Original Article
Natural History and Outcome in Systemic AA Amyloidosis
N Engl J Med 2007; 356:2361-2371June 7, 2007
- Abstract
Background
Deposition of amyloid fibrils derived from circulating acute-phase reactant serum amyloid A protein (SAA) causes systemic AA amyloidosis, a serious complication of many chronic inflammatory disorders. Little is known about the natural history of AA amyloidosis or its response to treatment.
Methods
We evaluated clinical features, organ function, and survival among 374 patients with AA amyloidosis who were followed for a median of 86 months. The SAA concentration was measured serially, and the amyloid burden was estimated with the use of whole-body serum amyloid P component scintigraphy. Therapy for inflammatory diseases was administered to suppress the production of SAA.
Results
Median survival after diagnosis was 133 months; renal dysfunction was the predominant disease manifestation. Mortality, amyloid burden, and renal prognosis all significantly correlated with the SAA concentration during follow-up. The risk of death was 17.7 times as high among patients with SAA concentrations in the highest eighth, or octile, (≥155 mg per liter) as among those with concentrations in the lowest octile (<4 mg per liter); and the risk of death was four times as high in the next-to-lowest octile (4 to 9 mg per liter). The median SAA concentration during follow-up was 6 mg per liter in patients in whom renal function improved and 28 mg per liter in those in whom it deteriorated (P<0.001). Amyloid deposits regressed in 60% of patients who had a median SAA concentration of less than 10 mg per liter, and survival among these patients was superior to survival among those in whom amyloid deposits did not regress (P=0.04).
Conclusions
The effects of renal dysfunction dominate the course of AA amyloidosis, which is associated with a relatively favorable outcome in patients with SAA concentrations that remain in the low-normal range (<4 mg per liter).
Media in This Article
Figure 1
Changes in Amyloid Burden from Baseline to Most Recent Follow-up in 221 Patients and Changes in Amyloid Burden and Renal Function during Follow-up in 178 Patients with a Baseline Creatinine Clearance of More Than 20 ml per Minute.Figure 2
Regression of AA Amyloid Deposits in a Patient with Familial Mediterranean Fever.Article Activity
- Article
Reactive systemic AA amyloidosis can complicate chronic inflammatory disorders that are associated with a sustained acute-phase response. AA amyloid fibrils are derived from the acute-phase reactant serum amyloid A protein (SAA) protein through a process of cleavage, misfolding, and aggregation into a highly ordered abnormal β-sheet conformation.1 Amyloid fibrils associate with other moieties, including glycosaminoglycans and serum amyloid P component (SAP), forming deposits that disrupt the structure and function of tissues and organs.2 SAA is an apolipoprotein constituent of high-density lipoprotein3 that is synthesized by hepatocytes under the transcriptional regulation of proinflammatory cytokines.4 The median plasma concentration of SAA in healthy persons is 3 mg per liter, but the concentration can increase to more than 2000 mg per liter during the acute-phase response.5 Sustained overproduction of SAA is a prerequisite for the development of AA amyloidosis, although for reasons that are not known, amyloidosis occurs only in a small proportion of patients with chronic inflammatory disorders.6,7
Few systematic clinical studies of AA amyloidosis have been reported, and recent data on its clinical features, natural history, and long-term outcome are scanty. We report the clinical features and course in 374 patients with AA amyloidosis who were followed at a single national center during a period of 15 years. In addition to conventional clinical follow-up assessment, the amyloid burden was estimated annually with the use of SAP scintigraphy, and the plasma concentration of the AA amyloid precursor protein was monitored by monthly measurement of SAA.
Methods
Patients
We included in this study all 374 patients with systemic AA amyloidosis who were referred to the U.K. National Amyloidosis Centre during a period of 15 years, to August 2005. The diagnosis of AA amyloidosis was confirmed in 320 patients by immunohistochemical testing and in 54 patients by noninvasive means. Inclusion criteria were amyloid deposition on SAP scintigraphy; evidence of an overt chronic inflammatory disease, no mutations in the genes encoding transthyretin, the fibrinogen A α-chain, apolipoprotein A-I, apolipoprotein A-II, and lysozyme (to rule out hereditary forms of amyloidosis8,9); negative serum free light-chain assay; negative monoclonal immunoglobulin screening, including the use of serum and urine immunofixation (to rule out monoclonal light-chain [AL] amyloidosis10,11); and the absence of neuropathy and of cardiac amyloidosis, both of which are uncommon in the AA type of amyloidosis. A biopsy was performed if any of these criteria were not met. The study was approved by the ethics committee of the Royal Free Hospital, and all patients provided written informed consent.
Congo Red Staining and Immunohistochemical Testing
The Congo red method12 was used to detect amyloid in tissue sections. Amyloid was identified as the AA type on immunohistochemical testing with the use of monoclonal antibodies specific to SAA (Euro-Diagnostica).13
Clinical Assessment
Patients underwent an initial clinical assessment and annual review at our center. Blood samples were scheduled to be obtained monthly to determine the SAA concentration, and a mean of 10.6 samples per patient per year were obtained. Quantitative estimation of the distribution and extent of visceral amyloid deposits was performed with the use of whole-body 123I-labeled SAP scintigraphy.14 Blinded assessments of amyloid deposits were performed at baseline and annually by an investigator with expertise in the interpretation of SAP scans. The whole-body amyloid burden was classified as 0 when there was no abnormal localization of the tracer; as small when uptake in one or more organs was discernible but the intensity of the blood-pool background signal remained normal; as moderate when abnormal uptake in one or more organs was sufficiently intense for the blood-pool background signal to be partially lost when the gray scale was normalized to encompass the target-organ signal; and as large when the blood-pool background was lost with adjustment of the gray scale to encompass the target-organ uptake.
Regression of amyloid was defined as a reduction in tracer uptake in affected organs or an increase in the blood-pool background signal, or both; an accumulation of amyloid was defined as an increase in tracer uptake in affected organs, an abnormal tracer uptake in a previously unaffected organ, or a decrease in the blood-pool background signal; and a stable amyloid burden was defined as unchanged tracer localization.15,16 Clinically important organ involvement and changes in organ function were defined according to international consensus criteria.17 Deteriorating kidney function was categorized as either the onset of end-stage renal failure, defined by a requirement for long-term dialysis, or as an increase of 25% or more in the serum creatinine concentration or a decrease of 25% or more in creatinine clearance measured by 24-hour urine collection. In patients in whom the serum creatinine concentration or creatinine clearance did not deteriorate by 25% or more, renal function was deemed to have deteriorated if urinary protein excretion had increased by 50% or more and by more than 1 g per day (24 hours). Renal function was categorized as improved if the serum creatinine concentration or creatinine clearance improved by 25% or more, or if these values did not worsen if 24-hour urinary protein excretion decreased by more than 50% and by more than 0.5 g. Patients whose condition met none of these criteria were classified as having stable kidney function. SAA was assayed with the use of latex-enhanced immunonephelometry (BN II analyzer, Dade Behring) with the use of the World Health Organization's International Reference Standard.5,18,19
Treatment
Treatment was undertaken with the objective of suppressing underlying inflammatory disease (Table 1Table 1
Underlying Disorders and Treatment in 374 Patients with AA Amyloidosis.) and reducing the SAA concentration as much as possible. Patients also received supportive care, including, when required, renal-replacement therapy.Statistical Analysis
Survival and time from the diagnosis of amyloidosis to end-stage renal failure (dependence on dialysis) were estimated in Kaplan–Meier analyses. Changes in renal function were analyzed in the subgroup of 257 patients who had a creatinine clearance greater than 20 ml per minute (0.3 ml per second) at baseline — that is, those in whom progression to end-stage renal failure was not deemed to be inevitable. Relationships of a variety of factors with survival and with the development of end-stage renal failure were examined with the use of Cox regression analysis. Potential covariates were categorized as factors that were fixed at the baseline assessment (age, sex, race or ethnic group, calendar year when amyloidosis was diagnosed, initial amyloid burden and renal function, evidence of hepatic amyloid, underlying disease, and duration of inflammatory disease before diagnosis) or as factors that could vary between annual follow-up assessments. Race or ethnic group was self-reported. Factors that could vary (changes in amyloid burden, serum albumin concentration, median SAA concentration, creatinine concentration, creatinine clearance, proteinuria, and the development of end-stage renal failure) were incorporated into the Cox model as time-dependent covariates.
The data set that was extracted consisted of yearly summaries (medians) of SAA values for each patient (e.g., the median SAA value for year 1 was calculated as the median value of all the measurements obtained during the first year of follow-up), and these values were updated in the Cox model at yearly intervals. Changes in the amyloid burden were assessed annually and updated in the model at each annual follow-up assessment, along with renal-function status and serum albumin concentration; end-stage renal failure was incorporated in the model as a binary variable with a value of 0 before the onset of end-stage renal failure and of 1 thereafter. Continuous measurements were categorized into octiles, and unadjusted relative risks were examined to assess whether it was appropriate to simplify the models by including each measurement in the model as a continuous covariate (possibly after log transformation). Variables that were significant in the univariate models (P<0.01) were analyzed in a multivariate regression model with the use of a backward-selection procedure and SAS software, version 9.1.
Results
Baseline Characteristics
Baseline characteristics of the 374 patients are listed in Table 2Table 2
Characteristics of Patients at Baseline.. The most frequent underlying disorder was inflammatory arthritis (Table 1). Rare causes of AA amyloidosis included vasculitis, sickle cell anemia, malignant disease, epidermolysis bullosa, and cyclic neutropenia. For 23 patients, the precise nature of the inflammatory disorder could not be established, despite extensive investigation. The median duration of symptomatic inflammatory disease before the diagnosis of amyloidosis was 17 years, and there were no significant differences in latency among the various underlying disorders.The predominant feature of amyloidosis at diagnosis was renal dysfunction; in 97% of patients, more than 500 mg of protein per day was excreted or the serum creatinine concentration was more than 1.5 mg per deciliter (133 μmol per liter), or both; at diagnosis, 41 patients (11%) had end-stage renal failure. Median protein excretion among the 333 patients not requiring dialysis was 3.9 g per day (interquartile range, 1.9 to 6.3); of these patients, 12% had urinary protein excretion of more than 10 g per day, and 2% had urinary protein excretion of more than 20 g per day; the serum albumin concentration was less than 3.5 g per deciliter in 184 patients (55%). Among those not requiring dialysis, the median serum creatinine concentration at baseline was 1.2 mg per deciliter (interquartile range, 0.8 to 2.4) (106 μmol per liter [interquartile range, 71 to 212]); the serum creatinine concentration was less than 3.0 mg per deciliter (265 μmol per liter) at diagnosis in 75% of patients.
Hepatomegaly was present on examination at baseline in 35 patients (9%), but hepatic amyloid deposits were evident on SAP scintigraphy in 85 patients (23%). Serum alkaline phosphatase concentrations greater than 1.5 times the upper limit of the normal range (which varies according to age, sex, and method of analysis), a value that is widely regarded as suggesting liver involvement in amyloidosis,17 were present in 21 patients with hepatic amyloidosis but also in 25 patients who had normal liver signal on SAP scintigraphy. The median SAA concentration in these patients was 51 mg per liter, a finding that is consistent with increased production of alkaline phosphatase as an acute-phase reactant. No patient had jaundice, elevated serum aminotransferase concentrations, or hepatic synthetic dysfunction.
Cardiac failure attributable to amyloidosis was present in only 1 patient, and findings consistent with cardiac infiltration were present in only 2 of 224 patients who underwent echocardiography. No patient had symptomatic autonomic neuropathy, and although adrenal amyloid deposits were evident on SAP scintigraphy in 41% of the patients, only five required long-term adrenocorticoid replacement therapy.
SAP scintigraphy was diagnostic of amyloidosis at baseline in all but four patients, each of whom had nonfunctioning atrophic kidneys and had undergone splenectomy. In 370 patients (99%), the scans showed striking splenic amyloid deposits, and in 331 patients (89%), the scans also showed renal or adrenal deposits, or both.
Clinical Course and Outcome
The cohort was followed for a median of 86 months (range, 2 to 447) after diagnosis, representing 2673 person-years. Forty-seven patients (13%) were lost to follow-up, and data for them were censored as of the date of the last contact. A total of 221 patients underwent serial SAP scintigraphy; in 27 (12%) the amyloid burden increased, in 107 (48%) it was unchanged, and in 87 (39%) there was evidence of regression from baseline to the most recent follow-up assessment (Figure 1Figure 1
Changes in Amyloid Burden from Baseline to Most Recent Follow-up in 221 Patients and Changes in Amyloid Burden and Renal Function during Follow-up in 178 Patients with a Baseline Creatinine Clearance of More Than 20 ml per Minute. and Figure 2Figure 2Regression of AA Amyloid Deposits in a Patient with Familial Mediterranean Fever.). SAA values were significantly lower in patients in whom amyloid deposits regressed (median, 7 mg per liter) than in those in whom the amyloid burden increased (median, 54 mg per liter) (P<0.001).A total of 163 patients (44%) died, and the median survival from diagnosis was 133 months (95% confidence interval [CI], 100 to 153) in the Kaplan–Meier analysis. The median SAA concentration during each year of follow-up was strongly associated with survival (Table 3Table 3
Unadjusted Relative Risk of Death Associated with the Most Recent Median Annual SAA Concentration during Follow-up.); the relative risk of death among patients with an SAA concentration of less than 4 mg per liter (the lowest octile) was almost 18 times lower than among patients with an SAA concentration of 155 mg per liter or greater (the highest octile). Even among those in the second-lowest octile, the very modest elevation in the SAA concentration of 4 to 9 mg per liter, which is widely cited as within the normal reference range, was associated with a risk of death that was increased by a factor of 4, as compared with those with SAA concentrations in the lowest octile.Other factors associated with increased mortality were older age (relative risk of death, 1.53 for each additional decade of age [95% CI, 1.34 to 1.74]; P<0.001) and end-stage renal failure (relative risk, 2.97 [95% CI, 2.10 to 4.21]; P<0.001) (Table 4Table 4
Factors Significantly Associated with the Risk of Death or Progression to End-Stage Renal Failure (Cox Regression Models).). In contrast, underlying periodic fever syndromes and evidence of regression of amyloid on serial SAP scintigraphy were both associated with reduced mortality (relative risk of death, 0.36 [95% CI, 0.14 to 0.88; P=0.03] and 0.13 [95% CI, 0.02 to 0.94; P=0.04], respectively) (Table 4).Among the 257 patients who had a creatinine clearance greater than 20 ml per minute at baseline, 59 (23%) had progression to end-stage renal failure; the estimated median time to end-stage renal failure from diagnosis was 256 months in the Kaplan–Meier analysis. The relative risk of end-stage renal failure was 1.24 (95% CI, 1.08 to 1.43; P=0.002) for each doubling of the SAA concentration. Among 178 patients for whom at least one assessment during follow-up was available, renal function improved in 54 patients and deteriorated in 86 patients, and improvement was associated with median SAA values of 6 mg per liter and 28 mg per liter, respectively (P<0.001 by the Kruskal–Wallis test) (Figure 1). Among the 92 patients in whom values for creatinine clearance remained stable or improved, the nephrotic syndrome abated in 33 patients after a median of 29 months, as defined by the disappearance of edema, a decrease in urinary protein excretion to less than 3 g per day, and an increase in the serum albumin concentration to 3.5 g per deciliter or more.
Cox regression analyses (Table 4) indicated that the relative risk of progression to end-stage renal failure was four times as high among patients who had underlying Crohn's disease or chronic sepsis as among those who did not (P=0.01 and P=0.006, respectively) and two times as high among patients who had hepatic amyloid deposits at baseline as among those who did not (P=0.04). The relative risk of progression to end-stage renal failure was also increased among patients whose renal function was relatively worse at baseline, with an increase by a factor of 5 for each doubling of the baseline serum creatinine concentration (P<0.001).
Five patients had a very rapid and striking relapse of proteinuric renal dysfunction when there was a flare of inflammatory disease activity during follow-up. For example, the amyloid-related nephrotic syndrome resolved gradually over a period of 4 years in a patient whose underlying rheumatoid arthritis was in sustained complete remission, yet when an intense acute-phase reaction associated with community-acquired pneumonia developed in this patient, the nephrotic syndrome recurred within 2 weeks. Her renal function normalized again during the ensuing 2 years.
Discussion
This study involving patients with AA amyloidosis included specific quantitative measurements of the whole-body amyloid burden on SAP scintigraphy and the circulating AA amyloid fibril precursor SAA. Observations that challenge the still widespread perception of amyloidosis as an inexorably progressive disease include the demonstration that AA amyloid deposits often regress and that survival is prolonged in patients in whom the circulating SAA concentration remains at low values.
Although the spleen, adrenal glands, liver, and gut are frequent sites of AA amyloid deposition, renal involvement dominated the clinical course in the patients in this study. Evidence of amyloid cardiomyopathy and autonomic neuropathy were extremely rare, as compared with previously reported series.20,21 None of the patients had clinically significant liver amyloidosis; furthermore, nearly one third of the patients with an elevated serum alkaline phosphatase concentration, which has been suggested as a marker of hepatic amyloid by an international consensus panel,17 had no evidence of liver deposits on SAP scintigraphy. The features of amyloidosis in terms of the duration of underlying disease, clinical presentation, distribution of amyloid deposits, and outcome were similar in patients with different types of underlying inflammatory disorders, with the exception of a worse renal outcome in patients with chronic sepsis or Crohn's disease. It is possible that the high frequency of surgical intervention and administration of immunosuppressive drugs contributed to renal failure in patients with Crohn's disease.
Factors associated with a poor prognosis included older age, a reduced serum albumin concentration, end-stage renal failure at baseline, and the degree by which the SAA concentration was elevated during follow-up. Increased production of SAA was the most powerful risk factor for end-stage renal failure and death, but it is also one that may be ameliorated through antiinflammatory treatment.
Despite the high correlations among SAA production, amyloid burden, and renal function overall within the cohort, the association between the median SAA concentration and the status of the amyloid deposits did differ among individual patients (Figure 1). Thus, although amyloid deposits regressed in about 60% of patients whose median SAA concentration was less than 10 mg per liter, the deposits were stable in the remainder. Similarly, although the amyloid deposits progressed in all patients whose median SAA concentration was more than 120 mg per liter, deposits among individual patients with moderately elevated SAA concentrations were stable, regressed, or progressed. The efficiency with which SAA is converted into amyloid or the rate at which amyloid deposits are turned over within the tissues, or both, may differ from patient to patient, although neither mechanism has been elucidated.
There were also differences between individual patients in the relationship between amyloid burden and renal function. Renal function improved in 17 patients in whom the amyloid burden was merely stable, and it deteriorated in 15 patients in whom amyloid deposits regressed. The basis for renal recovery in association with a stable amyloid burden and a low SAA concentration is unknown. However, progressive kidney dysfunction in patients in whom the amyloid deposits regressed was undoubtedly influenced by additional renal insults, including drugs, sepsis, hypovolemia, and hypertension, as well as by the extent of irreversible renal damage occurring before diagnosis. Discrepancies between the course of the amyloid deposits and the direction of change in organ function are salient reminders that the molecular mechanisms of tissue damage in amyloidosis actually remain little understood.
In contrast to the improvement in amyloid-associated renal dysfunction after successful antiinflammatory therapy that typically took months to years, the relapse of renal dysfunction after renewed inflammatory disease activity could be remarkably rapid. This finding probably reflects the conversion of abundant SAA into its fibrillar form on a template of residual amyloid deposits. This finding is reminiscent of the long-recognized phenomenon of the “amyloid-enhancing factor” that has been observed in experimentally induced murine AA amyloidosis, in which substantial amyloid deposits can develop in less than 24 hours in mice injected with ex vivo amyloid material and subsequently given an inflammatory stimulus.22,23
Treatment of AA amyloidosis depends on control of the underlying inflammatory disorder. Successful pharmacologic approaches in our patients ranged from nonspecific immunosuppression for those with inflammatory arthritis treated with chlorambucil24 to highly specific inhibition of interleukin-1 for those with the Muckle–Wells syndrome (an autosomal dominant fever syndrome characterized by urticaria, progressive perceptive deafness, and amyloidosis).25 Surgical treatments included excision of solitary cytokine-secreting Castleman's tumors (angiofollicular lymph-node hyperplasia)26 and amputation of osteomyelitic limbs. Surprisingly, 23 patients (6%) who presented with AA amyloidosis had clinically covert inflammatory disease that could not be characterized. The majority of these patients had been presumed by their referring physicians to have primary AL amyloidosis, yet on immunohistochemical testing, we confirmed AA amyloid in all of them. Antiinflammatory treatment must be empirical in such patients but should be guided, we believe, as in all patients with AA amyloidosis, by frequent measurement of SAA concentrations.27
In conclusion, AA amyloidosis usually presents with proteinuric renal dysfunction, for which patients with chronic inflammatory disorders should be evaluated routinely. The period of latency between the onset of inflammation and clinical presentation with AA amyloidosis appears to vary and is often prolonged, but the progression of amyloid can be rapid. In the present study, decreased production of SAA was associated with a favorable renal outcome, stabilization or regression of amyloid deposits, and prolonged survival.
Supported in part by grants from the U.K. Medical Research Council (G7900510, to Dr. Hawkins) and the National Health Service. Dade Behring provided the BN II analyzer and SAA assay kits.
Dr. Lachmann reports receiving consulting fees from Neurochem and Genzyme, and Dr. Hawkins, consulting fees from Domantis. No other potential conflict of interest relevant to this article was reported.
We thank our many colleagues for referring and caring for the patients; S. Madhoo, P. Spencer-Gittens, and D. Gopaul for their care of the patients at the National Amyloidosis Centre; and M. Pepys at the National Amyloidosis Centre for his scientific support, review of the manuscript, and establishment of the National Amyloidosis Centre.
Source Information
From the National Amyloidosis Centre and Centre for Amyloidosis and Acute Phase Proteins, Department of Medicine (H.J.L., H.J.B.G., J.A.G., J.R.G., J.D.G., P.N.H.), and the Department of Primary Care and Population Sciences (C.A.S.), Royal Free and University College Medical School, London.
- References
References
1
Merlini G ,Bellotti V . Molecular mechanisms of amyloidosis. N Engl J Med 2003;349:583-596
Full Text | Web of Science | Medline2
Pepys MB . Amyloidosis. Annu Rev Med 2006;57:223-241
CrossRef | Web of Science | Medline3
Parmelee DC ,Titani K ,Ericsson LH ,Eriksen N ,Benditt EP ,Walsh KA . Amino acid sequence of amyloid-related apoprotein (apoSAA1) from human high density lipoprotein. Biochemistry 1982;21:3298-3303
CrossRef | Web of Science | Medline4
Urieli-Shoval S ,Linke RP ,Matzner Y . Expression and function of serum amyloid A, a major acute-phase protein, in normal and disease states. Curr Opin Hematol 2000;7:64-69
CrossRef | Web of Science | Medline5
Ledue TB ,Weiner DL ,Sipe JD ,Poulin SE ,Collins MF ,Rifai N . Analytical evaluation of particle-enhanced immunonephelometric assays for C-reactive protein, serum amyloid A and mannose-binding protein in human serum. Ann Clin Biochem 1998;35:745-753
Web of Science | Medline6
Laiho K ,Tiitinen S ,Kaarela K ,Helin H ,Isomaki H . Secondary amyloidosis has decreased in patients with inflammatory joint disease in Finland. Clin Rheumatol 1999;18:122-123
CrossRef | Web of Science | Medline7
Singh G ,Kumari N ,Aggarwal A ,Krishnani N ,Misra R . Prevalence of subclinical amyloidosis in ankylosing spondylitis. J Rheumatol 2007;34:371-373
Web of Science | Medline8
Lachmann HJ ,Booth DR ,Booth SE , et al. Misdiagnosis of hereditary amyloidosis as AL (primary) amyloidosis. N Engl J Med 2002;346:1786-1791
Full Text | Web of Science | Medline9
Benson MD . Ostertag revisited: the inherited systemic amyloidoses without neuropathy. Amyloid 2005;12:75-87
CrossRef | Web of Science | Medline10
Lachmann HJ ,Gallimore R ,Gillmore JD , et al. Outcome in systemic AL amyloidosis in relation to changes in concentration of circulating free immunoglobulin light chains following chemotherapy. Br J Haematol 2003;122:78-84
CrossRef | Web of Science | Medline11
Rajkumar SV ,Dispenzieri A ,Kyle RA . Monoclonal gammopathy of undetermined significance, Waldenstrom macroglobulinemia, AL amyloidosis, and related plasma cell disorders: diagnosis and treatment. Mayo Clin Proc 2006;81:693-703[Erratum, Mayo Clin Proc 2006;81:1509.]
CrossRef | Web of Science | Medline12
Puchtler H ,Sweat F ,Levine M . On the binding of Congo red by amyloid. J Histochem Cytochem 1962;10:355-364
CrossRef | Web of Science13
Hazenberg BPC, Grond J, van den Top D, Bijzet J, Limburg PC, van Rijswijk MH. Immunohistochemical detection of amyloid AA in formaline-fixed paraffin-embedded rectal biopsies with the monoclonal anti-human SAA antibody Reu.86.2. In: Natvig JB, Forre O, Husby G, et al., eds. Amyloid and amyloidosis 1990. Dordrecht, the Netherlands: Kluwer Academic, 1991:809-12.
14
Hawkins PN ,Lavender JP ,Pepys MB . Evaluation of systemic amyloidosis by scintigraphy with 123I-labeled serum amyloid P component. N Engl J Med 1990;323:508-513
Full Text | Web of Science | Medline15
Hawkins PN ,Richardson S ,MacSweeney JE , et al. Scintigraphic quantification and serial monitoring of human visceral amyloid deposits provide evidence for turnover and regression. Q J Med 1993;86:365-374
Web of Science | Medline16
Rydh A ,Suhr O ,Hietala S-O ,Ahlstrom KR ,Pepys MB ,Hawkins PN . Serum amyloid P component scintigraphy in familial amyloid polyneuropathy: regression of visceral amyloid following liver transplantation. Eur J Nucl Med 1998;25:709-713
CrossRef | Medline17
Gertz MA ,Comenzo R ,Falk RH , et al. Definition of organ involvement and treatment response in immunoglobulin light chain amyloidosis (AL): a consensus opinion from the 10th International Symposium on Amyloid and Amyloidosis, Tours, France, 18-22 April 2004. Am J Hematol 2005;79:319-328
CrossRef | Web of Science | Medline18
WHO Expert Committee on Biological Standardization: 48th report. World Health Organ Tech Rep Ser 1999;889:18-19
19
Poole S ,Walker D ,Gaines Das RE ,Gallimore JR ,Pepys MB . The first international standard for serum amyloid A protein (SAA): evaluation in an international collaborative study. J Immunol Methods 1998;214:1-10
CrossRef | Web of Science | Medline20
Tanaka K ,Horita M ,Shibayama H , et al. Secondary amyloidosis associated with Castleman's disease. Intern Med 1995;34:122-126
CrossRef | Web of Science | Medline21
Hamer JPM ,Janssen S ,van Rijswijk MH ,Lie KI . Amyloid cardiomyopathy in systemic non-hereditary amyloidosis: clinical, echocardiographic and electrocardiographic findings in 30 patients with AA and 24 patients with AL amyloidosis. Eur Heart J 1992;13:623-627
Web of Science | Medline22
Werdelin O ,Ranlov P . Amyloidosis in mice produced by transplantation of spleen cells from casein-treated mice. Acta Pathol Microbiol Scand 1966;68:1-18
Medline23
Kisilevsky R, Gruys E, Shirahama T. Does amyloid enhancing factor (AEF) exist? Is AEF a single biological entity? Amyloid: Int J Exp Clin Invest 1995;2:128-33.
24
Schnitzer TJ ,Ansell BM . Amyloidosis in juvenile chronic polyarthritis. Arthritis Rheum 1977;20:Suppl 2:245-252
Medline25
Hawkins PN ,Lachmann HJ ,McDermott MF . Interleukin-1-receptor antagonist in the Muckle-Wells syndrome. N Engl J Med 2003;348:2583-2584
Full Text | Web of Science | Medline26
Shimojima Y ,Takei Y ,Tazawa K , et al. Histopathological regression of systemic AA amyloidosis after surgical treatment of a localized Castleman's disease. Amyloid 2006;13:184-186
CrossRef | Web of Science | Medline27
Gillmore JD ,Lovat LB ,Persey MR ,Pepys MB ,Hawkins PN . Amyloid load and clinical outcome in AA amyloidosis in relation to circulating concentration of serum amyloid A protein. Lancet 2001;358:24-29
CrossRef | Web of Science | Medline
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Will C. Guest, J. Maxwell Silverman, Edward Pokrishevsky, Megan A. O'Neill, Leslie I. Grad, Neil R. Cashman. (2011) Generalization of the Prion Hypothesis to Other Neurodegenerative Diseases: An Imperfect Fit. Journal of Toxicology and Environmental Health, Part A 74:22-24, 1433-1459
CrossRef17
Inmaculada Macías Fernández, Antonia María Fernández Rodríguez, Sergio García Pérez. (2011) Uso de etanercept en amiloidosis secundarias a artritis reumatoide: a propósito de dos casos. Reumatología Clínica 7:6, 397-400
CrossRef18
T. Kofman, P. Grimbert, F. Canouï-Poitrine, J. Zuber, V. Garrigue, C. Mousson, L. Frimat, N. Kamar, G. Couvrat, N. Bouvier, L. Albano, A. Le Thuaut, E. Pillebout, G. Choukroun, L. Couzi, J. Peltier, C. Mariat, M. Delahousse, M. Buchler, P. Le Pogamp, F. Bridoux, C. Pouteil-Noble, P. Lang, V. Audard. (2011) Renal Transplantation in Patients With AA Amyloidosis Nephropathy: Results From a French Multicenter Study. American Journal of Transplantation 11:11, 2423-2431
CrossRef19
Inmaculada Macías Fernández, Antonia María Fernández Rodríguez, Sergio García Pérez. (2011) Use of Etanercept in Amyloidosis Secondary to Rheumatoid Arthritis: A Report of Two Cases. Reumatolog ía Cl ínica (English Edition) 7:6, 397-400
CrossRef20
S. Schönland, N. Blank, A.V. Kristen, J. Beimler, T. Ganten, U. Hegenbart. (2011) Systemische Amyloidosen. Der Internist
CrossRef21
Ulrich Meinzer, Pierre Quartier, Jean-François Alexandra, Véronique Hentgen, Frédérique Retornaz, Isabelle Koné-Paut. (2011) Interleukin-1 Targeting Drugs in Familial Mediterranean Fever: A Case Series and a Review of the Literature. Seminars in Arthritis and Rheumatism 41:2, 265-271
CrossRef22
Z. Birsin Özçakar, Fatoş Yalçınkaya. (2011) Vascular comorbidities in familial Mediterranean fever. Rheumatology International 31:10, 1275-1281
CrossRef23
Yasuaki Okuda, Toshiyuki Yamada, Masaaki Matsuura, Kiyoshi Takasugi, Makoto Goto. (2011) Ageing: a risk factor for amyloid A amyloidosis in rheumatoid arthritis. Amyloid 18:3, 108-111
CrossRef24
Michael J. Hausmann, Esther Maor, Leonid Kachko. (2011) Colchicine-sensitive nephrotic syndrome due to AA amyloidosis. Amyloid 18:3, 169-171
CrossRef25
H. J. Lachmann. (2011) Clinical Immunology Review Series: An approach to the patient with a periodic fever syndrome. Clinical & Experimental Immunology 165:3, 301-309
CrossRef26
Barbara Kluve-Beckerman, Joyce Hardwick, Lijing Du, Merrill D. Benson, Brett P. Monia, Andrew Watt, Rosanne M. Crooke, Adam Mullick. (2011) Antisense oligonucleotide suppression of serum amyloid A reduces amyloid deposition in mice with AA amyloidosis. Amyloid 18:3, 136-146
CrossRef27
T. Ueno, K. Takeda, M. Nagata. (2011) Remission of proteinuria and preservation of renal function in patients with renal AA amyloidosis secondary to rheumatoid arthritis. Nephrology Dialysis Transplantation
CrossRef28
Federico Perfetto, Francesco Cappelli, Franco Bergesio, Gabriele Ciuti, Maria Cristina Porciani, Luigi Padeletti, Alberto Moggi Pignone. (2011) Cardiac amyloidosis: the heart of the matter. Internal and Emergency Medicine
CrossRef29
A. Saha, J. D. Theis, J. A. Vrana, N. K. Dubey, V. V. Batra, S. Sethi. (2011) AA amyloidosis associated with hepatitis B. Nephrology Dialysis Transplantation 26:7, 2407-2412
CrossRef30
Miguel Pinto Valdivia, Milagros Ortiz Torres, Jaime Villena Chávez. (2011) Bocio amiloide secundario a artritis reumatoide. A propósito de un caso. Endocrinología y Nutrición
CrossRef31
M. De La Torre, L. Arboleya, S. Pozo, J. Pinto, J. Velasco. (2011) Rapid and sustained response to tocilizumab, anti-interleukin-6 receptor antibody, in a patient with nephrotic syndrome secondary to systemic juvenile idiopathic arthritis-related amyloidosis. NDT Plus 4:3, 178-180
CrossRef32
(2011) Abstracts. Amyloid 18:Suppl. 1, 6-238
CrossRef33
S. Murata, M. Ueda, Y. Tanabe, N. Kurata, N. Demura, H. Gram, M. Tasaki, Y. Su, H. Jono, M. Shono, K. Obayashi, Y. Ando. (2011) Inhibitory effects of anti-IL-1
antibody in murine AA amyloidosis model. Amyloid 18:Suppl. 1, 38-39
CrossRef34
W. Ishii, B. Kluve-Beckerman, J. J. Liepnieks, S. T. Vakili, M. D. Benson. (2011) Rapidly progressive AA cardiomyopathy. Amyloid 18:Suppl. 1, 203-205
CrossRef35
S. Girnius, L. Dember, G. Doros, M. Skinner. (2011) The changing face of AA amyloidosis: a single center experience. Amyloid 18:Suppl. 1, 226-228
CrossRef36
G. Merlini. (2011) Reducing the amyloid burden through immunotherapy: a major therapeutic advance. Nephrology Dialysis Transplantation 26:5, 1471-1473
CrossRef37
Nagaaki Katoh, Masayuki Matsuda, Ayako Tsuchiya-Suzuki, Shu-ichi Ikeda. (2011) Regression of gastroduodenal amyloid deposition in systemic AL amyloidosis after intensive chemotherapies. British Journal of Haematology 153:4, 535-538
CrossRef38
G. Monsel, V. Martinez, H. Izzedine, B. Mory, F. Bricaire, E. Caumes. (2011) Anal tuberculosis complicated by secondary amyloidosis. Médecine et Maladies Infectieuses 41:5, 264-266
CrossRef39
Udi Nussinovitch, Naomi Nussinovitch, Moshe Nussinovitch, Benjamin Volovitz, Olga Feld, Ilan Ben-Zvi, Avi Livneh. (2011) QT dispersion in amyloidosis due to familial Mediterranean fever. Rheumatology International
CrossRef40
José Manuel Ángel Rey, Antonio Poyato González, Camilo Julio Llamoza Torres, José Luís Montero Álvarez. (2011) Amiloidosis sistémica AA en un receptor de trasplante hepático con complicaciones biliares en el postrasplante. Medicina Clínica 136:9, 411-412
CrossRef41
Murat İnanç Cengiz, Nazır Yayla, Kuddusi Cengiz, Hasan Bagci, Emre Taşkın. (2011) Interaction Between Periodontal Disease and Systemic Secondary Amyloidosis: From Inflammation to Amyloidosis. Journal of Periodontology 82:4, 566-574
CrossRef42
Kai Immonen, Patrik Finne, Carola Grönhagen-Riska, Tom Pettersson, Timo Klaukka, Hannu Kautiainen, Markku Hakala. (2011) A marked decline in the incidence of renal replacement therapy for amyloidosis associated with inflammatory rheumatic diseases – data from nationwide registries in Finland. Amyloid 18:1, 25-28
CrossRef43
K. El Karoui, V. Vuiblet, D. Dion, H. Izzedine, J. Guitard, L. Frimat, M. Delahousse, P. Remy, J.-J. Boffa, E. Pillebout, L. Galicier, L.-H. Noel, E. Daugas. (2011) Renal involvement in Castleman disease. Nephrology Dialysis Transplantation 26:2, 599-609
CrossRef44
Michael J. Ombrello, Daniel L. Kastner. (2011) Autoinflammation in 2010: Expanding clinical spectrum and broadening therapeutic horizons. Nature Reviews Rheumatology 7:2, 82-84
CrossRef45
Wataru Ishii, Dai Kishida, Ayako Suzuki, Yasuhiro Shimojima, Masayuki Matsuda, Yoshinobu Hoshii, Shu-ichi Ikeda. (2011) A case with rheumatoid arthritis and systemic reactive AA amyloidosis showing rapid regression of amyloid deposition on gastroduodenal mucosa after a combined therapy of corticosteroid and etanercept. Rheumatology International 31:2, 247-250
CrossRef46
Ilan Ben-Zvi, Avi Livneh. (2011) Chronic inflammation in FMF: markers, risk factors, outcomes and therapy. Nature Reviews Rheumatology 7:2, 105-112
CrossRef47
Juan I. Aróstegui. (2011) Hereditary systemic autoinflammatory diseases. Reumatolog ía Cl ínica (English Edition) 7:1, 45-50
CrossRef48
Katia Stankovic, Gilles Grateau. (2011) Is there any treatment for inflammatory amyloidosis?. Joint Bone Spine 78:1, 7-9
CrossRef49
Simon M. Mueller, Peter Itin, Peter Haeusermann. (2011) Muckle-Wells Syndrome Effectively Treated with Canakinumab: Is the Recommended Dosing Schedule Mandatory?. Dermatology 223:2, 113-118
CrossRef50
Jasmin B Kuemmerle-Deschner, Peter Lohse, Ina Koetter, Guenther E Dannecker, Fabian Reess, Katharina Ummenhofer, Silvia Koch, Nikolay Tzaribachev, Anja Bialkowski, Susanne M Benseler. (2011) NLRP3 E311K mutation in a large family with Muckle-Wells syndrome - description of a heterogeneous phenotype and response to treatment. Arthritis Research & Therapy 13:6, R196
CrossRef51
Naomi Nussinovitch, Avi Livneh, Keren Katz, Pnina Langevitz, Olga Feld, Moshe Nussinovitch, Benjamin Volovitz, Merav Lidar, Udi Nussinovitch. (2011) Heart rate variability in familial Mediterranean fever. Rheumatology International 31:1, 39-43
CrossRef52
Yuji AKIYAMA. (2011) Anti-rheumatic therapy in patients with rheumatoid arthritis undergoing hemodialysis. Japanese Journal of Clinical Immunology 34:6, 485-492
CrossRef53
Jasmin B Kuemmerle-Deschner, Eduardo Ramos, Norbert Blank, Joachim Roesler, Sandra D Felix, Thomas Jung, Kirstin Stricker, Abhijit Chakraborty, Stacey Tannenbaum, Andrew M Wright, Christiane Rordorf. (2011) Canakinumab (ACZ885, a fully human IgG1 anti-IL-1β mAb) induces sustained remission in pediatric patients with cryopyrin-associated periodic syndrome (CAPS). Arthritis Research & Therapy 13:1, R34
CrossRef54
Tadashi Nakamura, Syu-ichi Higashi, Kunihiko Tomoda, Michishi Tsukano, Masahiro Shono. (2010) Etanercept can induce resolution of renal deterioration in patients with amyloid A amyloidosis secondary to rheumatoid arthritis. Clinical Rheumatology 29:12, 1395-1401
CrossRef55
Muhammad Masoom Javaid, Manivarma Kamalanathan, Sui Phin Kon. (2010) RAPID DEVELOPMENT OF RENAL FAILURE SECONDARY TO AA-TYPE AMYLOIDOSIS IN A PATIENT WITH POLYMYALGIA RHEUMATICA. Journal of Renal Care 36:4, 199-202
CrossRef56
Catarina Fidalgo, Joaquim Calado, Marilia Cravo. (2010) Secondary Amyloidosis in a Patient with Long Duration Crohnʼs Disease Treated with Infliximab. BioDrugs 24, 15-17
CrossRef57
S. E. Kolstoe, P. P. Mangione, V. Bellotti, G. W. Taylor, G. A. Tennent, S. Deroo, A. J. Morrison, A. J. A. Cobb, A. Coyne, M. G. McCammon, T. D. Warner, J. Mitchell, R. Gill, M. D. Smith, S. V. Ley, C. V. Robinson, S. P. Wood, M. B. Pepys. (2010) Trapping of palindromic ligands within native transthyretin prevents amyloid formation. Proceedings of the National Academy of Sciences 107:47, 20483-20488
CrossRef58
Karl Bodin, Stephan Ellmerich, Melvyn C. Kahan, Glenys A. Tennent, Andrzej Loesch, Janet A. Gilbertson, Winston L. Hutchinson, Palma P. Mangione, J. Ruth Gallimore, David J. Millar, Shane Minogue, Amar P. Dhillon, Graham W. Taylor, Arthur R. Bradwell, Aviva Petrie, Julian D. Gillmore, Vittorio Bellotti, Marina Botto, Philip N. Hawkins, Mark B. Pepys. (2010) Antibodies to human serum amyloid P component eliminate visceral amyloid deposits. Nature 468:7320, 93-97
CrossRef59
Didem Ozdemir, Selcuk Dagdelen, Tomris Erbas. (2010) Endocrine Involvement in Systemic Amyloidosis. Endocrine Practice 16:6, 1056-1063
CrossRef60
Raine Tatara, Tadashi Nagai, Hiroyuki Kobayashi, Kaoru Hatano, Takahiro Suzuki, Kazuo Muroi, Keiya Ozawa. (2010) AA amyloidosis associated with macroglobulinemia. International Journal of Hematology 92:4, 675-677
CrossRef61
M Vasala, K Immonen, H Kautiainen, M Hakala. (2010) More evidence of declining incidence of amyloidosis associated with inflammatory rheumatic diseases. Scandinavian Journal of Rheumatology 39:6, 461-465
CrossRef62
Werner Van Steenbergen, Lieve Braeye, Rudy Harlet, Frederik Nevens, Johan Fevery, Valeer Desmet, Tania Roskams, Jacques Pirenne. (2010) Primary sclerosing cholangitis complicated by amyloid A amyloidosis: complete regression of the nephrotic syndrome by liver transplantation. European Journal of Gastroenterology & Hepatology 22:10, 1265-1270
CrossRef63
Daichi Inoue, Hiroshi Arima, Chiharu Kawanami, Yoko Takiuchi, Seiji Nagano, Takaharu Kimura, Sonoko Shimoji, Minako Mori, Sumie Tabata, Soshi Yanagita, Akiko Matsushita, Kenichi Nagai, Yukihiro Imai, Takayuki Takahashi. (2010) Excellent therapeutic effect of tocilizumab on intestinal amyloid a deposition secondary to active rheumatoid arthritis. Clinical Rheumatology 29:10, 1195-1197
CrossRef64
Arvind J Trindade, Wenquing Cao, Divyesh Sejpal. (2010) Crohn's Disease Masquerading as Idiopathic Amyloidosis and Nephrotic Syndrome for 2 Years Before Diagnosis. The American Journal of Gastroenterology 105:10, 2301-2302
CrossRef65
Alejandra Fernández Luque, Iván Urra, Raquel López-Martos. (2010) Mujer de 41 años con insuficiencia renal y masa hepática. Medicina Clínica 135:11, 519-526
CrossRef66
Luciana Breda, Manuela Nozzi, Sara De Sanctis, Francesco Chiarelli. (2010) Laboratory Tests in the Diagnosis and Follow-Up of Pediatric Rheumatic Diseases: An Update. Seminars in Arthritis and Rheumatism 40:1, 53-72
CrossRef67
Federico Perfetto, Alberto Moggi-Pignone, Riccardo Livi, Alessio Tempestini, Franco Bergesio, Marco Matucci-Cerinic. (2010) Systemic amyloidosis: a challenge for the rheumatologist. Nature Reviews Rheumatology 6:7, 417-429
CrossRef68
Krish Bhadra, Kelly J. Butnor, Gerald S. Davis. (2010) A Bronchoscopic Oddity. Journal of Bronchology & Interventional Pulmonology 17:3, 248-252
CrossRef69
Csilla Trinn. (2010) Amyloidosis. Orvosi Hetilap 151:29, 1182-1189
CrossRef70
Laima Leonavičienė, Danutė Povilėnaitė, Rūta Bradūnaitė, Dalia Vaitkienė, Algirdas Venalis. (2010) Treatment of experimental amyloidosis with antirheumatic drugs. Acta medica Lituanica 17:1, 17-29
CrossRef71
Antonio Fernández-Nebro, Alejandro Olivé, María Carmen Castro, Angela Herranz Varela, Elena Riera, Maria V. Irigoyen, María Jesús García de Yébenes, Rosario García-Vicuña. (2010) Long-term TNF-α Blockade in Patients with Amyloid A Amyloidosis Complicating Rheumatic Diseases. The American Journal of Medicine 123:5, 454-461
CrossRef72
Tom Pettersson, Yrjö T. Konttinen. (2010) Amyloidosis—Recent Developments. Seminars in Arthritis and Rheumatism 39:5, 356-368
CrossRef73
Anupama Bhat, Carlo Selmi, Stanley M. Naguwa, Gurtej S. Cheema, M. Eric Gershwin. (2010) Currents Concepts on the Immunopathology of Amyloidosis. Clinical Reviews in Allergy & Immunology 38:2-3, 97-106
CrossRef74
R. P. E. Sarkany, S. M. Breathnach, A. A. M. Morris, K. Weismann, P. D. Flynn. 2010. Metabolic and Nutritional Disorders. , 1-103.
CrossRef75
Julian D. Gillmore, Glenys A. Tennent, Winston L. Hutchinson, Janet Ruth Gallimore, Helen J. Lachmann, Hugh J.B. Goodman, Mark Offer, David J. Millar, Aviva Petrie, Philip N. Hawkins, Mark B. Pepys. (2010) Sustained pharmacological depletion of serum amyloid P component in patients with systemic amyloidosis. British Journal of Haematology 148:5, 760-767
CrossRef76
Shogo Tajima, Tomonori Ushijima, Shoji Matuya, Hajime Horiuchi. (2010) AA-type amyloidosis in association with non-Hodgkin's lymphoma following CMV viremia: Autopsy case. Pathology International 60:3, 222-227
CrossRef77
Young Sil Lee, Seong Su Moon, Soon Kim, Jong Im Lee. (2010) A Case of Thyroid Amyloidosis Misrecognized as Subacute Thyroiditis. Endocrinology and Metabolism 25:4, 360
CrossRef78
Eun Ae Yang, Dong Won Lee, Myung Chul Hyun, Min Hyun Cho. (2010) Secondary renal amyloidosis in a 13-year-old girl with bronchiectasis. Korean Journal of Pediatrics 53:7, 770
CrossRef79
Kenya Kusunose, Hirotsugu Yamada, Takashi Iwase, Susumu Nishio, Noriko Tomita, Toshiyuki Niki, Koji Yamaguchi, Kunihiko Koshiba, Yoshio Taketani, Takeshi Soeki, Tetsuzo Wakatsuki, Masashi Akaike, Takao Shoichiro, Masafumi Harada, Noriko Kagawa, Eiji Kudo, Masataka Sata. (2010) Cardiac Magnetic Resonance Imaging and 2-Dimensional Speckle Tracking Echocardiography in Secondary Cardiac Amyloidosis. Circulation Journal 74:7, 1494-1496
CrossRef80
Hirotoshi Fukatsu, Haruka Miyoshi, Kuniharu Ishiki. (2010) Spontaneous Resolution of Multiple Nodular Pulmonary AA Amyloidosis. Internal Medicine 49:21, 2303-2307
CrossRef81
Harit V. Desai, Wilbert S. Aronow, Stephen J. Peterson, William H. Frishman. (2010) Cardiac Amyloidosis. Cardiology in Review 18:1, 1-11
CrossRef82
Prayman Sattianayagam, Philip Hawkins, Julian Gillmore. (2009) Amyloid and the GI tract. Expert Review of Gastroenterology & Hepatology 3:6, 615-630
CrossRef83
U. Wenzel, J. Velden, U. Helmchen. (2009) Proteinurie bei einem 62-jährigen Patienten. Der Nephrologe 4:6, 527-531
CrossRef84
Laura Obici, Sara Raimondi, Francesca Lavatelli, Vittorio Bellotti, Giampaolo Merlini. (2009) Susceptibility to AA amyloidosis in rheumatic diseases: A critical overview. Arthritis & Rheumatism 61:10, 1435-1440
CrossRef85
(2009) Outcomes of Heart Transplantation for Cardiac Amyloidosis: Subanalysis of the Spanish Registry for Heart Transplantation. American Journal of Transplantation 9:10, 2443-2443
CrossRef86
Prayman T. Sattianayagam, Philip N. Hawkins, Julian D. Gillmore. (2009) Systemic amyloidosis and the gastrointestinal tract. Nature Reviews Gastroenterology & Hepatology 6:10, 608-617
CrossRef87
T. Brünnler, F. Bataille, F. Hofstädter, G. Birkenfeld, J. Schölmerich. (2009) 41-jähriger Patient mit unklarer Diarrhö. Der Internist 50:9, 1149-1154
CrossRef88
Hanna von Hutten, Michael Mihatsch, Hartmut Lobeck, Birgit Rudolph, Magdalena Eriksson, Christoph Röcken. (2009) Prevalence and Origin of Amyloid in Kidney Biopsies. The American Journal of Surgical Pathology 33:8, 1198-1205
CrossRef89
Arnaud Millet, Nathalie Rioux-Leclercq, Jean-pierre Le Lay, Patrick Le Pogamp, Cécile Vigneau. (2009) Unexpected remission of renal AA amyloidosis associated with rheumatoid arthritis. Joint Bone Spine 76:4, 431-432
CrossRef90
Lachmann, Helen J., Kone-Paut, Isabelle, Kuemmerle-Deschner, Jasmin B., Leslie, Kieron S., Hachulla, Eric, Quartier, Pierre, Gitton, Xavier, Widmer, Albert, Patel, Neha, Hawkins, Philip N., . (2009) Use of Canakinumab in the Cryopyrin-Associated Periodic Syndrome. New England Journal of Medicine 360:23, 2416-2425
Full Text91
E. Roig, L. Almenar, F. González-Vílchez, G. Rábago, J. Delgado, M. Gómez-Bueno, M. G. Crespo-Leiro, J. M. Arizón, L. de la Fuente, N. Manito, . (2009) Outcomes of Heart Transplantation for Cardiac Amyloidosis: Subanalysis of the Spanish Registry for Heart Transplantation. American Journal of Transplantation 9:6, 1414-1419
CrossRef92
N. Blank, H.M. Lorenz. (2009) Diagnostik und Therapie der AA-Amyloidose. Der Pathologe 30:3, 219-225
CrossRef93
Mohamed Younes, Wided Korbaa, Adnène Moussa, Saoussen Zrour, Ismail Bejia, Mongi Touzi, Abdelfatteh Zakhama, Naceur Bergaoui. (2009) Prevalence of subclinical amyloidosis in Tunisian patients with rheumatoid arthritis. Joint Bone Spine 76:3, 254-259
CrossRef94
Ingrid I van Gameren, Edo Vellenga, Bouke PC Hazenberg. (2009) Novel treatments for systemic amyloidosis. International Journal of Clinical Rheumatology 4:2, 171-188
CrossRef95
Arathi R. Setty, Dwight Robinson. (2009) A 62-year-old man with wrist and hand pain. Arthritis Care & Research 61:1, 132-138
CrossRef96
Seok Jae Kang, Joo-Hark Yi, Hyun-Seok Hong, Si-Hyung Jang, Moon-Hyang Park, Ho-Jung Kim, Kyu-Yong Lee, Young-Joo Lee, Sang-Woong Han, Seong-Ho Koh. (2009) Secondary Amyloidosis Associated with Multiple Sclerosis. Journal of Clinical Neurology 5:3, 146
CrossRef97
Hiroaki TAMURA, Kiminori HASEGAWA. (2009) A review for recent advances in AA amyloid research and therapeutic approach to AA amyloidosis complicating rheumatoid arthritis. Japanese Journal of Clinical Immunology 32:1, 35-42
CrossRef98
Hiroshi Nonoguchi, Yukimasa Kohda, Rika Fukutomi, Yushi Nakayama, Masahiro Naruse, Kenichiro Kitamura, Takeaki Inoue, Takeshi Nakanishi, Kimio Tomita. (2009) A Case with Acute Renal Failure and Subsequent Nephrotic Syndrome. Renal Failure 31:2, 162-166
CrossRef99
Simmie L. Foster, Ruslan Medzhitov. (2009) Gene-specific control of the TLR-induced inflammatory response. Clinical Immunology 130:1, 7-15
CrossRef100
Mirjam Ricarda Hampel, Joerg Kinne, Ulrich Wernery, Andreas Pospischil, Josef Kellermann, Reinhold Paul Linke. (2009) Increasing fatal AA amyloidosis in hunting falcons and how to identify the risk: a report from the United Arab Emirates. Amyloid 16:3, 122-132
CrossRef101
Maria Cristina Porciani, Alessio Lilli, Federico Perfetto, Francesco Cappelli, Carmelo Massimiliano Rao, Stefano Del Pace, Mauro Ciaccheri, Gabriele Castelli, Roberto Tarquini, Lara Romagnani, Tiziana Pastorini, Luigi Padeletti, Franco Bergesio. (2009) Tissue Doppler and strain imaging: a new tool for early detection of cardiac amyloidosis. Amyloid 16:2, 63-70
CrossRef102
L. C. Kramer, T. A. J. M. Manschot, J. N. M. Barendregt, J. M. Smit. (2008) Whipple's disease: often a late diagnosis and a rare cause of nephropathy. NDT Plus 2:1, 55-58
CrossRef103
K. Stankovic, G. Grateau. (2008) Quoi de neuf dans les maladies auto-inflammatoires ?. La Revue de Médecine Interne 29:12, 994-999
CrossRef104
K. Groot, M.J. Mihatsch. (2008) Nierenmanifestationen bei rheumatischen Erkrankungen. Der Nephrologe 3:6, 484-493
CrossRef105
Carlo Tomasini, Anna Claudia Butera, Mario Pippione. (2008) Spectrum of cutaneous diseases in monoclonal gammopathies. Expert Review of Dermatology 3:5, 613-629
CrossRef106
T Pettersson, YT Konttinen, CPJ Maury. (2008) Treatment strategies for amyloid A amyloidosis. Expert Opinion on Pharmacotherapy 9:12, 2117-2128
CrossRef107
Lucio Manenti, Pius Tansinda, Augusto Vaglio. (2008) Eprodisate in amyloid A amyloidosis: a novel therapeutic approach?. Expert Opinion on Pharmacotherapy 9:12, 2175-2180
CrossRef108
S. Elitok, R. Kettritz. (2008) Pathogenese und Diagnostik von AA-Amyloidosen. Der Nephrologe 3:4, 285-290
CrossRef109
Györgyi Műzes, Pál Miheller, Zsolt Tulassay. (2008) Az amyloidosis emésztőrendszeri következményei. Orvosi Hetilap 149:29, 1363-1366
CrossRef110
T. Cornelis, B. Bammens, E. Lerut, L. Cosyn, G. Goovaerts, R. Westhovens, Y. Vanrenterghem. (2008) AA amyloidosis due to chronic oxalate arthritis and vasculitis in a patient with secondary oxalosis after jejunoileal bypass surgery. Nephrology Dialysis Transplantation 23:10, 3362-3364
CrossRef111
Dimitrios A. Pappas, Janis M. Taube, Joan M. Bathon, Jon T. Giles. (2008) A 73-year-old woman with rheumatoid arthritis and shortness of breath. Arthritis & Rheumatism 59:6, 892-899
CrossRef112
Franktien Turkstra, Rico N. P. M. Rinkel, Hagen Biermann, Paul Valk, Alexandre E. Voskuyl. (2008) Tracheobronchomalacia due to amyloidosis in a patient with rheumatoid arthritis. Clinical Rheumatology 27:6, 807-808
CrossRef113
Anita Annaházi, István Németh, Szabolcs Modok, Károly Szentpáli, László Tiszlavicz, Tibor Wittmann, László Czakó. (2008) Amyloidosis okozta colonstrictura mint a myeloma multiplex első tünete – Esetismertetés. Orvosi Hetilap 149:25, 1181-1185
CrossRef114
Marco Gattorno, Silvia Federici, Maria Antonietta Pelagatti, Roberta Caorsi, Giacomo Brisca, Clara Malattia, Alberto Martini. (2008) Diagnosis and Management of Autoinflammatory Diseases in Childhood. Journal of Clinical Immunology 28:S1, 73-83
CrossRef115
U. Helmchen, J. Velden, U. Kneissler, R.A.K. Stahl. (2008) Klinische Pathologie der renalen Amyloidosen. Der Nephrologe 3:3, 203-215
CrossRef116
Tadashi Nakamura. (2008) Clinical strategies for amyloid A amyloidosis secondary to rheumatoid arthritis. Modern Rheumatology 18:2, 109-118
CrossRef117
Ellen C. Ebert, Michael Nagar. (2008) Gastrointestinal Manifestations of Amyloidosis. The American Journal of Gastroenterology 103:3, 776-787
CrossRef118
L. Renders. (2008) Eprodisat. Der Nephrologe 3:2, 134-135
CrossRef119
Georgene Hergenroeder, John B. Redell, Anthony N. Moore, William P. Dubinsky, Robert T. Funk, John Crommett, Guy L. Clifton, Robert Levine, Alex Valadka, Pramod K. Dash. (2008) Identification of Serum Biomarkers in Brain-Injured Adults: Potential for Predicting Elevated Intracranial Pressure. Journal of Neurotrauma 25:2, 79-93
CrossRef120
B.H. Thiers. (2008) Eprodisate for the Treatment of Renal Disease in AA Amyloidosis. Yearbook of Dermatology and Dermatologic Surgery 2008, 392-393
CrossRef121
B.H. Thiers. (2008) Natural History and Outcome in Systemic AA Amyloidosis. Yearbook of Dermatology and Dermatologic Surgery 2008, 391-392
CrossRef122
Riitta Koivuniemi, Leena Paimela, Risto Suomalainen, Tom Törnroth, Marjatta Leirisalo-Repo. (2008) Amyloidosis is frequently undetected in patients with rheumatoid arthritis. Amyloid 15:4, 262-268
CrossRef123
John G Ryan, Raphaela Goldbach-Mansky. (2008) The spectrum of autoinflammatory diseases: recent bench to bedside observations. Current Opinion in Rheumatology 20:1, 66-75
CrossRef124
Andrew D Rule, Nelson Leung. (2007) Eprodisate slows the progression of renal disease in patients with AA amyloidosis. Nature Clinical Practice Nephrology 3:11, 592-593
CrossRef125
(2007) Eprodisate in AA Amyloidosis. New England Journal of Medicine 357:11, 1153-1154
Full Text126
Shai Padeh, Yakov Berkun. (2007) Auto-inflammatory Fever Syndromes. Rheumatic Disease Clinics of North America 33:3, 585-623
CrossRef
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