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 37 records · Page 2Linked to original sources
PubMed1975

Amyloidosis associated with dermatomyositis and features of multiple myeloma. The progression of amyloidosis associated with corticosteroid and cytotoxic drug therapy.

Described here is a 59 year old man with dermatomyositis and hypogammaglobulinemia. His muscle power improved after corticosteroid therapy, but extensive amyloidosis and repeated infections appeared. Bone marrow morphology suggested multiple myeloma, but treatment with cytotoxic drugs had no beneficial effect on the amyloidosis. Because of rapid progression of the amyloidosis and further infections, cytotoxic drug therapy was stopped, corticosteroid dosage was decreased, and supplementary immunoglobulin therapy was instituted. The infections occurred less frequently and the amyloidosis appeared to regress. This case suggests that immunosuppressive therapy may exacerbate amyloidosis. The literature is reviewed, and the possible role of humoral immunodeficiency in the pathogenesis of amyloidosis is discussed. It is suggested that supplementary immunoglobulin may be beneficial in amyloidosis.

Agammaglobulinemia↗
PubMed1987

Vagus nerve and celiac ganglion lesions in generalized amyloidosis. A correlative study of familial amyloid polyneuropathy and AL-amyloidosis.

To clarify the cause of gastrointestinal disorders in systemic amyloidosis we made pathologic and morphometric studies of vagus nerves, celiac ganglia, stomach and rectum in three autopsied cases with type 1 familial amyloid polyneuropathy (FAP) and two with nonhereditary generalized amyloidosis (AL-amyloidosis). The gastric and rectal walls in all cases were affected in the same way by amyloid deposition. On the other hand, there was a great difference between the two diseases in the severity of vagus nerve and celiac ganglion lesions: the vagus nerves in FAP showed very extensive endoneurial deposition of amyloid with severe loss of myelinated nerve fibers, but in AL-amyloidosis there was no loss of myelinated nerve fibers and only slight amyloid deposition in the endoneurium. Similarly, in the celiac ganglion, intraganglionic deposition of amyloid was prominent in FAP and slight in AL-amyloidosis. It is known that bowel symptoms frequently occur in type I FAP and are less prominent in AL-amyloidosis. This study demonstrated that the gastrointestinal autonomic nerves were more markedly disturbed by amyloid in the former than in the latter, and disorder in neural control of the digestive tract may be responsible for the bowel symptoms in systemic amyloidosis, especially in type I FAP.

Aged↗
PubMed2005

Autologous transplantation for primary systemic AL amyloidosis is feasible outside a major amyloidosis referral centre: the Calgary BMT Program experience.

Recent reports from large amyloidosis referral centers suggest that primary systemic AL amyloidosis patients treated with high-dose melphalan (HDM) and autologous stem cell transplantation (ASCT) survive longer than historical controls treated with less intensive chemotherapy, despite high transplant-related mortality (TRM) rates of >10%. A retrospective review was conducted to determine if the outcome of ASCT for AL amyloidosis at our institution was similar to that reported at major amyloidosis referral centers. Over a 7 year period, we treated a total of 15 AL amyloidosis patients with ASCT, including four with poor prognosis cardiac or multisystem involvement. No TRM was observed. Overall, 10 patients (67%) achieved a complete hematological response and four patients (27%) achieved a complete organ response. The 4-year event-free and overall survival rates were 60% (95% CI 32-89%) and 75% (95% CI 50-100%), respectively. One patient, who presented with cardiac failure and multiorgan involvement with colonic bleeding currently remains in complete remission 62 months post-ASCT. In conclusion, ASCT for primary AL amyloidosis can safely be performed at experienced transplant centers that are not associated with major amyloidosis referral centers, and is feasible for patients who have multisystem involvement, particularly for motivated patients with good performance status.

Adult↗
PubMed1994

Lymphatic amyloidosis, a previously unrecognized form of amyloid deposition in generalized amyloidosis.

Although amyloid deposition in relation to blood vessels is a well-recognized feature of generalized amyloidosis, lymphatic vessel amyloidosis is not mentioned in the literature. Systematic investigation of tissue removed at autopsy from patients with generalized amyloidosis and biopsy specimens from cases of localized amyloidosis and familial Mediterranean fever showed that amyloid deposition around lymphatics is by no means uncommon. The material investigated was mainly large and small bowel, lung, heart and kidney. Amyloid was identified by green birefringence with the Congo red stain on cross-polarization and lymphatics by their lack of immunostaining for CD34. Involvement of lymphatics was noted in 20 of the 42 organs from which specimens were examined, and was always accompanied by involvement of blood vessels and/or the interstitium. In the intestine, lymphatic amyloidosis was found mainly in the submucosa and subserosa, and was also demonstrated by electronmicroscopy in one case. Although lymphatic amyloidosis was equally common in the heart, lung and kidney, it was usually less prominent here than in the intestine. No lymphatic involvement was seen in localized amyloidosis. As the lymphatics play a central role in the resorption of interstitial proteins, they are probably also involved in the resorption of amyloid proteins. Amyloid deposition in the vicinity of lymphatics is probably the result of decompensation of this process.

Amyloidosis↗
PubMed1997

Histomorphological patterns of renal amyloidosis: a correlation between histology and chemical type of amyloidosis.

A retrospective study was conducted to investigate whether there was a correlation between the histological pattern of renal amyloidosis, the chemical type of amyloid protein involved and the clinical presentation. Eighteen consecutive cases of systemic amyloidosis that had renal biopsies processed and examined histopathologically at the Department of Pathology, Faculty of Medicine, University of Malaya, Kuala Lumpur were reviewed. The age range of patients was 25 to 64 yrs (mean, 46 yrs). The male:female ratio was 2.6:1. Three patients were Malay, 9 Chinese, 3 Indian, 1 Indonesian, 1 Iban, and 1 Bisaya. According to the predominant site of amyloid deposition, 14 cases showed a glomerular pattern and 4 a vascular pattern. 8 cases were designated as 2 anti-human amyloid-A (AA) amyloidosis on the basis of permanganate-sensitivity and immunoreactivity of deposits with anti-human AA protein antibody. Ten cases contained deposits that were permanganate-resistant and nonimmunoreactive for AA protein and were designated as AL in type. The histomorphologic pattern of renal amyloidosis did not provide a reliable means of differentiating AA from AL amyloidosis. The glomerular pattern tended to present with renal manifestations such as nephrotic syndrome and chronic renal failure, whereas the vascular pattern tended to present with nonrenal manifestations such as diarrhoea. These findings may have a bearing on the pathophysiology of amyloidosis and provide clues to appropriate management.

Adult↗
PubMed1992

Amyloid cardiomyopathy in systemic non-hereditary amyloidosis. Clinical, echocardiographic and electrocardiographic findings in 30 patients with AA and 24 patients with AL amyloidosis.

To underline the role of echocardiography in the detection of cardiac involvement in patients with amyloidosis, physical examination, echocardiography and electrocardiography were performed in 30 patients with AA amyloidosis (amyloid protein A, associated with chronic inflammatory disease, usually without cardiomyopathy) and 24 patients with AL amyloidosis (the immunoglobulin light chain derived type, often associated with cardiomyopathy). All patients had histological confirmation of amyloidosis by rectal or subcutaneous abdominal fat biopsy. The combination of increased thickness of the left ventricular posterior wall and interventricular septum with a low voltage electrocardiographic pattern is highly specific for cardiac amyloidosis and was found in 3/30 (10%) of the AA patients and in 13/24 (54%) of the AL patients. The echocardiographic abnormalities were strongly related to the degree of clinical heart disease, showing mildly or moderately increased wall thickness in the early asymptomatic phase or severe thickening and hypokinesia of the left ventricular posterior wall and interventricular septum in clinically apparent cardiac dysfunction. Echocardiography appears to be a sensitive test for the detection of cardiac involvement in amyloidosis, in symptomatic as well as asymptomatic patients.

Adult↗
PubMed1992

Pulmonary vascular amyloidosis in aged dogs. A new form of spontaneously occurring amyloidosis derived from apolipoprotein AI.

The N-terminus of a mutant form of apolipoprotein AI [apoAI] has previously been shown to be the subunit protein of amyloid fibrils in a human kindred with a form of familial amyloid polyneuropathy (FAP, type III) and in a recently reported kindred with a form of non-neuropathic hereditary amyloidosis. In this study, we demonstrate by amino-acid sequence analysis, that a form of vascular amyloidosis occurring in the lungs of aged dogs is derived from a N-terminal fragment of apoAI and that no amino acid substitution is present in this confirmed sequence. This represents the first documentation of apoAI as a precursor for a form of amyloidosis in animals, and provides the first documentation of apoAI as a precursor for amyloid fibrils in a form of age-associated ("senile") amyloidosis. Secondary structure prediction analysis of the N-terminal regions of normal human and dog apoAI indicated a propensity for beta-pleated sheet conformation, and thus amyloidogenesis, in 40 and 45% of the respective sequences. These results suggest that apoAI (like transthyretin) may serve as an amyloid precursor protein for both familial and senile forms of amyloidosis. ApoAI should, therefore, be considered as a potential amyloid precursor when forms of human senile amyloidosis of unknown origin are evaluated.

Aging↗
PubMed1992

[Inflammatory cell infiltration around beta 2-microglobulin amyloid deposition: histologic comparison of beta 2-microglobulin amyloidosis with AA or AL amyloidosis].

Thirty-one autopsy cases of beta 2-microglobulin (beta 2M) amyloidosis were pathologically investigated in comparison with 17 autopsy cases of AA or AL amyloidosis. In 20 cases (65%, 20/31) of beta 2M amyloidosis, inflammatory cells, mainly macrophages were seen infiltrating around beta 2M amyloid in intervertebral disks. The more beta 2M amyloidosis advances, the more macrophage infiltration tends to be prominent. In cases of severe beta 2M amyloidosis, the cytoplasm of macrophages around amyloid deposition were swollen with engulfed amyloid substance and were often transforming to foreign body multinucleated giant cells. In addition, granulation tissue was formed with infiltrating macrophages, foreign body multinucleated giant cells, capillary proliferation and fibrosis around beta 2M amyloid deposition. On the other hand, inflammatory cell infiltration around amyloid deposition was scarcely seen in AA or AL amyloidosis. Ultrastructurally, macrophages were abundant in phagocytic vacuoles containing amyloid fibrils. These macrophages were immunohistochemically positive for CD68, IL-1 beta and TNF-alpha. Thus, macrophage infiltration around beta 2M amyloid is thought to be responsible for local pain and tissue destruction of dialysis patients.

Amyloid↗
PubMedDate not supplied

[Digestive localization of generalized amyloidosis: attempt of differentiation of "primary" and "secondary" amyloidosis (author's transl)].

The aim of this study is to precise topography of amyloid deposits in the alimentary tract and to differenciate the primary or secondary nature of amyloid substance according to these topographical data and with the help of the Wright's technic. The material of this study consists in nine necropsies and seventeen digestive biopsies, concerning patients with generalized amyloidosis. Immunoglobulinic amyloidoses (so-called "primary") contain predominating deposits in the muscularis propria which remain after Wright's technic. On the other hand, in the non-immunoglobulinic amyloidoses (so-called "secondary"), deposits are essentially localized in the mucosa and disappear (more than 80%) after Wright's technic. Moreover, some special cases, as Portugese amyloidosis and amyloidosis in the course of Crohn's disease, are studied. In the first case, the immunoglobulinic nature of amyloidosis seems to be very likely. In Crohn's disease, in one case, the classical notion of non-immunoglobulinic amyloidosis is confirmed, while, in another one, the amyloidosis is much likely an immunoglobulinic one, and that is a new fact. The authors insist on the practical aspect of this study: it is usually possible to precise the nature of the amyloid deposit on digestive biopsy and so, to give indications to the clinicians about an etiological group.

Amyloidosis↗
PubMed1982

[Digestive amyloidosis in generalized amyloidosis. Current data and practical applications (author's transl)].

Following a summary of the modern, biochemical classification of generalized amyloidosis into immunoglobulin-induced (AL) and non immunoglobulin-induced (AA), the authors study amyloid lesions of the digestive tract. The classical topographical data concerning primary and secondary amyloidosis are described. These data are confirmed by current studies based on the new classification and completed by a technique recently developed by Wright, where treatment of histological sections with potassium permanganate makes it possible to differentiate AL amyloidosis from AA amyloidosis. The resulting practical classification of amyloid deposits enables clinicians to form an idea of the aetiological group concerned. A study of rectal biopsies emphasizes the value of the results. The special cases of Portuguese amyloidosis and amyloidosis associated with Crohn's disease are also studied.

Amyloid↗
PubMed2002

Misdiagnosis of hereditary amyloidosis as AL (primary) amyloidosis.

BACKGROUND: Hereditary, autosomal dominant amyloidosis, caused by mutations in the genes encoding transthyretin, fibrinogen A alpha-chain, lysozyme, or apolipoprotein A-I, is thought to be extremely rare and is not routinely included in the differential diagnosis of systemic amyloidosis unless there is a family history. METHODS: We studied 350 patients with systemic amyloidosis, in whom a diagnosis of the light-chain (AL) type of the disorder had been suggested by clinical and laboratory findings and by the absence of a family history, to assess whether they had amyloidogenic mutations. RESULTS: Amyloidogenic mutations were present in 34 of the 350 patients (9.7 percent), most often in the genes encoding fibrinogen A alpha-chain (18 patients) and transthyretin (13 patients). In all 34 of these patients, the diagnosis of hereditary amyloidosis was confirmed by additional investigations. A low-grade monoclonal gammopathy was detected in 8 of the 34 patients (24 percent). CONCLUSIONS: A genetic cause should be sought in all patients with amyloidosis that is not the reactive systemic amyloid A type and in whom confirmation of the AL type cannot be obtained.

Adult↗
PubMed1993

Symptomatic gastric amyloidosis in patients with primary systemic amyloidosis.

We reviewed the clinical records of 769 patients with primary systemic amyloidosis who had been examined at Mayo Clinic Jacksonville (Jacksonville, Florida) or Mayo Clinic Rochester (Rochester, Minnesota) during a 12-year period (1978 through 1989). Of these 769 patients, 59 (8%) had biopsy-established gastrointestinal amyloidosis, and 8 (1%) had symptomatic gastric amyloidosis. All eight patients with symptomatic gastric amyloidosis had hematemesis or prolonged nausea and vomiting in association with weight loss. Additional findings were gastroparesis (in three patients), gastric tumor (in one), and gastric outlet obstruction (in one). Macroglossia was present in two patients, and multiple myeloma was diagnosed in three. Six of the eight patients had coexisting small bowel amyloidosis and weight losses of 6.5 to 22.5 kg. Congo red staining identified gastric amyloid in the media of blood vessels in all cases. All cases stained selectively for lambda (seven cases) or kappa (one) light chain. All eight patients died; the median duration of survival after diagnosis was 13.8 months (range, 0.5 to 39.5). Death was due to cardiac failure (three patients), renal failure (two), chronic gastrointestinal obstruction and severe cachexia (two), or hepatic failure (one). Chemotherapy was given to seven patients but was only partially effective for ameliorating symptoms in one.

Amyloidosis↗
PubMed1985

Plasma total prekallikrein/kallikrein activity in rheumatoid arthritis with and without amyloidosis. Increased kaolin-stimulated activity in patients with amyloidosis.

Following exposure to kaolin, plasma samples were assayed for total prekallikrein/kallikrein activity in 19 patients with rheumatoid arthritis (RA), 39 patients with RA complicated by amyloidosis, 13 patients with nonamyloid nephropathy and 54 healthy subjects. Increased total kallikrein activity was found in RA patients with amyloidosis and in patients with nonamyloid nephropathy. The concentrations of the plasma kallikrein inhibitors C1-inactivator and alpha 2-macroglobulin were normal in RA patients without amyloidosis, whereas they were increased in patients with amyloidosis as well as in patients with nonamyloid nephropathy. The results suggest that the increased activity of plasma kaolin-stimulated kallikrein in RA patients with amyloidosis is due to the nephropathy per se and probably reflects increased levels of prekallikrein.

Adult↗
PubMed1985

Primary systemic amyloidosis with severe cardiac amyloidosis.

An autopsy case of primary systemic amyloidosis with severe cardiac amyloidosis in a 75-year-old Japanese man is reported. The initial signs were dyspnea and cough, followed by general fatigue and loss of appetite. Heart failure, pleural effusion, and liver cysts were found on physiological examination. Autopsy findings were primary systemic amyloidosis with severe diffuse cardiac amyloidosis and cardiac hypertrophy (585 g). Focal necrosis by infarction was found in the liver and spleen. The cause of amyloidosis was unknown.

Aged↗
PubMed2006

Transmission of amyloidosis in offspring of mice with AApoAII amyloidosis.

Pre-existing amyloid fibrils can induce further polymerization of endogenous precursor proteins in vivo. Thus, transmission of amyloid fibrils (AApoAII) may induce a conformational change in endogenous apolipoprotein A-II and accelerate amyloid deposition in mouse senile amyloidosis. To characterize transmissibility, we examined amyloidosis in the offspring of AApoAII-injected mother mice that possessed the amyloidogenic Apoa2(c) allele of the apolipoprotein A-II gene. At 4 months of age, amyloid deposits were detected in the intestines of offspring born from and nursed by amyloid fibril-injected mothers, with intensity of deposition increasing thereafter. No amyloid deposits were detected in the offspring of noninjected control mothers. Accelerated amyloidosis was also observed in offspring born from mothers without injection but nursed by amyloid fibril-injected mothers. However, this was not observed in offspring born from amyloid fibril-injected mothers but nursed by control mothers. This fostering excluded vertical transmission through the placenta, suggesting the presence of factors that accelerate amyloidosis during the nursing period. In addition, milk obtained from amyloid fibril-injected mothers induced AApoAII amyloidosis in young mice, and transmission electron microscopy detected noodle-like amyloid fibrils in milk of amyloid fibril-injected mothers. These results provide important insight into the etiology and pathogenesis of amyloid diseases.

Alleles↗
PubMed2001

[Treatment of AL-amyloidosis and some other types of amyloidosis].

Patients with AL-amyloidosis are treated at present by conventional or large-dose chemotherapy with autologous transplantation of haematopoietic stem cells, similarly as patients with multiple myeloma. Only the timing of treatment is different. In myeloma treatment is usually indicated only in clinical stage II or III, in clinical stage I only in case of adverse prognostic factors. In AL-amyloidosis treatment is indicated immediatelyafter establishment of the diagnosis. It was found that high-dose chemotherapy with autologous transpantation of haematopoietic cells is at present the most effective treatment for selected patients with not advanced forms of primary systemic AL-amyloidosis. Allogenic transplantation of the liver is treatment of choice in ATTR amyloidosis. In AA-amyloidosis the basis of treatment is removal or suppression of the chronic inflammatory process, possibly colchicin administration.

Amyloidosis↗
PubMed1987

Differentiation of cardiac amyloidosis and hypertrophic cardiomyopathy. A comparison of familial amyloidosis with polyneuropathy and hypertrophic cardiomyopathy by electrocardiography and echocardiography.

The clinical and echocardiographic features of cardiac amyloidosis may closely resemble those of hypertrophic cardiomyopathy, and the disorders may thus be mixed up. The present study was undertaken in an attempt to identify features separating the two conditions by analysis of electro- and echocardiographic findings in patients with familial amyloid polyneuropathy and hypertrophic cardiomyopathy. Twenty-nine patients with familial amyloidosis and 22 with hypertrophic cardiomyopathy were studied. Particular attention was given to the sum of the S wave in V1 and R wave in V5 or V6, the echocardiographic left ventricular mass and cross-sectional area, the presence or absence of asymmetrical septal thickening, granular and sparkling myocardial appearance, thickened heart valves, systolic anterior motion of the mitral valve, and pericardial effusion. A granular and sparkling appearance of the myocardium and thickened heart valves were found to be the best predictors of cardiac amyloidosis, while low QRS amplitudes in relation to echocardiographic left ventricular mass and a pericardial effusion seemed less important. The presence of systolic anterior movement of the mitral valve, a large left ventricular mass and a sum of S in V1 and R in V5 or V6 greater than 35 mm indicated hypertrophic cardiomyopathy. When the four strongest predictors (left ventricular mass, thickened heart valves, a granular sparkling myocardial appearance, and systolic anterior movement of the mitral valve) were used to reclassify the present patients, 28 of 29 amyloidosis patients and 21 of 22 patients with hypertrophic cardiomyopathy were correctly categorized. Noninvasive methods may thus be useful for detecting the myocardial infiltrative process, and cardiac amyloidosis may be confidently diagnosed by typical noninvasive findings together with histopathological documentation of amyloid in an organ other than the heart.

Adult↗
PubMed1985

Classification of amyloidosis: immunohistochemistry versus the potassium permanganate method in differentiating AA from AL amyloidosis.

As systemic AA and Al amyloidosis differ considerably with regard to prognosis and therapeutic approach, it is of importance to make an accurate histochemical classification with regard to the amyloid protein involved. In the present study the results of the potassium permanganate (KMnO4) method, an indirect histochemical procedure based on differences in cross-beta-potential of different amyloid fibril proteins, were compared with the results of an immunohistochemical method utilizing anti-AA and anti-AP antibodies. Renal biopsy sections of patients with systemic amyloidosis related to inflammatory conditions, systemic amyloidosis associated with plasma cell dyscrasia, idiopathic systemic amyloidosis, and nonamyloidotic controls were studied. Positive reaction of anti-AA was observed on all KMnO4-sensitive amyloid deposits, whereas the KMnO4-resistant amyloid deposits remained unstained, provided that highly purified anti-AA antiserum was used. Anti-AP produced not only comparable staining of both KMnO4-sensitive and -resistant amyloid deposits, but also of glomerular basement membranes and elastin layers of blood vessels in amyloid and control biopsies. The intensity of anti-AP reactivity was comparable with the reaction of anti-AA on KMnO4-sensitive amyloid deposits. The present results confirm the specificity of the KMnO4 method, which is a simple method available to every laboratory, in differentiating between AA and AL amyloidosis. Furthermore, the results indicate that, at least in renal biopsy specimens, anti-AP may serve as a general marker for AA and AL amyloid deposition; this finding is in contrast to the results of a recently published report.

Amyloid↗