[Clinico-functional aspects of amyloidosis of the liver (amyloidosis secondary to tuberculosis and other diseases; primary amyloidosis)].
Explore the source record for details and available documents.
Amyloidosis↗
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.
The long-term prognosis of AA and AL renal amyloidosis and the pathogenesis of chronic renal failure in renal amyloidosis.
Investigation of the long-term prognosis and pathogenesis of chronic renal failure in 225 cases of AA and AL renal amyloidosis (perireticular and perireticular + pericollagenous amyloidosis) yielded the following results: 1) The prognosis of both AA and AL amyloidosis is poor, and is worse than all other types of glomerulopathy with the exception of rapidly progressive glomerulonephritis. 2) The probability of maintaining renal function in AL amyloidosis is no lower than that in AA amyloidosis. 3) The prognosis of both AA and AL amyloidosis is significantly worse in cases in which the renal cortical interstitium exhibits fibrosis at the time of the biopsy than in those in which it is normal. 4) In AA and AL amyloidosis, as in various types of inflammatory glomerulopathy, the relative area of the renal cortical interstitium shows a significant positive correlation with the serum creatinine concentration and a significant negative correlation with the creatinine clearance. However, the extent of interstitial amyloid deposition does not correlate with the serum creatinine concentration. Deposition of amyloid in the renal cortical interstitium has no effect on renal excretory function. 5) The long-term prognosis of renal amyloidosis is related to the severity of the glomerular amyloidosis in as much as it is generally worse in Grades III to V than in Grades I and II. However, it must be borne in mind that the incidence of interstitial fibrosis, which is decisive for the long-term prognosis, increases with the severity of glomerular changes. 6) The long-term prognosis of renal amyloidosis is worse if acute renal failure or interstitial fibrosis is present at the time of the biopsy. Patients with both acute renal failure and interstitial fibrosis have the worst prognosis. 7) Isolated glomerular amyloidosis, even if there is severe vascular amyloidosis (vas afferns), does not lead to renal insufficiency or even to a rise in serum creatinine concentration. 8) The number of T lymphocytes in the tubular epithelium in AA and AL amyloidosis is significantly greater than normal, and the number of T lymphocytes, macrophages/monocytes, and fibroblasts/fibrocytes per unit area of interstitium is also significantly increased. 9) As far as the pathogenesis of renal cortical interstitial fibrosis in renal amyloidosis is concerned, it is proposed that, in some cases, this develops from the interstitial edema that is seen in biopsy specimens of patients with renal amyloidosis and acute renal failure.(ABSTRACT TRUNCATED AT 400 WORDS)
Adult↗
Perimembranous-type renal amyloidosis: a peculiar form of AL amyloidosis.
Six cases of perimembranous-type renal amyloidosis were reported. This type of renal amyloidosis was characterized by amyloid deposition predominantly involving the epithelial aspect of the glomerular capillary wall. Florid spicular arrangement was another representative feature. This type of amyloid deposition was found in 8% of autopsy cases of systemic amyloidosis. All cases were categorized as AL amyloidosis and developed the nephrotic syndrome irrespective of the amount of amyloid within the glomeruli. The results obtained suggest that perimembranous-type renal amyloidosis is a peculiar form of AL amyloidosis both in morphology and clinical manifestations. autopsy cases of systemic amyloidosis. All cases were categorized as AL amyloidosis and developed the nephrotic syndrome irrespective of the amount of amyloid within the glomeruli. The results obtained suggest that perimembranous-type renal amyloidosis is a peculiar form of AL amyloidosis both in morphology and clinical manifestations. autopsy cases of systemic amyloidosis. All cases were categorized as AL amyloidosis and developed the nephrotic syndrome irrespective of the amount of amyloid within the glomeruli. The results obtained suggest that perimembranous-type renal amyloidosis is a peculiar form of AL amyloidosis both in morphology and clinical manifestations.
Amyloid↗
Localized amyloidosis of the parotid gland: a case report and review of the localized amyloidosis of the head and neck.
BACKGROUND: Localized amyloidosis in the head and neck is a rare and benign process. METHODS: We present the first case report in the literature of localized amyloidosis of the parotid glands and also comprehensively review the literature regarding localized amyloidosis of the head and neck. RESULTS: Amyloidosis affecting the head and neck region is uncommon and is mostly in the form of localized amyloidosis. Larynx is the commonest site of involvement and accounts for 0.2% to 0.5% of benign laryngeal tumors. Laryngeal involvement could be either diffuse subepithelial deposition or discrete tumor nodules. Although localized amyloidosis occurs much more frequently in the oral cavity and pharynx, only seven cases of nasopharyngeal amyloidosis and eight cases of nasal septum amyloidosis have been reported. There is no documentation to suggest that localized amyloidosis can progress to systemic amyloidosis. Local surgical excision is the treatment of choice for laryngeal amyloidosis and laser excision is probably the best. CONCLUSION: While localized amyloidosis of the head and neck region is rare, it should be recognized, understood, evaluated, and properly treated.
Aged↗
Obstructive intramural coronary amyloidosis and myocardial ischemia are common in primary amyloidosis.
PURPOSE: The purpose of this study was to determine the prevalence of clinical syndromes and pathologic changes of myocardial ischemia due to obstructive intramural coronary amyloidosis among patients with primary amyloidosis and cardiac involvement. SUBJECTS AND METHODS: Medical records and pathologic specimens were reviewed from 96 patients with primary amyloidosis and cardiac involvement at autopsy or after cardiac transplantation during a 20-year period. Medical records were reviewed for patient demographic and clinical characteristics, including evidence for syndromes of myocardial ischemia. Pathologic specimens were examined for obstructive intramural coronary amyloidosis and microscopic changes of myocardial ischemia. RESULTS: Obstructive intramural coronary amyloidosis was present in 63 of 96 patients (66%). Microscopic changes of myocardial ischemia were more common in patients with obstructive intramural coronary amyloidosis (86%) than in those without (52%) (P <.001). In the 76 patients without coexistent severe epicardial coronary atherosclerosis, changes of myocardial ischemia were more common in those with obstructive intramural coronary amyloidosis (83%) than in those without (45%) (P <.001). In patients who had tissue available for review, none had obstruction of epicardial coronary arteries from amyloid. Syndromes of myocardial ischemia affected 16 patients (25%) with obstructive intramural coronary amyloidosis but only 2 patients (6%) without (P=.027). For 11% of the patients with obstructive intramural coronary amyloidosis, a syndrome of myocardial ischemia consisting of acute myocardial infarction or angina pectoris was the first manifestation of primary amyloidosis. CONCLUSION: Most patients with primary systemic amyloidosis and cardiac involvement have obstructive intramural coronary amyloidosis and associated microscopic changes of myocardial ischemia. Syndromes of myocardial ischemia may occur in these patients.
Adult↗
Senile systemic amyloidosis presenting with heart failure: a comparison with light chain-associated amyloidosis.
BACKGROUND: Small deposits of amyloid are often found in the hearts of elderly patients. However, extensive deposition of transthyretin-derived amyloid fibrils in the heart (senile systemic amyloidosis [SSA]) can cause heart failure. The clinical features of SSA that involve the heart are ill defined, and the condition may be overlooked as a cause of heart failure. We sought to better define the clinical, echocardiographic, and electrocardiographic features of cardiac involvement in SSA and to compare them with the findings in patients with light chain-associated (AL) amyloidosis that affects the heart. METHODS: Eighteen consecutive patients with SSA and heart failure evaluated at a tertiary referral center for the diagnosis and treatment of amyloidosis were compared with 18 randomly selected patients with AL amyloidosis that involved the heart. All patients underwent a complete clinical and biochemical evaluation. Echocardiograms and electrocardiograms were interpreted by blinded investigators. RESULTS: Patients with SSA were older than those with AL amyloidosis and were all male. Proteinuria (protein output of >1 g per 24 hours) was common in AL amyloidosis but was not present in SSA. Left ventricular wall thickness was greater in patients with SSA than those with AL amyloidosis, but despite thicker walls and older age, the severity of heart failure was less in the SSA group and the median survival was much longer (75 vs 11 months; P = .003). CONCLUSIONS: Senile systemic amyloidosis is a disorder of elderly men and is characterized by amyloidosis clinically limited to the heart. In contrast to the rapid progression of heart failure in AL amyloidosis, SSA results in slowly progressive heart failure. The difference in survival, despite evidence of more myocardial disease in the senile group, suggests that heart failure in AL amyloidosis may have a toxic component, possibly related to the circulating monoclonal light chain.
Adult↗
[Position of ocular amyloidosis among various forms of amyloidosis].
New data, concerning incidence, morphology, clinical manifestations of eye amyloidosis are obtained following its study using modern verification methods. Eye amyloidosis is represented either by its local forms or is associated with a generalized amyloidosis. Local eye amyloidosis predominated and may be isolated and combined. Isolated amyloidosis is represented by two variants: with an involvement of the anterior part of the eye in the form of pseudoexfoliative amyloidosis (PEA) and involvement of the posterior part of the eye with the development of senile macular degeneration (SMD). Local amyloidosis may be associated with senile cerebral amyloidosis, insular amyloidosis of pancreas and both. Predominant involvement of the eye vessels and extraocular structures is an important feature of the ocular amyloidosis as a manifestation of generalized forms. Vitreous body is involved mainly in FAP. New clinico-morpho-pathogenetic classification is suggested.
Adult↗
Tumor necrosis factor alpha, its soluble receptor I, and -308 gene promoter polymorphism in patients with rheumatoid arthritis with or without amyloidosis: implications for the pathogenesis of nephropathy and anemia of chronic disease in reactive amyloidosis.
OBJECTIVE: To study tumor necrosis factor alpha (TNFalpha) -308 gene promoter polymorphism and circulating levels of TNFalpha and soluble TNF receptor type I (sTNFRI) in rheumatoid arthritis (RA) patients with and without reactive amyloidosis. METHODS: In a retrospective study, we examined 55 RA patients with biopsy-proven reactive amyloidosis and 55 control RA patients without amyloidosis (matched for age, sex, rheumatoid factor titer, and RA duration). Inflammatory activity was assessed by measuring the erythrocyte sedimentation rate and C-reactive protein level. TNFalpha gene promoter polymorphism was studied using polymerase chain reaction-restriction fragment length polymorphism assay. Cytokine and receptor levels were measured by enzyme-linked immunoassays. RESULTS: Patients with RA and amyloidosis had significantly higher TNFalpha and sTNFRI levels than did the control RA patients. The increased circulating levels of TNFalpha correlated with interleukin-18 levels, but not with the serum amyloid A protein levels or with TNFalpha -308 gene promoter polymorphism (reported to be associated with high TNFalpha levels and certain disease susceptibilities). In the patients with RA and amyloidosis, those with anemia had significantly higher TNFalpha and sTNFRI levels than did those without anemia, and circulating TNFalpha and sTNFRI levels correlated negatively with hemoglobin concentrations. In the patients with RA and amyloidosis, those with nephropathy had significantly higher TNFalpha and sTNFRI levels than did those without nephropathy; in patients with isolated proteinuria (but no creatinine elevation) the TNFalpha level was also significantly increased, indicating that the TNFalpha elevation was not merely a consequence of impaired renal function. CONCLUSION: This study shows that circulating levels of TNFalpha and sTNFRI are significantly increased in RA patients with amyloidosis as compared with control RA patients without amyloidosis and that the increased levels may be implicated in the pathogenesis of certain disease manifestations, including anemia of chronic disease and renal pathology in reactive amyloidosis.
Adult↗
Amyloid in localized cutaneous amyloidosis: immunofluorescence studies with anti-keratin antiserum especially concerning the difference between systemic and localized cutaneous amyloidosis.
Amyloid of localized cutaneous amyloidosis and systemic amyloidosis were subjected to study with an indirect immunofluorescence technique using anti-keratin antiserum. Anti-keratin antiserum was prepared ad modum Sun & Green. Amyloid of localized cutaneous amyloidosis was positively stained for the antiserum, whereas amyloid of systemic amyloidosis (primary and multiple myeloma-associated) was negative. There was no difference between primary localized cutaneous amyloidosis (lichen amyloidosus and macular amyloidosis) and secondary localized cutaneous amyloidosis (amyloidosis associated with skin tumor). These results indicate that amyloid of localized cutaneous amyloidosis contains components derived from epidermal fibrous protein, probably tonofilaments of keratinocytes.
Amyloid↗
Mouse senile amyloidosis. ASSAM amyloidosis in mice presents universally as a systemic age-associated amyloidosis.
Amyloid deposition in 11 inbred strains of mice (A/J, SJL/J, DDD, C57BL/6J, B10.BR, C57BL/10, B10A/SgSn, C3H/HeMs, B10A(5R), DBA/2 and C57BL/6Cr5/c) was studied using the peroxidase antiperoxidase (PAP) method and antisera against ASSAM and murine protein AA. Among the 170 mice examined, in 77 (45.3%) from the nine strains other than C3H/HeMs and DBA/2, there was evidence of spontaneous amyloid deposits in routine histological sections. Immunohistochemical studies using 54 mice with amyloid deposition, demonstrated ASSAM deposition in 45 mice (83.3%) in all nine strains, although the incidence and intensity of the deposition differed somewhat between strains. SJL/J and A/J had ASSAM deposits from the age of 8 months and the incidence increased with advancing age. In the other seven strains, ASSAM was first deposited at an older age than in the SJL/J and A/J strains. In A J, C57BL/6J, C57BL/10, B10.BR, B10A(5R) and C57BL/6Cr5/c, protein AA often coexisted with ASSAM. The distribution pattern of the ASSAM deposits was similar to that observed among the SAM strains. Thus, ASSAM is an ubiquitously distributed senile amyloid protein in the mouse. Determination of the molecular type of apoA-II, a serum precursor of ASSAM, among all 11 strains using the polymerase chain reaction (PCR) revealed the SAM-P/1 type apoA-II variant in SJL/J and A/J strains with a high susceptibility to ASSAM deposition. We concluded from this study that amino acid substitution in precursor apoA-II may be responsible for the early onset and severe amyloid deposition in the mouse.
Aging↗
Skin in amyloidosis. (A case report on primary systemic amyloidosis with skin involvement and a review of skin manifestations of amyloidosis).
Explore the source record for details and available documents.
Aged↗
[Amyloidosis in allergic processes: renal amyloidosis (reversible in appearance) and urticaria. Renal amyloidosis and asthma].
Explore the source record for details and available documents.
Adult↗
Casein-induced amyloidosis in the nude mouse. I. Acceleration of amyloidosis in recipients of spleen grafts from casein-sensitized donor mice. II. Transfer of amyloidosis by spleen cells.
Explore the source record for details and available documents.
Amyloid↗
[Electromicroscopic studies of vascular changes in amyloidosis--comparison of lichen amyloidosis and systemic amyloidosis].
Explore the source record for details and available documents.
Amyloidosis↗
RET mutation screening in familial cutaneous lichen amyloidosis and in skin amyloidosis associated with multiple endocrine neoplasia.
In several families, multiple endocrine neoplasia type 2A (MEN 2A) has been found in association with cutaneous lichen amyloidosis. It has been debated, however, whether the skin amyloidosis found in MEN 2A families, localized exclusively in the interscapular area, represents the same anomaly as that found in autosomal dominant familial cutaneous lichen amyloidosis, which is more generalized. We screened two MEN 2A families with associated skin amyloidosis for germline mutations in the RET gene responsible for the MEN 2A cancer syndrome, and found the same mutation characteristic of MEN 2A in both families. We also screened probands from three pedigrees with familial cutaneous lichen amyloidosis for RET mutations. In none of the RET coding and flanking intronic sequences was a mutation detected. This most probably indicates that skin amyloidosis found in some MEN 2A families and familial cutaneous lichen amyloidosis are different conditions. Consequently, patients with apparent familial cutaneous lichen amyloidosis do not appear to be at risk for MEN 2A.
Amyloidosis↗
Histopathological and immunohistochemical study of amyloidosis cutis nodularis atrophicans--comparison with systemic amyloidosis.
Three cases of amyloidosis cutis nodularis atrophicans (ACNA) were investigated histologically and immunohistochemically to determine the nature and origin of the deposited amyloid. A pulmonary lesion from a case of nodular pulmonary amyloidosis, and cutaneous lesions from three cases of primary systemic amyloidosis, two cases of secondary systemic amyloidosis and three cases of secondary cutaneous amyloidosis following basal cell epithelioma were also examined for comparison. Histology showed infiltration of numerous plasma cells adjacent to amyloid deposits in ACNA and nodular pulmonary amyloidosis, but not in systemic amyloidosis. Immunohistochemically, the cytoplasm of the plasma cells was stained with anti-immunoglobulin light chain or anti-Bence-Jones protein antisera or both, and amyloid material stained with anti-AL antiserum in ACNA and nodular pulmonary amyloidosis. These results suggest that, in ACNA, the plasma cells may produce and secrete immunoglobulin light chains or Bence-Jones protein or both, which undergo proteolysis to protein AL or amyloid fibril proteins which have the same immunoglobulin determinants as protein AL. The product is then deposited locally to form nodules in the dermis.
Adult↗
Amyloidosis of pancreatic islets in primary amyloidosis (AL type).
Seven cases of primary amyloidosis (AL-type) were studied immunocytochemically for the possible involvement of pancreatic islets. The two cases with extensive organ involvement by AL-amyloidosis revealed amyloid deposits in pancreatic islets by routine HE and Congo red staining, which were positive for amyloid p and amyloid a, but were only focally positive for light chains kappa and lambda. Positive staining for amyloid p and amyloid a was also noted in the scattered pancreatic acinar tissues, and this positive staining was not specifically located in pancreatic islets as seen in type 2 diabetes mellitus. It is concluded that amyloid deposits in pancreatic islets occur in systemic AL-amyloidosis by a different mechanism from type 2 diabetes. Islet amyloidosis in AL-amyloidosis appears to deposit via circulation, depositing in both pancreatic islets and acinar tissue through blood vessels. In type 2 diabetes, beta islet cells die by cytotoxic effects of smaller amylin (islet amyloid polypeptide, IAPP) aggregates, and the interstitial space created by the necrotic beta cells is replaced by larger IAPP aggregates, to form complex, polymerized islet amyloid. In AL-amyloidosis, the amount of amyloid and light chain deposits in pancreatic islets is much less than that of the other organs and appears to have no connection to type 2 diabetes because the patients did not present diabetes or hyperglycemia. However, considerable islet amyloidosis can be seen in severe AL-type amyloidosis.
Aged↗
[Clinical manifestations of AL-amyloidosis and some other types of amyloidosis].
Amyloidosis is the term for specific pathological peptide deposits in various tissues. Amyloid substances may be the manifestation of the following nosological units: AL-amyloidosis, AA-amyloidosis, ATTR-amyloidosis, beta2-microglobulin amyloidosis and possibly othr familiar forms of amyloidosis. The most frequent symptoms of amyloidosis are: 1. proteinuria with nephrotic syndrome, 2. cardiac failure with restrictive cardiomyopathy, 3. unexplicable hepatomegaly, 4. idiopathic peripheral polyneuropathy, 5. haemorrhagic manifestations and symptoms of increased fragility of the capillaries while the number of thrombocytes is normal, 6. periorbital haematomas and 7. macroglossia. Diagnostic and therapeutic procedures differ according to the type of amyloidosis and are analyzed in detail in the text.
Amyloidosis↗