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At least 451 records · Page 25Linked to original sources
PubMed1984

Peripheral and autonomic nerve lesions in systemic amyloidosis. Three pathological types of amyloid polyneuropathy.

Twenty autopsy cases of systemic amyloidosis, consisting of 10 cases of primary systemic amyloidosis, 6 cases of myeloma-associated amyloidosis, 2 cases of secondary amyloidosis, and 2 cases of hereditary amyloidosis, were studied clinically and pathologically with special reference to peripheral and autonomic neuropathy. The peripheral nerves of 8 cases with clinical manifestations of polyneuropathy showed deposition of amyloid in the endoneurium, capillaries within the nerve fascicles, perineurium, and epineurium with a loss and degeneration of the nerve fibers. In the peripheral nerve lesions of these cases, there appeared to be three types: I. Endoneurial deposition of amyloid--loss of unmyelinated and small myelinated fibers, II. vessel wall deposition of amyloid in the vasa nervorum--loss of large myelinated fibers; and III. a mixed type of I and II. While the peripheral nerves of 12 cases without neuropathy mainly showed deposition of amyloid in the epineurium and perineurium with well preserved nerve fibers. The possibility was considered that the pathogenesis and variety of peripheral and autonomic nerve lesions might be related to the various molecular features of amyloid proteins or their precursors in systemic amyloidosis.

Adult↗
PubMed1982

Prolonged dimethylsulphoxide treatment in 13 patients with systemic amyloidosis.

Continuous oral dimethylsulphoxide (DMSO) treatment (7-15 g/day) was given to 3 patients with amyloidosis of familial Mediterranean fever (FMF), 3 patients with idiopathic amyloidosis, and 7 patients with secondary amyloidosis. The nephrotic syndrome and various degrees of renal insufficiency were the major clinical manifestation in all case. Renal function was used as the main parameter for evaluation of therapy. DMSO treatment for 7-16 months produced no effect in the FMF patients and in the patient with idiopathic amyloidosis; they all ran the predictable clinical course of their disease and either died of cardiac failure or have been maintained on chronic haemodialysis. In the 7 patients with secondary amyloidosis an unequivocal improvement of renal function was observed following 3-6 months of DMSO treatment. It was shown by a 30-100% rise of creatinine clearance and a decline in proteinuria. This new equilibrium has been maintained as long as DMSO was administered. No serious side effects of DMSO wee encountered. Mild nausea and an unpleasant breath odour were the patients' main concern. We conclude that a therapeutic trial with oral DMSO is warranted in all patients with secondary amyloidosis. This treatment is unpleasant but bears no exceptional risks. It may significantly prolong life, though its effect on amyloid deposits themselves is doubtful.

Adult↗
PubMed1997

Familial and primary (AL) cardiac amyloidosis: echocardiographically similar diseases with distinctly different clinical outcomes.

OBJECTIVE: To determine whether patients with myocardial amyloidosis due either to AL (primary) amyloid or familial amyloid have distinguishing echocardiographic or electrocardiographic features; and to compare the prevalence of heart failure and survival in the two types of amyloidosis in relation to echocardiographic findings. DESIGN: Blinded group comparison of randomly selected cases of cardiac amyloidosis. SETTING: International referral centre for amyloid research and treatment. PATIENTS: 36 patients with cardiac amyloid heart disease, of whom 12 had familial and 24 had primary AL amyloidosis. RESULTS: Familial and AL echocardiograms were morphologically indistinguishable, with similar left ventricular wall thickness, mean (SD) 15.4 (2.3) nu 15.8 (2.5) mm, respectively; right ventricular wall thickness was also similar between amyloid types: 9.6 (2.8) nu 9.7 (6.5) mm, respectively. Doppler indices of left and right ventricular function, left ventricular volume, and ejection fraction were also similar. Low voltage electrocardiograms (< 0.5 mV) were more common in the AL (16/24, 67%) than in the familial group (4/12, 25%), P < 0.05. The one year survival for familial and AL forms was 92% (11/12) nu 38% (6/24), respectively, with virtually all deaths due to cardiac causes. CONCLUSIONS: Although cardiac involvement is echocardiographically indistinguishable, cardiac mortality is very different between the two forms of amyloidosis. Preservation of electrocardiographic voltage in familial amyloidosis suggests that the particular biochemical characteristics of distinct types of amyloid fibril have different pathological effects on the myocardium. This distinction becomes critical in the evaluation, treatment, and management of patients who have a diagnosis within the spectrum of the protein deposition diseases.

Amyloidosis↗
PubMedDate not supplied

Amyloidosis: review and CT manifestations.

Amyloidosis is a collection of disease entities that produce considerable morbidity and mortality and are increasing in prevalence. The imaging findings are problematically nonspecific and diverse. This lack of specificity is compounded by the fact that amyloidosis is strongly associated with and frequently coexists with many other chronic disease states that have their own imaging findings. Amyloidosis can involve any organ singly or in conjunction with other organs and can do so in the form of a focal, tumorlike lesion or an infiltrative process. In the proper clinical setting, that is, in a patient with chronic inflammatory disease and especially in a patient with multiple myeloma, amyloidosis should be considered as a possible cause of worsening or new symptoms or imaging findings. Occasionally, the radiologic findings may precede the clinical findings, thus providing the radiologist with the opportunity to contribute to the patient's care. However, to make a difference in patient care, the radiologist must be familiar with the diverse imaging findings of amyloidosis as well as the patient's clinical history, which could raise the suspicion of amyloidosis.

Aged↗
PubMed2004

Association of FMF-related (MEFV) point mutations with secondary and FMF amyloidosis.

BACKGROUND: Familial Mediterranean fever (FMF) is the major cause of AA amyloidosis in Turkey. M694V mutation in MEFV gene was suggested to be associated with severe clinical features and amyloidosis of FMF. METHODS: In this study, the frequencies of three FMF-related MEFV mutations (M694V, M680I and V726A) were investigated in FMF patients with (AA-FMF, n = 37) and without amyloidosis (non-AA-FMF, n = 35), in patients with secondary amyloidosis related to non-FMF inflammatory conditions (S-AA, n = 19) and in a non-inflammatory control group (n = 185) by molecular genetic studies using polymerase chain reaction with the ARMS (amplification refractory mutation system) method. RESULTS: Both AA and non-AA-FMF patients had significantly higher MEFV mutations compared to non-inflammatory controls (81 and 62.7% respectively vs. 4.2%, p = 0.0001). AA-FMF patients carried significantly more MEFV mutations than non-AA-FMF patients (p = 0.01). M694V was the most common mutation in both FMF groups (63.5 vs. 51.4%), however allele frequency (p = 0.17) and the number of homozygous patients for this mutation did not differ between the groups (p = 0.77). Although lower compared to FMF patients, S-AA patients also had a significantly higher incidence of MEFV mutations than non-inflammatory controls (21 vs. 4.2%) (p = 0.0002). M694V was the only MEFV mutation in this group. CONCLUSION: MEFV mutations are found to be increased both in FMF and non-FMF associated secondary amyloidosis in our study; however, no clear association between M694V and amyloidosis is observed, except in the non-FMF group. Our results suggest that MEVF mutations may also serve as a severity marker for other inflammatory conditions.

Adult↗
PubMed1992

Colchicine prevents kidney transplant amyloidosis in familial Mediterranean fever.

Twenty-one familial Mediterranean fever (FMF) patients who received a kidney transplant for terminal renal failure due to amyloidosis were studied retrospectively to evaluate the prophylactic effect of colchicine on graft amyloidosis. Proteinuria, highly suggestive of kidney transplant amyloidosis, developed in 11 patients within a median of 3 years after transplantation (range 0.5-10 years). In 10 patients, repeated urinalyses for protein were negative during a median of 5 years after transplantation (range 1-13). Patients who developed proteinuria or transplant amyloidosis received smaller colchicine doses than patients without proteinuria--mean 0.69 (range 0-1) versus 1.53 (range 1-2) milligrams per day (p = 0.0002), suggesting that colchicine prevents or delays development of transplant amyloidosis. This prophylactic effect of colchicine was complete at a dose of 1.5 mg/day or more and absent at a daily dose of 0.5 mg or less. In patients who received 1 mg/day, individual variability in the response to colchicine was observed. We conclude that the development of amyloidosis of the kidney transplant in FMF is inevitable at a colchicine dose lower than 1 mg/day, unpredictable at 1 mg/day and usually preventable with 1.5 mg/day or more.

Adolescent↗
PubMed1994

Hereditary renal amyloidosis with a novel variant fibrinogen.

Two families with hereditary renal amyloidosis were found to have a novel mutation in the fibrinogen A alpha chain gene. This form of amyloidosis is an autosomal dominant condition characterized by proteinuria, hypertension, and subsequent azotemia. DNAs of patients with amyloidosis were screened for a polymorphism in fibrinogen A alpha chain gene by single-strand conformation polymorphism analysis, and affected individuals from two kindreds were found to have a mutation. Both of these kindreds are American of Irish descent presenting with non-neuropathic, nephropathic amyloidosis in the fifth to the seventh decade of life. DNA sequencing showed a point mutation in the fibrinogen A alpha chain gene that is responsible for substitution of valine for glutamic acid at position 526. By restriction fragment length polymorphism analysis, 7 affected individuals and 14 asymptomatic individuals in these two kindreds were positive for the fibrinogen A alpha chain Val 526 gene. Fibrinogen was isolated from plasma of a heterozygous gene carrier and shown to contain approximately 50% variant fibrinogen. Discovery of this new mutation confirms the association between fibrinogen A alpha chain variant and hereditary renal amyloidosis and establishes a new biochemical subtype of amyloidosis.

Aged↗
PubMed2004

Laryngeal amyloidosis: localized versus systemic disease and update on diagnosis and therapy.

The clinical and pathological characteristics, possibility of systemic disease, and effect of local therapy were studied in laryngeal amyloidosis. Records of all patients with localized laryngeal amyloidosis in a single tertiary referral center were examined retrospectively at diagnosis and after local therapy. Of 188 new patients with amyloidosis between 1990 and 2003, 5 patients had localized laryngeal amyloidosis. A sixth patient with localized laryngeal amyloidosis turned out to have systemic AL (immunocyte-derived) amyloidosis 8 years later. Free light chains were found in this patient, as well as in 1 of the other 5 patients. Amyloid interfering with laryngeal or airway function was removed during microlaryngoscopy with a carbon dioxide laser or cold endoscopic excision. The best results were seen when glottic deposits were removed by cold endoscopic excision, and supraglottic deposits by a carbon dioxide laser. Four patients had recurrent disease. A systematic workup, including measurement of free light chains, helps to rule out systemic disease.

Adult↗
PubMedDate not supplied

Localized amyloidosis of the head and neck and upper aerodigestive and lower respiratory tracts.

Seven cases of localized amyloidosis limited to structures of the head and neck and upper aerodigestive and lower respiratory tracts evaluated and treated at Boston University Hospitals in a recent 7-year period were reviewed. Negative Congo red staining of abdominal adipose aspiration biopsy or rectal biopsy specimens established that the amyloidosis was not systemic. Localized amyloidosis occurred in discrete masses in a variety of sites in the aerodigestive tract including the orbit, nasopharynx, lips, floor of mouth, tongue, larynx, and tracheobronchial tree. Five patients required surgical excision because of significant airway obstruction or organic dysfunction. Amyloid deposits completely excised with the carbon dioxide laser have not recurred, though other amyloid masses may appear elsewhere within the same organ or region. Amyloidosis may occur primarily or secondarily to other disease states. Localized amyloidosis has not been chemically identified but is usually defined by the absence of systemic features. While rare, amyloidosis must be recognized and understood by the otolaryngologist/head and neck surgeon to allow appropriate diagnostic and therapeutic planning.

Adipose Tissue↗
PubMed2002

Analysis of V(lambda)-J(lambda) expression in plasma cells from primary (AL) amyloidosis and normal bone marrow identifies 3r (lambdaIII) as a new amyloid-associated germline gene segment.

Primary (AL) amyloidosis is a plasma cell dyscrasia characterized by extracellular deposition of monoclonal light-chain variable region (V) fragments in the form of amyloid fibrils. Light-chain amyloid is rare, and it is not fully understood why it occurs in only a fraction of patients with a circulating monoclonal component and why it typically associates with lambda isotype and lambdaVI family light-chain proteins. To provide insights into these issues, we obtained complete nucleotide sequences of monoclonal V(lambda) regions from 55 consecutive unselected cases of primary amyloidosis and the results were compared with the light-chain expression profile of polyclonal marrow plasma cells from 3 healthy donors (a total of 264 sequences). We demonstrated that: (1) the lambdaIII family is the most frequently used both in amyloidosis (47%) and in polyclonality (43%); (2) both conditions are characterized by gene restriction; (3) a very skewed repertoire is a feature of amyloidosis, because just 2 germline genes belonging to the lambdaIII and lambdaVI families, namely 3r (22% of cases, lambdaIII) and 6a (20%, lambdaVI), contributed equally to encode 42% of amyloid V(lambda) regions; (4) these same 2 gene segments have a strong association with amyloidosis if their prevalences are compared with those in polyclonal conditions (3r, 8.3%, P =.024; 6a, 2.3%, P =.0008, chi2 test); (5) the J(lambda)2/3 segment, encoding the fourth framework region, appears to be slightly overrepresented in AL (83% versus 67%, P =.03), and this might be related to preferential J(lambda)2/3 rearrangement in amyloid (11 of 12 cases) versus polyclonal 3r light chains (13 of 22 cases). These findings demonstrate that V(lambda)-J(lambda) expression is more restricted in plasma cells from amyloidosis than from polyclonal bone marrow and identify 3r as a new disease-associated gene segment. Overusage of just 2 gene segments, 3r and 6a, can thus account for the lambda light-chain overrepresentation typical of this disorder.

Adult↗
PubMed1978

Patterns of pulmonary involvement in systemic amyloidosis.

The clinical and histopathologic features of pulmonary amyloidosis were reviewed in 22 patients with systemic amyloidosis who came to autopsy. Eleven of 12 patients (92 percent) with primary amyloidosis had prominent interalveolar amyloid deposits. Symptoms attributable to these deposits were found in four cases (33 percent), while severe lung involvement was the apparent cause of death in one. Extensive deposition was noted in all three cases of amyloidosis associated with multiple myeloma or Waldenstrom's macroglobulinemia. Five of seven patients (71 percent) with secondary amyloidosis showed histologic lung involvement, which was perivascular or tracheobronchial in location, but not associated with symptoms. Histologic lung involvement is frequent in all forms of amyloidosis and lung tissue obtained from any patient with unexplained interstitial or reticular-alveolar pulmonary disease should be stained with Congo-red and viewed for green birefringence under polarizing microscopy for the presence of amyloid.

Adult↗
PubMed1999

Heart rate variability during chronic hemodialysis and after renal transplantation: studies in patients without and with systemic amyloidosis.

The present study was undertaken to compare heart rate variability (HRV) values in patients on maintenance hemodialysis with no evidence of ischemic or hypertensive heart diseases to those of age- and gender-matched healthy individuals and those of patients after renal transplantation. To assess the effects of a common confounding factor, HRV values were also determined in patients with systemic amyloidosis, in chronic hemodialysis, and after successful renal transplantation. Spectral analyses of RR intervals from continuous electrocardiogram recordings were performed to quantify ultra low frequency, very low frequency, low frequency, and high frequency powers. HRV determinations were all significantly reduced in uremic patients undergoing hemodialysis compared with the healthy control subjects, especially in those with systemic amyloidosis. Renal transplantation normalized HRV in most patients; HRV, however, remained reduced in isolated amyloidosis patients with cardiac or adrenal involvement. HRV circadian day/night differences were preserved in hemodialysis patients and after renal transplantation in those without amyloidosis but not in those with amyloidosis. These data suggest that reduced HRV in chronic hemodialysis patients may precede other manifestations of cardiovascular disease. In uremic patients with amyloidosis, a more severe form of autonomic failure may occur. Successful transplantation corrects HRV abnormalities in most patients, suggesting that the autonomic dysfunction of uremia is caused by humoral factors reversed by the normalization of the renal function.

Adolescent↗
PubMedDate not supplied

Clinical studies on amyloidosis complicated with rheumatoid arthritis--with particular reference to nephropathy.

Twenty-two patients with definite or classical rheumatoid arthritis (RA) who were diagnosed as amyloidosis by biopsy or at autopsy were investigated. The average duration of RA prior to the diagnosis of amyloidosis was 16.5 +/- 12.5 years. The symptoms that led to the diagnosis of amyloidosis were renal symptoms in 11 cases and gastrointestinal symptoms in 5 cases. Urinary protein was positive in 16 cases (73%). The degree of proteinuria varied in each case. Nephrotic syndrome was observed in 5 cases. Azotemia (Cr greater than 1.5 mg/dl) was present in 18 cases (82%). The period from the diagnosis of amyloidosis to death was 3.0 +/- 2.2 years. The causes of death were uremia in 10 cases, heart failure in 2 cases, malignancy in 2 cases, sepsis in 2 cases and others in 2 cases. Thirteen patients were autopsied and the frequency of amyloidosis complicated with RA was 22.0% in autopsied rheumatoid patients. Although nephropathy was present in most cases of amyloidosis complicated with RA, proteinuria and azotemia greatly varied in both degree and course.

Adult↗
PubMed1983

No evidence of amyloidosis in type I diabetics treated with continuous subcutaneous insulin infusion.

A recent study has demonstrated secondary amyloidosis in dogs treated with continuous intravenous insulin infusion. Since elevated levels of serum amyloid A protein (SAA) and diminished amyloid fibril degrading activity (AFDA) are associated with amyloidosis, we measured SAA and AFDA in ten type I diabetics treated with continuous subcutaneous insulin infusion and in five conventionally treated patients. Only one pump- and one conventionally treated patient had detectable but low SAA levels, comparable with these seen in healthy controls. In patients with secondary amyloidosis the mean SAA level was 24-fold higher than in controls (P less than 0.001). Similarly, in both diabetic groups, AFDA was normal whereas it was reduced by 41% in patients with amyloidosis (P less than 0.001). Furthermore, no local amyloidosis was seen at the infusion site in any of the patients studied. Thus, our data fail to provide any evidence of secondary amyloidosis in patients treated for 3-40 mo with continuous subcutaneous insulin infusion.

Adult↗
PubMedDate not supplied

Primary amyloidosis presenting as a nasopharyngeal mass.

Amyloid is defined as a pathologic proteinaceous substance which, when deposited between the cells of tissues and organs, leads to various clinical conditions. Immunohistochemistry has allowed for better classification and understanding of the pathophysiology of amyloidosis. In the upper aerodigestive tract, amyloidosis is a rare condition occurring most frequently in the larynx. We present the case of a 42-year-old woman with complete nasal obstruction due to primary nasopharyngeal amyloidosis. This represents the first reported case of primary nasopharyngeal amyloidosis containing both the lambda and kappa immunoglobulin light chains. The clinical and radiologic findings, as well as the management of primary amyloidosis of the upper aerodigestive tract, will be discussed. A review of the literature pertaining to nasal and nasopharyngeal amyloidosis will be presented.

Adult↗
PubMed1979

Amyloidosis of the larynx.

Amyloidosis of the larynx is a rare disease, accounting for less than 1% of all benign laryngeal 'tumours'. Three cases of this type of lesion are reported--one of the vocal cord, one of the false vocal cord and one of the subglottis and trachea. In 2 of the patients the amyloidosis was localized, while the third was later found also to have an epipharyngeal solitary plasmacytoma with amyloid deposits and in addition amyloidosis of the nasal cavity. However, the amyloidosis in this patient may still be regarded as being localized, as the clinical examination and laboratory tests afforded no evidence of generalized disease. Amyloidosis of the larynx may be manifested as a localized tumour or as a diffuse infiltration. The symptoms and signs will, of course, depend on the site of the amyloid deposit. When the vocal cords are involved hoarseness may result, and this was the most prominent sign in the present cases. The treatment of laryngeal amyloidosis is primarily by endoscopic excision. Amyloid substance has specific staining properties. The Congo red reaction with a green birefringence in polarized light and Phorwhite BBU using fluorescence microscopy are regarded as the most reliable staining reactions. Electron microscopy has revealed a typical fibrillar structure of amyloid.

Aged↗
PubMed1997

Behçet's disease and amyloidosis. Review of the literature.

In this report, we present a patient with BD, amyloidosis and end-stage-renal-disease and discuss the literature on BD and amyloidosis. Forty-four patients with BD and amyloidosis are described in the literature. The type of amyloid fibrils were studied in 27 of this 44 patients and all were AA. The interval between the onset of first symptom of BD and the diagnosis of amyloidosis ranged from one to 27 years. This clinical observation and AA type amyloid fibrils in BD suggest that amyloidosis is secondary to inflammation. Behçet's disease should be considered in the differential diagnosis of AA amyloidosis.

Adult↗
PubMed2000

Histochemical and immunohistochemical differential diagnosis of amyloidosis--a brief illustrated essay and personal experience with Romhányi's method.

The histochemical and immunohistochemical differential diagnosis of amyloidosis in surgical pathology in a referral center is presented. Different forms of amyloidosis are considered e.g. systemic generalized amyloidosis: secondary (AA), primary (AL), senile, hemodialysis-associated, hereditary and organ (tissue)-limited (localized) amyloidosis: cerebral, dystrophic (age-related, so-called "senile"), endocrine-related, localized to tumours, focal (concentrated secretion), and isolated plasma cell (solitary plasmacytoma, B-cell) dyscrasia related amyloidosis. The amyloid deposits were identified and characterized histochemically by Congo red staining after performate pre-treatment at 20 degrees C for 1, 3, 5, 10, 15, 20 or 25 sec, and with oxidation induced proteolysis by trypsin digestion at 20 degrees C for 5, 10, or 30 sec, 1, 2, 3, 4, 5, 6 or 10 min and covered with gum-arabic according to Romhányi, and confirmed by streptavidin-biotin-complex/horseradish peroxidase immunohistochemical reactions. The "sensitivity" or "resistance" to pre-treatment of amyloid deposits depends on the type of amyloid, and the length of pre-treatment. Secondary (AA) amyloid is sensitive to KMnO4 oxidation, followed by trypsin digestion (for 1 min), and its green birefringence under polarized light disappears, while primary (AL) (for 1-5 min), senile (for 1-10 min), and most forms of organ (tissue)-limited (localized) amyloid (for 1-10 min) are resistant. Performate pre-treatment is followed by pronounced congophilia. Secondary (AA) is sensitive to performate pre-treatment (for 1 sec), while primary (AL) amyloid (for 1-20 sec), senile (for 1-25 sec), and most forms of organ (tissue)-limited (localized, isolated) amyloid deposits (for 1-25 sec) are resistant, and are constantly positively birefringent. Early identification and differentiation of amyloid deposits is important for the prognosis and for the choice of therapy. The authors conclude that the presented classical histochemical methods are useful as first line screens for the histological identification of amyloidosis.

Amyloid↗