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PubMedDate not supplied

Orbital amyloidosis-induced compressive optic neuropathy accompanied by characteristic eyelid pigmentation.

The deposition of amyloid protein in orbital tissue is called orbital amyloidosis. Orbital amyloidosis is a rare condition that usually affects older patients. Although the disease is slowly progressive, it rarely involves the optic nerve or threatens vision. We report a case of orbital amyloidosis that initially appeared as impressive eyelid pigmentation and blepharoptosis and then progressed to systemic amyloidosis. The orbital lesion induced compressive optic neuropathy. Surgical management enabled partial but not full recovery of vision.

Amyloidosis↗
PubMed2003

Primary (AL) hepatic amyloidosis: clinical features and natural history in 98 patients.

The liver is a common site of amyloid deposition in primary systemic amyloidosis. We reviewed the clinical features and natural history of patients with primary systemic amyloidosis and biopsy-proven hepatic involvement who were evaluated at Mayo Clinic from January 1, 1975, to December 31, 1997. The median age of the study group (68 men; 30 women) was 58.5 years. Seventy-one patients (72%) had involuntary weight loss. Hepatomegaly was found in 79 patients (81%). Eighty-two patients (89%) had proteinuria, and 81 patients (86%) had elevated serum alkaline phosphatase levels. Seventy-six patients (83%) had either a serum or urine monoclonal protein. Before liver biopsy, clinicians considered amyloidosis in the differential diagnosis for only 14 patients (26%). None of our patients experienced hepatic rupture or death due to liver biopsy, and only 4 (4%) bled after liver biopsy. The median survival of the 98 patients was 8.5 months. Predictors of a poor prognosis were congestive heart failure, elevated concentrations of bilirubin, and a platelet count greater than 500 x 109/L. In conclusion, clinicians should consider the diagnosis of primary hepatic amyloidosis in patients who present with involuntary weight loss or hepatomegaly. Other clues to the diagnosis include an unexplained elevated serum alkaline phosphatase level, proteinuria, and evidence for hyposplenism (for example, Howell-Jolly bodies on peripheral blood smear). Liver biopsy was safe. Some patients benefit from systemic chemotherapy.

Amyloidosis↗
PubMed2003

Orthotopic liver transplantation for hereditary fibrinogen amyloidosis.

Systemic amyloidosis results from the deposition of insoluble protein fibrils in various organs and tissues. To date, several different proteins have been associated with amyloid fibril formation, including immunoglobulin light chain, serum amyloid A protein, and transthyretin. Recent reports have shown that variant fibrinogen chains can form amyloid in certain kindreds. Hepatic transplantation has previously been reported in the treatment of hereditary amyloidosis associated with variant transthyretin proteins, which are mainly synthesized in the liver. This article reports the first use and long-term follow-up of combined hepatic and renal transplantation in the successful treatment of two patients with hereditary fibrinogen amyloidosis. Both patients experienced sustained improvement in renal function and nutritional status at 61/2 years and 28 months of follow-up, respectively. Orthotopic liver transplantation is effective and potentially curative treatment of hereditary fibrinogen amyloidosis.

Amyloidosis, Familial↗
PubMed1987

Localized primary amyloidosis of the stomach presenting with gastric hemorrhage.

We report a patient with localized, primary gastric amyloidosis, who presented with recurrent hematemesis, a rare presentation for an unusual disease. The patient was initially thought to have stomach cancer because of the X-ray and gastroscopic appearance of the gastric mucosa, but was eventually found to have primary amyloidosis confined to the stomach and regional lymph nodes. The amyloid was found to be of immunoglobulin origin, AL amyloid. Other reports of localized gastric amyloidosis are reviewed and compared with the present case. Most of the patients were clinically suspected of gastric carcinoma, and only one had hematemesis. We propose that amyloidosis should be considered in the differential diagnosis of hematemesis and gastric tumors.

Amyloidosis↗
PubMed1994

Primary nodular cutaneous amyloidosis--long-term follow-up and treatment.

A case of facial primary nodular cutaneous amyloidosis is reported. This illustrates: the striking appearance of this unusual condition; the investigations appropriate to establish the diagnosis and to exclude underlying systemic amyloidosis or a condition which might contribute to amyloidosis; and the difficulty of successful management. Initial investigation failed to reveal any evidence of systemic amyloidosis or an associated internal illness. Two amyloid nodules were excised, but 7 years later the patient developed further nodules on the adjacent facial skin and again sought dermatological advice. He was reinvestigated and again no underlying condition was found. A trial of cryotherapy was unsuccessful, but curettage and cautery produced a cosmetically acceptable result.

Adult↗
PubMed2006

Successful treatment of lichen amyloidosis with combined bath PUVA photochemotherapy and oral acitretin.

Lichen amyloidosis (LA) is a chronic, pruritic skin disorder characterized by brownish-grey papules on extensor surfaces of legs and rarely on the trunk. Thioflavin T-positive amyloid deposits are found in the papillary dermis of affected skin, which is the only organ involved. A variety of therapeutic regimens for lichen amyloidosis have been described; however, in many cases with only limited effect. We report on two patients with lichen amyloidosis with typical clinical symptoms not responding to local treatment. A combined regimen with bath psoralen ultraviolet A (PUVA) and oral acitretin was initiated, resulting in nearly complete resolution of the papules and impressive relief from the severe pruritus. The beneficial response has persisted for 8 months. The suggested combined therapy with bath PUVA photochemotherapy and oral acitretin represents an efficacious and practical treatment modality for lichen amyloidosis with long-lasting effects.

Acitretin↗
PubMed2006

Secondary amyloidosis causing nephrotic syndrome in a patient with non-Hodgkin's lymphoma: quite a rare diagnosis.

Secondary amyloidosis is usually a complication of chronic inflammation. Amyloidosis cases during the course of non-Hodgkin's lymphoma (NHL) are usually of AL-type, only one NHL patient with secondary amyloidosis has been reported. Our 79-year-old male patient visited us with multiple lymphadenopathies, and he was diagnosed with nodal marginal zone B-cell lymphoma. After four cycles of combined chemotherapy; his urea, creatinine levels started to increase and he developed nephrotic-range proteinuria. His rectal biopsy demonstrated amyloid deposition in submucosal vessel walls. The patient has been under hemodialysis for 10 months and his lymphoma is still in partial remission. We presented this case because it is the second NHL patient who developed secondary amyloidosis during his disease course.

Aged↗
PubMed1994

Amyloidosis.

Amyloidosis is a heterogeneous group of disorders characterized by extracellular deposition of abnormal protein fibrils which are derived from different proteins in different forms of the disease. Asymptomatic amyloid deposition in a variety of tissues is a universal accompaniment of ageing, and clinical amyloidosis is not rare. Intracerebral and cerebrovascular beta-protein amyloid deposits are a hallmark of the pathology of both sporadic and familial Alzheimer's disease, beta 2-microglobulin-derived amyloid is a common complication of long term haemodialysis, and islet amyloid polypeptide is the fibril protein in the universal islet amyloidosis of type II diabetes mellitus. New fibril proteins have lately been identified in hereditary amyloidosis, including variants of gelsolin, apolipoprotein AI, lysozyme and fibrinogen. The development of radiolabelled serum amyloid P component (SAP) scintigraphy has allowed amyloid to be diagnosed non-invasively in vivo for the first time, provided unique insight into the distribution and size of amyloid deposits, and yielded novel information on the natural history and the effects of treatment. Amyloid deposits are in a state of dynamic turnover and can regress if new fibril formation is halted. The recent elucidation of the three dimensional structure of human SAP may enable the design of specific therapeutic agents.

Amino Acid Sequence↗
PubMed1996

Etiologies of the sicca syndrome: primary systemic amyloidosis and others.

BACKGROUND: The sicca syndrome has been defined as the occurrence of xerostomia and xerophthalmia. Sjögren's syndrome is the most common cause of the sicca syndrome; however, these two syndromes are not synonymous and there are many potential etiologies of the sicca syndrome. A less known cause of sicca syndrome is amyloidosis that to date has only been reported in the nondermatology literature. OBSERVATIONS: A 79-year-old man with known amyloidosis presented with persistent xerostomia. He had the classic cutaneous findings of periorbital and "pinch" purpura. A labial biopsy showed diffuse deposition of amorphous eosinophilic material surrounding salivary acini. Apple-green birefringence was noted with Congo red staining and the diagnosis was made of amyloidosis in the minor salivary glands causing xerostomia. CONCLUSIONS: The sicca syndrome can be caused by systemic amyloidosis. Because this fact is not in the dermatologic literature, many dermatologists are not aware of this uncommon presentation. The knowledge of the many causes of the sicca syndrome and an understanding of the differences between this and Sjögren's syndromes are important for any dermatologist.

Aged↗
PubMed1994

Improved outcome of renal transplantation in amyloidosis.

We report our results in 96 patients with amyloidosis who received 105 cadaveric renal allografts. The graft survival of amyloidosis patients has improved with time and with improved immunosuppression. The graft survival of amyloidosis patients is comparable to the results in another systemic disease, i. e., diabetes, and only slightly inferior to those in primary renal disease, even though amyloidosis patients tolerate complications poorly and the patients are at high risk of dying during the first 3 months.

Adolescent↗
PubMed1990

Beta 2-microglobulin amyloidosis in hemodialysis patients. An autopsy study of intervertebral disks and posterior longitudinal ligaments.

Ninety-five autopsy cases of chronic renal failure, which had or had not been treated by hemodialysis, were examined histologically and immunohistochemically for evidence of amyloid deposition in the intervertebral disks and posterior longitudinal ligaments of the spine. beta 2-Microglobulin (beta 2M) amyloid was not present in non-dialyzed patients with chronic renal failure. In cases showing beta 2M amyloid deposition, the shortest term of hemodialysis was 2 years and 5 months. The incidence of beta 2M amyloidosis tended to increase as the dialysis period was prolonged. An inverse correlation was present between dialysis period and age in 22 cases showing beta 2M amyloid deposition (correlation coefficient: -0.43, p less than 0.05), and beta 2M amyloidosis tended to occur earlier in elderly patients than in younger patients. This suggests that elderly patients are more susceptible to beta 2M amyloidosis. beta 2M amyloid was absent in all of 8 cases of systemic lupus erythematosus which were treated by dialysis for periods ranging from 2 days to 12 years. In these patients, beta 2M amyloidosis may have been prevented by steroids, which had been administered for long periods in all cases. Another amyloid of unknown composition was also frequently present in the intervertebral disks and posterior longitudinal ligaments not only in patients with chronic renal failure but also control patients without chronic renal failure. This amyloid was immunohistologically negative for beta 2M, amyloid A protein, light chain kappa or lambda, prealbumin, and apolipoprotein A-II.

Aging↗
PubMed1996

Immunohistochemical study with anti-advanced glycation end-products antibody in murine amyloidosis.

Advanced glycation end-products (AGE) are formed in the late phase of the non-enzymatic glycosylation reaction in conditions such as diabetes mellitus and aging. In amyloidosis, AGE have been found in the A beta 2M amyloid associated with long-term hemodialysis and in the beta-protein in Alzheimer's disease. Murine AApoAII and AA amyloidosis were examined immunohistochemically using anti-AGE monoclonal antibody, 6D12. AApoAII amyloid deposits studied in one senescence-accelerated mouse P1 (SAMP1), congenic mice that have the amyloidogenic apolipoprotein A-II of SAMP1 mice, and AKR mice all reacted with biotinylated 6D12 by formic acid pretreatment, whereas AA amyloid deposits did not react with the antibody. The immunoreaction with anti-apolipoprotein A-II for amyloid deposits in senile mice was approximately homogeneous in intensity; on the other hand the reaction with biotinylated 6D12 was irregular in distribution and intensity over the amyloid deposits. These findings suggest that amyloid precursor proteins are not associated uniformly with AGE modification before deposition as amyloid; it is more likely that the AGE modification progresses gradually and unevenly after amyloid deposition. Murine amyloidosis may be a useful model to elucidate the role of AGE in amyloidosis.

Amyloidosis↗
PubMed2005

Hereditary amyloidosis in early childhood associated with a novel insertion-deletion (indel) in the fibrinogen Aalpha chain gene.

BACKGROUND: Systemic amyloidosis occurring in early childhood is extremely rare, and is usually of AA type complicating chronic inflammatory diseases. We report the molecular basis of amyloidosis in a Korean girl who presented at 7 years of age with asymptomatic proteinuria and developed amyloid hepatomegaly and end-stage renal failure within 2 years. METHODS: Renal biopsy showed enlarged glomeruli virtually replaced by amyloid, but without interstitial or vascular involvement. The histologic appearance was identical to that seen in patients with hereditary fibrinogen Aalpha chain Glu526Val amyloidosis, and the amyloid deposits stained specifically with antibodies to fibrinogen. Mutations were sought in the genes of the amyloidogenic proteins, transthyretin, apolipoprotein AI, lysozyme and fibrinogen Aalpha chain genes by polymerase chain reaction (PCR) and sequencing. RESULTS: A unique frameshift insertion-deletion (indel) mutation was identified in one allele of her fibrinogen Aalpha chain gene, which encodes a partly novel peptide and a premature stop signal, similar to the two previously reported amyloidogenic point deletions at codons 522 and 524 in this molecule. The mutation was absent in samples verified to be from her parents, indicating that it had occurred de novo. CONCLUSION: This is the first description of hereditary fibrinogen Aalpha chain amyloidosis in an Asian individual, and the distinctive renal histology offered a strong clue to the diagnosis. The disease is potentially curable by combined hepatorenal transplantation.

Amino Acid Sequence↗
PubMed2001

Symptomatic gastrointestinal amyloidosis in an HIV-infected patient.

We report a rare case of symptomatic GI amyloidosis in an HIV-infected patient who ultimately developed uncontrollable upper GI bleeding. Gastric and jejunal biopsies revealed amyloidosis. Although the patient's history suggested the possibility of secondary amyloidosis, immunohistochemical staining together with serum electrophoresis and immunofixation revealed the presence of lambda light chains indicating primary amyloidosis.

Amyloid↗
PubMed2006

Successful hepatorenal transplantation in hereditary amyloidosis caused by a frame-shift mutation in fibrinogen Aalpha-chain gene.

Hereditary systemic amyloidosis comprises several autosomal dominant diseases caused by mutations in a number of plasma proteins, including the fibrinogen Aalpha-chain. Four mutations in the fibrinogen Aalpha-chain that are able to induce amyloidosis have been identified so far, the most common being the Glu526Val mutation. We have observed a family in which the father and his son reached end-stage renal failure because of renal amyloidosis induced by a frame-shift mutation in the fibrinogen Aalpha-chain gene producing a novel amyloid protein. Two kidney transplantations in the father and one in the son resulted in fast graft loss caused by recurrence of amyloid deposition. We then performed hepatorenal transplantation in the son. Three years later, liver and kidney functions are normal without recurrence of amyloid deposition. This case, together with three others with the Glu526Val mutation in the extensive literature, suggests that liver transplantation can cure hereditary fibrinogen amyloidosis, whatever the mutation may be.

Adult↗
PubMed1977

Amyloidosis in ageing obese-hyperglycemic mice and their lean litter-mates. A morphological study.

The occurrence of amyloidosis in obese-hyperglycemic mice (genotype obob) about 18 months old and their lean litter-mates was studied. Amyloidosis of varying degrees was found in 60 per cent of the mice and was equally common in both groups. Large amounts of amyloid were usually seen in the adrenal glands, liver, spleen and kidneys. In the kidneys, the amyloid was found mainly in the glomeruli, in the mesangial region. Electron microscopy of isolated amyloid fibrils showed that these consisted of two filaments about 40 A thick, twisted around each other. It is concluded that the distribution of the amyloidosis in these mice is similar to that seen in secondary or experimental murine amyloidosis.

Adrenal Glands↗
PubMed1987

The prevalence of renal amyloidosis of the AA-type in a series of 1,158 consecutive autopsies.

To determine the prevalence of renal amyloidosis of the AA-type in a defined population, formalin-fixed specimens from the kidneys of all the cases autopsied in 1983 at The General Hospital of Malmö, Sweden, were investigated using immunohistochemical techniques. Amyloid deposits of protein AA were found in 10 of 1,158 investigated cases and the calculated prevalence was 0.86 per cent. The mean age at death of the individuals with the AA-type of amyloidosis was 79 years. Six of the cases with amyloidosis had rheumatoid arthritis. The avidin-biotin-peroxidase complex technique was found to be superior to the immunofluorescence method and a high sensitivity and specificity was achieved when sequence-specific antibodies against a synthetized nonapeptide corresponding to a hydrophilic segment of the polypeptide chain of protein AA were used in the assay. Nine cases with other types of amyloid deposits in the kidneys were also detected. None of these cases showed any AA immunoreactivity but all of them demonstrated Congophilic deposits which were immunohistochemically stained by antibodies against the amyloid P-component. The prevalence of renal amyloidosis comprising all types of amyloid protein deposits was 1.64 per cent.

Aged↗
PubMed1997

Dialysis-related amyloidosis and clinical significance of extracorporeal removal of beta2-microglobulin.

Dialysis amyloidosis is a frequent complication encountered in patients receiving chronic hemodialysis. beta2-Microglobulin (beta2M) is a causative protein of amyloidosis, and its deposition in the tissues has been proven to be a primary cause of the onset. As a therapeutic approach to dialysis-related amyloidosis, high flux dialysis membranes permitting the elimination of beta2M with satisfactory biocompatibility have been developed, and the resultant high flux membranes have been clinically introduced. Positive clinical effects have been observed both in retrospective and prospective studies of the use of high flux membranes, together with a decrease in serum beta2M level. However, it cannot be concluded that amyloid deposits are decreased when the elimination of beta2M is maintained by a dialysis technique with a high flux membrane for some period of time. In the present paper, we review the recent clinical studies on extracorporeal removal of beta2M as a therapeutic approach to amyloidosis.

Adsorption↗