with multiple myeloma without any clinical or biological signs of amyloidosis (group 3). Whole-body images as well as regional views and tissue retention levels were obtained after 24 hours. Our study was approved by the institutional review committee and all individuals gave informed consent and were prospectively studied (median 13 months, range 1 to 47 from the date of the scintigraphy to May 1995). RESULTS: Organ localization of 123I-SAP, indicating the presence of substantial visceral amyloid deposits, was observed in all patients in group 1 and 2. The organ uptake of 123I-SAP included the spleen (1 patient was splenectomized) in 20 of 23 cases (87%), the liver in 15 of 24 (60%), and the kidneys in 6 of 24 (25%). Myocardial 123I-SAP was never seen although 13 out of the 24 patients had clinical or echographic data for amyloidosis. Twenty-four hour tissue retention was significantly elevated in all patients (group 1 and group 2): 55.66% +/- 19.16% in group 1 and 34.37% +/- 24.92% in group 2, as compared with normal levels < 24%. The sensitivity of the technique was 79% when only organ uptake was considered but reached 100% when tissue retention was also considered. The 24-hour tissue retention might be correlated with the severity of the amyloidosis: mean survival in patients with tissue retention greater than 50% was 11.3 months versus 24.5 months in patients with levels less or equal to 50%. Five of the 6 patients with multiple myeloma without evidence of amyloidosis had abnormal 123I-SAP imaging and 24-hour tissue retention levels. In 2 of them, amyloidosis was secondly detected. In the 9 patients who had two scintigraphies, variations in 24-hour tissue retention values were in accordance with the clinical evaluation. CONCLUSIONS: Spleen and liver distribution of amyloidosis is mostly revealed by 123I-SAP scintigraphy in patients with AL amyloidosis. The uptake of 123I-SAP appeared in proportion to the quantity of amyloidosis present in different tissues, and the relative quantity of amyloid deposits in the myocardium, carpal tunnel, digestive tract, and kidneys was often small and seldom visualized by 123I-SAP scintigraphy. In contrast 24-hour tissue retention levels were abnormal in all cases of known AL amyloidosis. This may be a positive argument for the diagnosis of amyloidosis when histopathological tests are normal. Tissue retention levels appear important as they may be correlated with survival.

Aged↗
PubMed2001

Useful polyclonal antibodies against synthetic peptides corresponding to immunoglobulin light chain constant region for immunohistochemical detection of immunoglobulin light chain amyloidosis.

For the immunohistochemical detection of immunoglobulin (Ig) light chain amyloidosis on formalin-fixed, paraffin-embedded tissue sections, we prepared polyclonal antibodies against synthetic peptides corresponding to positions 118-134 of Ig lambda light chain and positions 116-133 of Ig kappa light chain. Nineteen cases of systemic Ig lambda light chain amyloidosis (Alambda amyloidosis), 10 cases of systemic Ig kappa light chain amyloidosis (Akappa amyloidosis), one case of immunohistochemically unclassified systemic amyloidosis and five cases of localized Alambda amyloidosis were tested with these antibodies. Anti-lambda (118-134) antiserum and the affinity-purified antibody both reacted with 18 of the 19 cases of systemic Alambda amyloidosis and all cases of localized Alambda amyloidosis, although the immunoexpression was somewhat variable in intensity in different areas within the same specimen in both systemic and localized amyloidosis. The signal intensities in plasma cells and serum reacted for anti-lambda (118-134) antiserum were weaker than signals obtained with commercially available anti-Ig lambda light chain antibodies. Anti-kappa (116-133) antiserum and the affinity-purified antibody reacted with nine of the 10 cases of systemic Akappa amyloidosis. We conclude that these antibodies against synthetic peptides corresponding to the Ig light chain constant region are useful for the classification of amyloidosis on formalin-fixed, paraffin-embedded tissue sections.

Amyloidosis↗
PubMed2004

Apolipoprotein and anticardiolipin antibodies in patients with renal amyloidosis.

BACKGROUND: Thromboembolic events are seen more frequently in patients with chronic renal failure (CRF) and amyloidosis. The anticardiolipin antibody (ACA) that is important for thromboembolic events has never been studied. METHODS: This study included 43 amyloidosis patients of different aetiologies; 28 with CRF as well as 20 patients who had CRF without amyloidosis. Thirty normal subjects were included as a control group. We determined the serum levels of ACA, apolipoprotein AI (ApoAl), ApoE and lipoprotein (a) (Lp(a)) in these groups. RESULTS: Anticardiolipin antibody was found to be positive in 30.2% of patients with amyloidosis, this is in contrast to 3.3% in the control group (chi = 8.25, P < 0.005). We also showed that there was a statistically significant difference (chi = 5.03, P < 0.05) between the CRF patients with amyloidosis (31%) and the CRF patients without amyloidosis (5%). The average levels of serum ApoAI were shown to be significantly lower (P < 0.05) in CRF patients with amyloidosis in comparison with the amyloidosis patients who had normal renal functions (93.60 +/- 27.84 vs 119.8 +/- 36.26 mg/dL, P < 0.05). There was also significant a difference in ApoAI levels between CRF patients with and without amyloidosis (P < 0.001). The serum Lp (a) levels were significantly higher in CRF patients with amyloidosis when compared with the controls (41.2 +/- 22.39 vs 19.13 +/- 8.78 mg/dL, P < 0.001). The serum Lp (a) levels were also positively correlated with ACA (r = 0.211; P < 0.05). CONCLUSION: In conclusion, ACA positivity is more common in all patients with amyloidosis as compared with CRF patients and normal controls. This study is the first to show the presence of high levels of ACA in patients with CRF, which is caused by secondary amyloidosis. Further studies are recommended to investigate the mechanism of this finding.

Adult↗
PubMed1988

Senile cardiac amyloidosis in senescence accelerated mouse (SAM).

The characteristics of the senescence accelerated mouse (SAM), a new murine model for accelerated senescence, are early senescence and a high incidence of senile amyloidosis. This study was performed to clarify histopathologically the details of senile cardiac amyloidosis in SAM, and the incidence of amyloidosis in the heart of SAM (-P) was 46.0% (1+: 22.0; 2+: 16.0; 3+: 8.0%). Amyloid infiltrated the ventricular walls, interventricular septum, atrial walls and interatrial septum. Amyloid deposition was prominent around the myocardial fibers and in the vascular walls. Amyloid involvement was greater in the veins than in the arteries. Senile cardiac amyloidosis of SAM was mild or moderate and not severe, in general. The age dependency of amyloidosis incidence of the heart was confirmed. The heart/body weight ratio tended to parallel the grade of cardiac amyloidosis. SAM often had complications such as abscess, lymphoma, skin ulcer, etc. The incidence of amyloidosis was higher in SAM with these complications than in SAM without them. The complications seemed to promote the progress of cardiac amyloidosis and to superimpose secondary amyloidosis. In SAM senile cardiac amyloidosis is less frequent than renal amyloidosis (64.4%) or hepatic amyloidosis (63.3%).

Abscess↗
PubMed1996

Pulmonary amyloidosis. The Mayo Clinic experience from 1980 to 1993.

OBJECTIVE: To define the prognosis for and radiographic presentation of patients with pulmonary amyloidosis. DESIGN: Retrospective review of the Mayo Clinic experience with biopsy-proven pulmonary amyloidosis from 1980 to 1993. SETTING: Tertiary care center. PATIENTS: Patients with pulmonary biopsy specimens showing amyloid deposition. MEASUREMENTS: Medical records were reviewed, and pertinent information was recorded, including demographic data, type of pulmonary biopsy, results of biopsies of nonpulmonary sites and of immunoelectrophoresis, and other clinical, radiographic, and laboratory information necessary for distinguishing localized pulmonary amyloidosis, primary systemic amyloidosis, secondary amyloidosis, and familial amyloidosis. RESULTS: 35 of 55 patients with pulmonary amyloidosis had primary systemic amyloidosis that presented radiographically as an interstitial or reticulonodular pattern with or without pleural effusion. The median survival after diagnosis was 16 months. Nodular pulmonary "amyloidomas" (nodular amyloid lesions) were not associated with systemic disease and were associated with a benign prognosis. Three of 4 patients with localized tracheobronchial amyloidosis required Nd:YAG (neodymium:yttrium-aluminum-garnet) laser therapy for obstructive symptoms. "Senile" amyloid deposition was an incidental finding in some patients at autopsy. CONCLUSIONS: Localized amyloidomas are characterized by a benign course and are not associated with systemic amyloidosis. Despite its localized nature, tracheobronchial amyloid deposition may be asymptomatic or may result in significant morbidity due to obstructive phenomena. Pulmonary amyloidosis associated with primary systemic amyloidosis generally presents as a diffuse interstitial pattern with or without pleural effusion. Complete survival data indicate that long-term outcome is poor after diagnosis. We describe the largest series of patients diagnosed by bronchoscopic lung biopsy. Despite reports to the contrary, we have found bronchoscopic lung biopsy to be a safe and effective diagnostic technique.

Adult↗
PubMed2006

Diagnostic accuracy of subcutaneous abdominal fat tissue aspiration for detecting systemic amyloidosis and its utility in clinical practice.

OBJECTIVE: Aspiration of subcutaneous abdominal fat is a simple and fast method for detecting systemic amyloidosis; however, the sensitivity of this approach remains undetermined. The aim of this study was to assess the accuracy of fat tissue aspiration for detecting systemic amyloidosis and the utility of this method in clinical practice. METHODS: All consecutive patients with established and suspected systemic amyloidosis who attended our tertiary referral hospital between 1994 and 2004 underwent aspiration of subcutaneous abdominal fat. Congo red-stained tissue was assessed quickly in a single smear in a routine manner by a single observer, and was also assessed thoroughly in 3 smears by 2 independent observers. RESULTS: One hundred twenty patients with established systemic amyloidosis were studied (38 with AA amyloidosis, 70 with AL amyloidosis, and 12 with ATTR amyloidosis). Routine (quick) assessment was associated with a sensitivity of 80% (95% confidence interval [95% CI] 72-87%). Sensitivity increased to 93% (95% CI 87-97%) when 3 smears were thoroughly examined. The specificity of fat aspiration in 45 control subjects was 100% (95% CI 92-100%). One hundred sixty-two patients for whom there was a clinical suspicion of systemic amyloidosis were screened for amyloidosis by fat tissue aspiration and biopsy of at least 1 other tissue. In 69 (43%) of these 162 patients, a diagnosis of amyloidosis was established, and in 66 (96%) of these patients, the results of fat tissue aspiration were positive. The clinical utility of fat tissue aspiration was greater than that of biopsy of the rectum. CONCLUSION: Subcutaneous abdominal fat aspiration is the preferred method for detecting systemic amyloidosis, with sensitivity of 80% associated with use of a routine approach. The use of a thorough assessment (3 fat smears, 2 observers) increased sensitivity to >90%. If the results of fat tissue aspiration are negative, the additional value of a subsequent biopsy of the rectum is negligible.

Adolescent↗
PubMed2006

SAA1 alpha/alpha alleles in Behçet's disease related amyloidosis.

Behçet's disease (BD) related amyloidosis is relatively rare. Serum amyloid A protein (SAA) protein gene polymorphism is one of the factors implicated in the pathogenesis of AA type amyloidosis. The aim of this study is to investigate SAA1 gene polymorphism in different patient groups: (1) BD related amyloidosis, (2) BD without amyloidosis, and (3) healthy controls. One hundred eleven patients from three main groups were included in the study: (1) BD related amyloidosis (n = 9), (2) BD without amyloidosis (n = 39), and (3) healthy controls (n = 63). Homozygous alpha/alpha is present in 78% of patients with BD and amyloidosis. The SAA1 alpha/alpha genotype is significantly more common among patients with BD and amyloidosis. This study demonstrated increased frequency of alpha/alpha genotype in BD related amyloidosis. To our knowledge, the relationship between alpha/alpha genotype and BD related amyloidosis was not studied previously. In conclusion, the SAA1 alpha/alpha genotype is a risk factor for amyloidosis in BD.

Adult↗
PubMed2004

[AA Amyloidosis: recent knowledges on pathophysiology].

PURPOSE: Amyloidosis is a rare disease associated with an underestimated frequency because of the need of a pathological diagnosis identifying extracellular deposits with affinity for Congo red. There are moreover 20 proteins that can form extracellular fibril deposits. Some amyloidosis forms are more common than others, especially AA amyloidosis and AL amyloidosis. Among genetic amyloidosis, the transthyretin related amyloidosis is the most prevalent. The amyloid frequency could also be increased if amyloidosis related to Alzheimer's disease or prion's disease is included. In the absence of specific treatment for amyloidosis, researches are focused on amyloidosis pathophysiology especially, on AA amyloid pathophysiology. CURRENT KNOWLEDGE AND KEY POINTS: Amyloid is not only composed of fibrils but also of proteoglycanes, P component and amyloid-enhancing factor. A new research aim is focused on the cells involved in amyloid formation and on the relationship between amyloid, proteoglycanes and P component. FUTURE PROSPECTS AND PROJECTS: It was demonstrated that, in the absence of macrophages, an extracellular amyloid formation was possible with amyloid-enhancing factor as starting point. Some inhibitors of intra or extracellular amyloid formation are still to be discovered. Anti-P component has been recently developed; it was successful in the treatment of murin AA amyloidosis and gave some hope concerning the treatment of human amyloidosis.

Amyloidosis↗