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PubMed1994

Amyloid deposition in the digestive tract in casein-induced experimental amyloidosis in mice.

In mice with casein-induced experimental amyloidosis, the incidence of amyloidosis in various organs was examined in relation to time, and the extent of amyloid deposition in the digestive tract was investigated. Amyloid was deposited first in the spleen, a little later in the digestive tract, and then in the liver and kidney. In the digestive tract, amyloid appeared simultaneously in the small and large intestine, and later in the glandular stomach. Amyloid deposition was most severe in the ileum, while it was not induced in the esophagus or non-glandular stomach. Initially, amyloid deposition was observed along the small blood vessels and/or epithelial basement membranes in the lamina propria mucosa (LPM); it then extended to the stroma in the LPM. Amyloid deposition in each portion of the digestive tract had characteristic patterns in the LPM. Deposition of amyloid fibrils was confirmed by electron microscopy. The results suggest that the gastrointestinal biopsy used widely to diagnose human reactive amyloidosis is a sensitive early indicator of amyloidosis.

Amyloid↗
PubMed1981

Dubious effect of dimethylsulphoxide (DMSO) therapy on amyloid deposits and amyloidosis.

Data from the literature on DMSO therapy for amyloidosis in laboratory animals and man are reviewed and found to be inconclusive. In hamsters with casein-induced amyloidosis, as well as in dogs with spontaneous amyloidosis, therapeutic experiments with DMSO were performed. In these investigations no effect of DMSO on amyloid and amyloidosis was found.

Amyloid↗
PubMed1983

Amyloidosis of the colon. Report of a case and review of the literature.

A case of amyloidosis of the colon associated with multiple myeloma is presented. The unusual situation was that of obstructive signs with radiologic features of "megacolon and volvulus." A high index of suspicion and meticulous histologic search will demonstrate involvement of the gastrointestinal tract in 98 per cent of patients with systemic amyloidosis. Amyloidosis may mimic other gastrointestinal disorders. Rectal biopsy is diagnostic in 75 per cent of the patients. Treatment of amyloidosis of the colon involves treating the cause with the hope of reversing or at least retarding the process. The results of treatment based on the available experience have been dismal.

Aged↗
PubMed1993

Renal replacement therapy in multiple myeloma and systemic amyloidosis.

Renal failure frequently complicates both multiple myeloma and systemic amyloidosis. Renal replacement therapy (RRT) may be poorly tolerated and its role in such patients is not clearly defined. Of fifty patients (26 males and 24 females) referred to a single centre because of renal failure associated with multiple myeloma or systemic amyloidosis 37 progressed to end-stage renal failure and 30 of these patients received RRT. Nine patients have been treated by CAPD, 13 by haemodialysis, and 8 patients have required both forms of dialysis. Overall one year and two year survival rates were 66% and 57% respectively. The median duration on RRT was 7.5 months (range 1-96 months) with a 51% one year, and a 46% two year survival rate. Of 7 patients with amyloidosis who underwent renal transplantation, 3 died within 6 months of transplantation. Undiagnosed cardiac involvement contributed to this early mortality. We conclude that renal replacement therapy is appropriate for some patients with multiple myeloma and systemic amyloidosis who develop endstage renal failure. Careful assessment and selection of patients is necessary prior to renal transplantation.

Adolescent↗
PubMed2001

Waldenström's macroglobulinemia associated with AA amyloidosis.

It is widely accepted that amyloidosis in Waldenström's macroglobulinemia (WM) is exclusively due to amyloid light-chain deposition. However, only a small number of previous reports have actually characterized the type of amyloid in WM. We now report the third patient with WM and amyloid A protein (AA) amyloidosis. This patient developed malabsorption, nephrotic syndrome, and orthostatic hypotension. AA was immunohistochemically demonstrated in the rectal biopsy. In conjunction with previous examples of AA amyloidosis, the present report raises the possibility that AA amyloidosis may also occur in WM patients.

Aged↗
PubMed2002

Secondary amyloidosis in Castleman's disease: review of the literature and report of a case.

It is quite rare to diagnose secondary amyloidosis during the course of Castleman's disease (CD). A 51-year-old female who complained of fatigue, weight loss, and fever was diagnosed with CD -- plasma cell type -- in our hospital in 1993. One year after diagnosis, she developed nephrotic syndrome, the etiology of which was found to be secondary amyloidosis based on renal biopsy. As the patient rejected therapy, she was discharged after only symptomatic treatment. At her last follow-up in March 2001, she had no complaints; physical examination, blood chemistries, and urinalysis were normal. Abdominopelvic tomography revealed no lymphadenopathy in the abdomen, which had been previously present. We could identify 17 other cases of CD with secondary amyloidosis in the literature. Ours is the 18th such case and the 2nd case of multicentric CD leading to amyloidosis. This case also shows that CD might sometimes run a relatively benign course being cured with no therapy, whereas it might have a rapidly fatal downhill course -- even with therapy -- in others. Still, effective treatment strategies need to be developed.

Amyloidosis↗
PubMed2003

Development of amyloidosis in Behçet's syndrome with isolated mucocutaneous involvement.

Development of secondary amyloidosis is an infrequent complication in patients with Behçet's syndrome (BS). It has been reported that multiple systemic involvement, long disease duration, and male gender are major clinical factors accompanying the development of amyloidosis in BS. We report a case of secondary amyloidosis in a patient diagnosed as having BS with a positive pathergy test 9 years previously and who had isolated mucocutaneous involvement. Regular use of colchicine since the diagnosis and somewhat mild progress of the disease could not prevent the development of secondary amyloidosis in this patient. He is alive and receives hemodialysis regularly.

Adult↗
PubMed2006

Amyloidosis of the heart and respiratory system.

Since the incidence of amyloidosis is increasing, the purpose of this article is to review the imaging features of intrathoracic amyloidosis. Amyloidosis forms a heterogeneous group of disorders characterised by the extracellular deposition of a homologous protein complex. The heart is the most commonly involved organ in the chest. Respiratory amyloidal deposition is much less common and may be generalised, when it occurs as a part of a systemic disease, or it may be restricted only to the respiratory system. Although, the abnormalities are considered non-specific, recent literature suggests-especially for cardiac amyloidosis-specific patterns of abnormalities.

Amyloidosis↗
PubMed2005

Keratoepithelin in secondary corneal amyloidosis.

BACKGROUND: Amyloid is found in several corneal dystrophies, including distinct lattice corneal dystrophies (LCD) and Avellino corneal dystrophy. Recently, point mutations in the transforming growth factor-beta-induced gene (TGFBI) encoding for keratoepithelin (KE) have been demonstrated in these corneal disease entities. We intended to investigate if KE was also a component of the rarely seen secondary corneal amyloid deposits. METHODS: Immunohistochemical staining with a polyclonal antibody against KE was performed on formalin-fixed paraffin-embedded tissue of five corneal buttons with secondary amyloid obtained after keratoplasty. Secondary amyloidosis was due to Fuchs endothelial dystrophy (FED) with bullous keratopathy and/or recurrent erosions in all cases. The diagnosis had been established by light microscopy using Congo red staining. Two cases of LCD type I served as positive controls and three corneas with FED and one with keratoconus without amyloid served as negative controls. RESULTS: All corneas with secondary amyloidosis as well as LCD type I revealed positive staining in the respective amyloid deposits. KE was localized in the subepithelial pannus and in the anterior stroma in the corneas with secondary amyloidosis. In the specimens with LCD type I it was distributed in the amyloid deposits located in the anterior and mid-stroma. Staining for KE showed a granular appearance in all cases. The intensity of staining was variable among the specimens. CONCLUSIONS: KE is found not only in primary amyloid deposits of hereditary corneal dystrophies, but also in secondary amyloidosis of the cornea of diverse ethiologies.

Adult↗
PubMed2002

Pathology, diagnosis and pathogenesis of AA amyloidosis.

Amyloid is defined as a proteinaceous tissue deposit that shows a typical green birefringence in polarised light after staining with Congo red, the presence of non-branching linear fibrils of indefinite length with an approximate diameter of 10-12 nm and a distinct X-ray diffraction pattern consistent with Pauling's model of a cross-beta fibril. Approximately 45% of generalised amyloidoses are secondary or reactive (AA) amyloidosis. Among the causes of AA amyloidosis are rheumatic diseases, idiopathic diseases, inherited diseases, infectious diseases and malignant tumours. Recent decades have provided significant advances in our understanding of the pathology and pathogenesis of AA amyloidosis. Its pathogenesis is multifactorial involving many variables such as primary structure of the precursor protein, acute phase response, the presence of non-fibril proteins (e.g. amyloid P component, apolipoprotein E, glycosaminoglycans, proteoglycans and basement membrane proteins), receptors, lipid metabolism and proteases. Study of the pathogenesis of AA amyloidosis has provided many insights into the nature of conformational diseases, which may help in the understanding of other members of this particularly heterogeneous group of diseases, such as Alzheimer's disease and transmissible spongiform encephalopathies.

Amyloidosis↗
PubMed1999

Cerebrovascular involvement in systemic AA and AL amyloidosis: a clear haematogenic pattern.

Amyloid deposits in cerebral vessels are common in beta-amyloid diseases (Alzheimer's disease, congophilic amyloid angiopathy, Down's syndrome and hereditary cerebral amyloidosis with haemorrhage of the Dutch type). We report of 20 autopsies on patients who had died with systemic amyloidosis of the AA, Alambda and Akappa types: the brains were examined for the occurrence of amyloid. Vascular amyloid was detected in choroid plexus (in 17 of 20 cases), infundibulum (5 of 8), area postrema (6 of 11), pineal body (3 of 7) and subfornical organ (2 of 3), but not in cortical and leptomeningeal vessels. Immunohistochemical classification of the cerebral amyloid and the systemic amyloid syndrome showed identity proving the same origin of both. The distribution is indicative of a haematogenic pattern of amyloid deposition in systemic amyloidosis and is different from that in Alzheimer's, prion, ATTR and cystatin C diseases. It corresponds to areas of the brain with a "leaky" blood-brain barrier. Additionally, all the cases with AA amyloidosis exhibited an Abeta coreactivity in choroid plexus vessels. In one exceptional case, Abeta reactivity of AA amyloid also occurred outside of the brain.

Adult↗
PubMed2000

Gastric amyloidosis with massive bleeding requiring emergency surgery.

We report a 66-year-old woman who had massive bleeding from a gastric ulcer complicating primary systemic amyloidosis, in whom emergency surgery proved lifesaving. Physical examination revealed anemia and macroglossia. Gastroscopy was performed, and an extensive, irregular, hemorrhagic ulcer was found in the gastric body. Biopsy resulted in a diagnosis of amyloidosis. On the 11th hospital day the patient went into shock as a result of a massive hemorrhage. Emergency surgery was performed, but the extent of the submucosal lesion in the stomach could not be identified, and total gastrectomy was unavoidable. Histological examination of the surgical specimen and biopsy tissue collected from other organs revealed amyloid deposition extending from the submucosa to the muscularis propria of the stomach. There was also deposition of large amounts of amyloid around the small blood vessels in the liver and under the mucosa of the small intestine. The amyloid was AA-antibody-negative and resistant to treatment with K2MO4, and a diagnosis of AL-type systemic amyloidosis was made. The patient's general condition recovered after the operation, but on the 103rd hospital day, she experienced sudden onset of arrhythmia and died. Patients with amyloidosis in whom gastrointestinal surgery is performed are rare; only 41 cases, including our own, have been reported in the Japanese literature since 1972.

Aged↗
PubMed2006

Cardiac amyloidosis: shifting our impressions to hopeful.

Cardiac amyloidosis is a well-known but clinically rare cause of heart failure that has historically been associated with a poor prognosis. Cardiac amyloidosis involves fibril formation from one of several underlying conditions, and the course of illness and prognosis varies among these conditions. Evolving treatment strategies for patients with primary systemic amyloidosis have given this subset of cardiac amyloidosis patients a cause for hope. The identification and appropriate referral of patients in whom this condition is suspected will help to improve the likelihood of successful therapy and long-term survival.

Amyloidosis↗
PubMed1988

Detection of novel proteins associated with secondary amyloidosis and Alzheimer's disease by monoclonal antibody.

We have established a monoclonal antibody (MoAb) AM34 (IgG1) which was prepared by a hybridoma constructed from fusion between murine myeloma cells and murine splenocytes. Crude amyloid proteins which were used as immunogen, were extracted from the kidney of a patient with rheumatoid arthritis by the distilled water method. This antibody strongly reacted with all 8 cases of secondary amyloidosis, but did not react or very weakly reacted with 17 tissue sections of primary or myeloma-associated amyloidosis. Other amyloid tissues did not give any positive reaction. Interestingly, 6 brain tissues of Alzheimer's disease clearly showed positive staining with this antibody, whereas two apparently normal brain tissues exhibited negative staining. Senile plaque cores, neurofibrillary tangles (weakly stained) and cerebrovascular amyloid in Alzheimer's disease were stained. Absorption of the MoAb AM34 with the crude amyloid proteins abolished the immunoreactivity of the MoAb AM34 not only with the kidney tissue section of the secondary amyloidosis, but also with the above mentioned portions of the brain in the case of Alzheimer's disease. Therefore, these immunohistological data suggest that the MoAb AM34 recognizes common epitope which exists in amyloid deposits of both secondary amyloidosis and Alzheimer's disease. An inhibition test on the kidney section showed that the reactivity of MoAb AM34 was not at all inhibited by the pretreatment of the section with 10 times higher concentration of anti-human amyloid A (AA) MoAb KM268 which was prepared against synthetic peptides of AA protein, suggesting that MoAb AM34 might react with amyloid-related protein other than AA protein. In addition, MoAb KM268 did not react with any lesions in Alzheimer's disease.(ABSTRACT TRUNCATED AT 250 WORDS)

Alzheimer Disease↗
PubMed1975

Amyloidosis: a rational approach to diagnosis by intraoral biopsy.

Amyloidosis and its oral manifestations are briefly described. The techniques for antemortem tissue diagnosis of amyloidosis are reviewed and evaluated. In screening for amyloidosis, biopsy of specific oral lesions (when present) is recommended instead of the traditional biopsy of normal-appearing gingiva. This approach is illustrated with four cases. Although rectal biopsy is generally accepted as the screening technique of choice, it is suggested that intraoral biopsy be considered as an easier, safer, more comfortable, and possibly more fruitful technique. It is advocated that in cases of both documented and suspected amyloidosis both intraoral and rectal biopsies should be performed in order to help provide documentation of the most useful technique for routine screening.

Aged↗
PubMed1977

Amyloidosis associated with multiple myeloma.

Amyloidosis is a rare, fatal disease caused by deposition of a sulfated mucopolysaccharide in various tissues and organs. Seven to ten per cent of patients with multiple myeloma, a disease of abnormal myeloid cells, have associated amyloidosis. A case of amyloidosis associated with multiple myeloma is described and a differential diagnosis for oral amyloidosis is presented to familiarize the practitioner with this entity.

Amyloidosis↗
PubMed1989

Hemodialysis-associated amyloidosis presenting as lingual nodules.

Hemodialysis has permitted long-term survival of patients with kidney failure, but not without many complications, such as mineral loss from bones, secondary hyperparathyroidism, and increased risk of infection. Recently a new form of amyloidosis, AB2M, has been characterized that is specifically associated with long-term dialysis. The tissues and organs affected by deposits of AB2M appear to differ from those affected by the other major types of amyloidosis; AB2M affects mainly the carpal ligament, synovia of large joints, juxtaarticular bone, and intervetebral disks, while involvement of the oral tissues has been rare. We present here a case in which the biopsy of superficial lingual deposits of AB2M led to the recognition that the patient had developed hemodialysis-associated amyloidosis. It is suggested that periodic inspection of the oral soft tissues for signs or symptoms of amyloidosis should become a part of the dental care of patients undergoing dialysis.

Amyloidosis↗
PubMed1988

The clinical and biochemical spectrum of hereditary amyloidosis.

Familial amyloidosis, once described as a puzzling and highly unusual form of polyneuropathy, is now recognized to be a collection of familial diseases with usually autosomal-dominant inheritance and widespread ethnic distribution. Familial amyloidosis occurs throughout the world and encompasses an extremely broad spectrum of clinical manifestations. In some families, progressive peripheral neuropathy dominates the illness, while in others, renal failure, ocular amyloid deposits, cardiac decompensation, or intracranial hemorrhage is the most significant clinical feature. The Portuguese (type I) and the Iowa (type III) neuropathies characteristically begin with lower limb involvement, while in the Indiana (type II) form, upper limb neuropathy is seen first; in the Japanese families with familial amyloid polyneuropathy, symptoms first become evident around age 40, whereas in the Texas family, onset is in the seventh decade. The prognosis for the different families is highly variable. Current classification of the familial amyloid polyneuropathy syndromes is based on their characteristic clinical presentations, but ongoing biochemical identification of the protein composition of amyloid substance in each form will make a more rational nosology feasible in the near future. To date, no therapy has been shown to arrest or reverse the progressive accumulation of amyloid deposits in most forms of familial amyloidosis. Familial Mediterranean fever is a major exception, and the incidence of amyloidosis associated with this disease has been dramatically reduced by the widespread prophylactic use of colchicine. Technology currently available permits the reliable identification of asymptomatic relatives at risk for developing amyloid neuropathy as well as the prenatal identification of carriers of the mutant transthyretin gene. These strategies can be used in genetic counseling aimed at reducing the continued propagation of the mutant gene.

Amyloid↗