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Helen J. Lachmann - One of the best experts on this subject based on the ideXlab platform.
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Secondary, AA, Amyloidosis
Rheumatic diseases clinics of North America, 2018Co-Authors: Riccardo Papa, Helen J. LachmannAbstract:AA Amyloidosis, otherwise known as secondary Amyloidosis, is a complication of chronic inflammation. The amyloid fibrils are derived from the hepatic acute phase reactant, serum amyloid A protein. Clinically AA Amyloidosis has a predominantly renal presentation with proteinuria and renal impairment. Untreated disease will progress to end-stage renal failure. Treatment depends on complete control of the underlying chronic inflammatory condition, and if this can be achieved long-term outcomes are favourable. Median survival in patients with AA Amyloidosis now exceeds 12 years although renal failure eventually develops in more than 40%.
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P02-019 - Detection of risk factors for AA-Amyloidosis
Pediatric Rheumatology, 2013Co-Authors: S Németh, Laura Obici, Helen J. Lachmann, S Grandemange, C OberkaninsAbstract:Systemic reactive (AA) Amyloidosis represents the most important complication within TNF receptor associated periodic syndrome (TRAPS), familial Mediterranean fever (FMF) and other autoinflammatory syndromes, progressively leading to endstage renal failure. The homozygous condition of the serum amyloid A (SAA) variant SAA1.1 is significantly associated with the occurrence of AA Amyloidosis in TRAPS patients. Likewise in FMF patients the MEFV mutation c.2080A>G (M694V) correlates with Amyloidosis and the SAA1.1/SAA1.1 genotype increases clinical severity (age at disease onset, Amyloidosis, arthritis).
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brief report AA Amyloidosis complicating the hereditary periodic fever syndromes
Arthritis & Rheumatism, 2013Co-Authors: Thirusha Lane, Julian D. Gillmore, Ashutosh D. Wechalekar, Janet A. Gilbertson, Dorota Rowczenio, Philip N. Hawkins, J Loeffler, A Bybee, T Russell, Helen J. LachmannAbstract:Objective AA Amyloidosis is a life-threatening complication of the hereditary periodic fever syndromes (HPFS), which are otherwise often compatible with normal life expectancy. This study was undertaken to determine the characteristics, presentation, natural history, and response to treatment in 46 patients who had been referred for evaluation at the UK National Amyloidosis Centre. Methods Disease activity was monitored by serial measurement of serum amyloid A. Renal function was assessed by measurement of serum creatinine and albumin levels, the estimated glomerular filtration rate, and proteinuria from 24-hour urine collections. The amyloid load was measured by serum amyloid P scintigraphy. Results Twenty-four patients had familial Mediterranean fever, 12 patients had tumor necrosis factor receptor–associated periodic syndrome, 6 patients had cryopyrin-associated periodic syndromes, and 4 patients had mevalonate kinase deficiency. The median age at onset of HPFS was 5 years; median age at presentation with AA Amyloidosis was 38 years. Diagnosis of an HPFS had not been considered prior to presentation with AA Amyloidosis in 23 patients (50%). Eleven patients (24%) had end-stage renal failure (ESRF) at presentation; of these, 3 had received transplants prior to referral. A further 13 patients developed ESRF over the followup period, with 10 undergoing renal transplantation. The median time to progression to ESRF from onset of AA Amyloidosis was 3.3 years (interquartile range [IQR] 2–8), with a median time to transplant of 4 years (IQR 3–6). Eleven patients (24%) died. The median survival in the entire cohort was 19 years from diagnosis of AA Amyloidosis. Of the 37 patients who were treated successfully, or in whom at least partial suppression of the underlying HPFS was achieved, 17 (46%) showed amyloid regression, 14 (38%) showed a stable amyloid load, and 2 (5%) showed increased amyloid deposition over the followup period. Conclusion AA Amyloidosis remains a challenging and serious late complication of HPFS; however, outcomes are excellent when HPFS is diagnosed early enough to allow effective treatment, thus preventing or retarding further amyloid deposition and organ damage.
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Inflammatory bowel disease and systemic AA Amyloidosis.
Digestive diseases and sciences, 2013Co-Authors: Prayman T. Sattianayagam, Julian D. Gillmore, Jennifer H. Pinney, Simon D. J. Gibbs, Ashutosh D. Wechalekar, Janet A. Gilbertson, Dorota Rowczenio, Philip N. Hawkins, Helen J. LachmannAbstract:Background Systemic AA Amyloidosis is a recognised complication of inflammatory bowel disease. AA Amyloidosis is a potential cause of end-stage renal failure and mortality but little is known of the natural history of this condition in inflammatory bowel disease.
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Natural history and outcome in systemic AA Amyloidosis.
The New England journal of medicine, 2007Co-Authors: Helen J. Lachmann, Julian D. Gillmore, Janet A. Gilbertson, Hugh J. B. Goodman, J. Ruth Gallimore, Caroline A. Sabin, Philip N. HawkinsAbstract: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 highe...
Shu-ichi Ikeda - One of the best experts on this subject based on the ideXlab platform.
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Unexpectedly high incidence of visceral AA-Amyloidosis in slaughtered cattle in Japan
Amyloid, 2005Co-Authors: Kana Tojo, Takahiko Tokuda, Yoshinobu Hoshii, Keiichi Higuchi, Takane Matsui, Fuyuki Kametani, Shu-ichi IkedaAbstract:Experimental mouse AA Amyloidosis can be transmissible by dietary ingestion of amyloid fibrils and it is well known that AA Amyloidosis occasionally develops in aged cattle. Bovine liver and intestine have conventionally been used in Oriental foods, and the incidence of visceral AA Amyloidosis in slaughtered cattle was evaluated. Renal tissues from 302 aged cattle older than 4 years were obtained from a local abattoir. Amyloid deposition was microscopically examined and amyloid protein was immunochemically determined. Renal amyloid deposition was seen in 15 out of 302 cattle with no previous history of diseas, an incidence of 5.0%. Amyloid protein in these cattle was AA and they had pathological findings in their visceral organs on gross examination. The incidence of visceral AA Amyloidosis in slaughtered cattle in this study was disturbingly high compared with those (0.4–2.7%) previously reported from Japan and other foreign countries. AA Amyloidosis is a life-threatening complication in patients with ch...
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Unexpectedly high incidence of visceral AA-Amyloidosis in slaughtered cattle in Japan.
Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis, 2005Co-Authors: Kana Tojo, Takahiko Tokuda, Yoshinobu Hoshii, Keiichi Higuchi, Takane Matsui, Fuyuki Kametani, Shu-ichi IkedaAbstract:Experimental mouse AA Amyloidosis can be transmissible by dietary ingestion of amyloid fibrils and it is well known that AA Amyloidosis occasionally develops in aged cattle. Bovine liver and intestine have conventionally been used in Oriental foods, and the incidence of visceral AA Amyloidosis in slaughtered cattle was evaluated. Renal tissues from 302 aged cattle older than 4 years were obtained from a local abattoir. Amyloid deposition was microscopically examined and amyloid protein was immunochemically determined. Renal amyloid deposition was seen in 15 out of 302 cattle with no previous history of diseas, an incidence of 5.0%. Amyloid protein in these cattle was AA and they had pathological findings in their visceral organs on gross examination. The incidence of visceral AA Amyloidosis in slaughtered cattle in this study was disturbingly high compared with those (0.4-2.7%) previously reported from Japan and other foreign countries. AA Amyloidosis is a life-threatening complication in patients with chronic inflammatory diseases and these patients at risk should avoid ingesting food that may possibly contain AA amyloid fibrils. More detailed information on cattle Amyloidosis is required to guarantee the safety of our food.
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Fatal Acute Pancreatitis with Cystic Formation in Reactive Systemic AA Amyloidosis Secondary to Rheumatoid Arthritis
Internal medicine (Tokyo Japan), 2003Co-Authors: Masayuki Matsuda, Shunpei Sakurai, Akio Suzuki, Masumi Kadoya, Shu-ichi IkedaAbstract:We report a patient with reactive systemic AA Amyloidosis secondary to rheumatoid arthritis who showed fatal acute pancreatitis with a cystic formation in the pancreas head. The pancreatitis rapidly worsened despite intensive treatment and resulted in death. In this patient severe deposition of amyloid in the gastrointestinal tract was considered to play an important role in the pathogenesis of the acute pancreatitis. This is an unusual complication in patients with AA Amyloidosis, but we should consider it as a possible diagnosis when patients with AA Amyloidosis show recurrent or intractable pain in the upper abdomen.
Fuyuki Kametani - One of the best experts on this subject based on the ideXlab platform.
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Fecal transmission of AA Amyloidosis in the cheetah contributes to high incidence of disease.
Proceedings of the National Academy of Sciences of the United States of America, 2008Co-Authors: Beiru Zhang, Yumi Une, Jingmin Yan, Junjie Yao, Jinko Sawashita, Masayuki Mori, Hiroshi Tomozawa, Fuyuki KametaniAbstract:AA Amyloidosis is one of the principal causes of morbidity and mortality in captive cheetahs (Acinonyx jubatus), which are in danger of extinction, but little is known about the underlying mechanisms. Given the transmissible characteristics of AA Amyloidosis, transmission between captive cheetahs may be a possible mechanism involved in the high incidence of AA Amyloidosis. In this study of animals with AA Amyloidosis, we found that cheetah feces contained AA amyloid fibrils that were different from those of the liver with regard to molecular weight and shape and had greater transmissibility. The infectious activity of fecal AA amyloid fibrils was reduced or abolished by the protein denaturants 6 M guanidine·HCl and formic acid or by AA immunodepletion. Thus, we propose that feces are a vehicle of transmission that may accelerate AA Amyloidosis in captive cheetah populations. These results provide a pathogenesis for AA Amyloidosis and suggest possible measures for rescuing cheetahs from extinction.
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Unexpectedly high incidence of visceral AA-Amyloidosis in slaughtered cattle in Japan
Amyloid, 2005Co-Authors: Kana Tojo, Takahiko Tokuda, Yoshinobu Hoshii, Keiichi Higuchi, Takane Matsui, Fuyuki Kametani, Shu-ichi IkedaAbstract:Experimental mouse AA Amyloidosis can be transmissible by dietary ingestion of amyloid fibrils and it is well known that AA Amyloidosis occasionally develops in aged cattle. Bovine liver and intestine have conventionally been used in Oriental foods, and the incidence of visceral AA Amyloidosis in slaughtered cattle was evaluated. Renal tissues from 302 aged cattle older than 4 years were obtained from a local abattoir. Amyloid deposition was microscopically examined and amyloid protein was immunochemically determined. Renal amyloid deposition was seen in 15 out of 302 cattle with no previous history of diseas, an incidence of 5.0%. Amyloid protein in these cattle was AA and they had pathological findings in their visceral organs on gross examination. The incidence of visceral AA Amyloidosis in slaughtered cattle in this study was disturbingly high compared with those (0.4–2.7%) previously reported from Japan and other foreign countries. AA Amyloidosis is a life-threatening complication in patients with ch...
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Unexpectedly high incidence of visceral AA-Amyloidosis in slaughtered cattle in Japan.
Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis, 2005Co-Authors: Kana Tojo, Takahiko Tokuda, Yoshinobu Hoshii, Keiichi Higuchi, Takane Matsui, Fuyuki Kametani, Shu-ichi IkedaAbstract:Experimental mouse AA Amyloidosis can be transmissible by dietary ingestion of amyloid fibrils and it is well known that AA Amyloidosis occasionally develops in aged cattle. Bovine liver and intestine have conventionally been used in Oriental foods, and the incidence of visceral AA Amyloidosis in slaughtered cattle was evaluated. Renal tissues from 302 aged cattle older than 4 years were obtained from a local abattoir. Amyloid deposition was microscopically examined and amyloid protein was immunochemically determined. Renal amyloid deposition was seen in 15 out of 302 cattle with no previous history of diseas, an incidence of 5.0%. Amyloid protein in these cattle was AA and they had pathological findings in their visceral organs on gross examination. The incidence of visceral AA Amyloidosis in slaughtered cattle in this study was disturbingly high compared with those (0.4-2.7%) previously reported from Japan and other foreign countries. AA Amyloidosis is a life-threatening complication in patients with chronic inflammatory diseases and these patients at risk should avoid ingesting food that may possibly contain AA amyloid fibrils. More detailed information on cattle Amyloidosis is required to guarantee the safety of our food.
Kana Tojo - One of the best experts on this subject based on the ideXlab platform.
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Unexpectedly high incidence of visceral AA-Amyloidosis in slaughtered cattle in Japan
Amyloid, 2005Co-Authors: Kana Tojo, Takahiko Tokuda, Yoshinobu Hoshii, Keiichi Higuchi, Takane Matsui, Fuyuki Kametani, Shu-ichi IkedaAbstract:Experimental mouse AA Amyloidosis can be transmissible by dietary ingestion of amyloid fibrils and it is well known that AA Amyloidosis occasionally develops in aged cattle. Bovine liver and intestine have conventionally been used in Oriental foods, and the incidence of visceral AA Amyloidosis in slaughtered cattle was evaluated. Renal tissues from 302 aged cattle older than 4 years were obtained from a local abattoir. Amyloid deposition was microscopically examined and amyloid protein was immunochemically determined. Renal amyloid deposition was seen in 15 out of 302 cattle with no previous history of diseas, an incidence of 5.0%. Amyloid protein in these cattle was AA and they had pathological findings in their visceral organs on gross examination. The incidence of visceral AA Amyloidosis in slaughtered cattle in this study was disturbingly high compared with those (0.4–2.7%) previously reported from Japan and other foreign countries. AA Amyloidosis is a life-threatening complication in patients with ch...
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Unexpectedly high incidence of visceral AA-Amyloidosis in slaughtered cattle in Japan.
Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis, 2005Co-Authors: Kana Tojo, Takahiko Tokuda, Yoshinobu Hoshii, Keiichi Higuchi, Takane Matsui, Fuyuki Kametani, Shu-ichi IkedaAbstract:Experimental mouse AA Amyloidosis can be transmissible by dietary ingestion of amyloid fibrils and it is well known that AA Amyloidosis occasionally develops in aged cattle. Bovine liver and intestine have conventionally been used in Oriental foods, and the incidence of visceral AA Amyloidosis in slaughtered cattle was evaluated. Renal tissues from 302 aged cattle older than 4 years were obtained from a local abattoir. Amyloid deposition was microscopically examined and amyloid protein was immunochemically determined. Renal amyloid deposition was seen in 15 out of 302 cattle with no previous history of diseas, an incidence of 5.0%. Amyloid protein in these cattle was AA and they had pathological findings in their visceral organs on gross examination. The incidence of visceral AA Amyloidosis in slaughtered cattle in this study was disturbingly high compared with those (0.4-2.7%) previously reported from Japan and other foreign countries. AA Amyloidosis is a life-threatening complication in patients with chronic inflammatory diseases and these patients at risk should avoid ingesting food that may possibly contain AA amyloid fibrils. More detailed information on cattle Amyloidosis is required to guarantee the safety of our food.
Naotaka Ishiguro - One of the best experts on this subject based on the ideXlab platform.
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Experimental transmission of systemic AA Amyloidosis in autoimmune disease and type 2 diabetes mellitus model mice.
Experimental animals, 2016Co-Authors: Mayuko Maeda, Tomoaki Murakami, Yasuo Inoshima, Naeem Muhammad, Naotaka IshiguroAbstract:AA Amyloidosis is a protein misfolding disease characterized by extracellular deposition of amyloid A (AA) fibrils. AA Amyloidosis has been identified in food animals, and it has been postulated that AA Amyloidosis may be transmissible to different animal species. Since the precursor protein of AA fibrils is serum amyloid A (SAA), which is an inflammatory acute phase protein, AA Amyloidosis is considered to be associated with inflammatory diseases such as rheumatoid arthritis. Chronic diseases such as autoimmune disease and type 2 diabetes mellitus could be potential factors for AA Amyloidosis. In this study, to examine the relationship between the induction of AA Amyloidosis and chromic abnormalities such as autoimmune disease or type 2 diabetes mellitus, amyloid fibrils from mice, cattle, or chickens were experimentally injected into disease model mice. Wild-type mice were used as controls. The concentrations of SAA, IL-6, and IL-10 in autoimmune disease model mice were higher than those of control mice. However, induction of AA Amyloidosis in autoimmune disease and type 2 diabetes mellitus model mice was lower than that in control mice, and the amount of amyloid deposits in the spleens of both mouse models was lower than that of control mice according to Congo red staining and immunohistochemistry. These results suggest that factors other than SAA levels, such as an inflammatory or anti-inflammatory environment in the immune response, may be involved in amyloid deposition.
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Systemic AA Amyloidosis as a prion-like disorder.
Virus research, 2014Co-Authors: Tomoaki Murakami, Yasuo Inoshima, Naotaka IshiguroAbstract:Amyloidosis is a collective term for a group of disorders that induce functional impairment of organs and occurs through the accumulation of amyloid, or misfolded protein in beta-sheets. AA Amyloidosis is a lethal systemic Amyloidosis with SAA as the precursor protein, and is observed in various animal species, including humans. AA Amyloidosis can be induced artificially by continuously administering inflammatory stimuli in experimental animal models. In this process of experimental induction, the administration of AA amyloids from either the same or different species is known to markedly expedite AA Amyloidosis development, and this is also termed transmission of AA Amyloidosis. Similarly to prion disease, AA Amyloidosis is considered to be transmitted via a "seeding-nucleation" process. In this manuscript, we reviewed the pathology and transmissibility of AA Amyloidosis in animals.
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Transmission of Systemic AA Amyloidosis in Animals
Veterinary pathology, 2013Co-Authors: Tomoaki Murakami, Naotaka Ishiguro, K. HiguchiAbstract:Amyloidoses are a group of protein-misfolding disorders that are characterized by the deposition of amyloid fibrils in organs and/or tissues. In reactive amyloid A (AA) Amyloidosis, serum AA (SAA) protein forms deposits in mice, domestic and wild animals, and humans that experience chronic inflammation. AA amyloid fibrils are abnormal β-sheet–rich forms of the serum precursor SAA, with conformational changes that promote fibril formation. Extracellular deposition of amyloid fibrils causes disease in affected animals. Recent findings suggest that AA Amyloidosis could be transmissible. Similar to the pathogenesis of transmissible prion diseases, amyloid fibrils induce a seeding-nucleation process that may lead to development of AA Amyloidosis. We review studies of possible transmission in bovine, avian, mouse, and cheetah AA Amyloidosis.
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AA Amyloidosis in vaccinated growing chickens.
Journal of comparative pathology, 2013Co-Authors: Tomoaki Murakami, Yasuo Inoshima, E. Sakamoto, Hideto Fukushi, Hiroki Sakai, Tokuma Yanai, Naotaka IshiguroAbstract:Systemic amyloid-A (AA) Amyloidosis in birds occurs most frequently in waterfowl such as Pekin ducks. In chickens, AA Amyloidosis is observed as amyloid arthropathy. Outbreaks of systemic Amyloidosis in flocks of layers are known to be induced by repeated inflammatory stimulation, such as those resulting from multiple vaccinations with oil-emulsified bacterins. Outbreaks of fatal AA Amyloidosis were observed in growing chickens in a large scale poultry farm within 3 weeks of vaccination with multiple co-administered vaccines. This study documents the histopathological changes in tissues from these birds. Amyloid deposits were also observed at a high rate in the tissues of apparently healthy chickens. Vaccination should therefore be considered as a potential risk factor for the development of AA Amyloidosis in poultry.
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Experimental induction and oral transmission of avian AA Amyloidosis in vaccinated white hens.
Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis, 2013Co-Authors: Tomoaki Murakami, Yasuo Inoshima, Tokuma Yanai, Naeem Muhammad, Masanobu Goryo, Naotaka IshiguroAbstract:AbstractAvian AA Amyloidosis is commonly observed in adult birds afflicted with bacterial infections or chronic inflammatory disorders. Experimental AA Amyloidosis in birds can be induced by repeated inflammatory stimulation, such as injection with casein or vaccination with oil-emulsified bacterins. However, the transmission of Amyloidosis among avian species has not been studied well to date. In the present study, we confirm the potential induction of avian AA Amyloidosis by inoculation of Salmonella enteritidis (SE) vaccine or Mycoplasma gallisepticum vaccine. To determine the transmission of chicken AA Amyloidosis among white hens, we induced experimental AA Amyloidosis in vaccinated chickens by intravenous or oral administration of chicken AA fibrils. Amyloid deposits were observed in chickens injected with SE and inoculated with chicken AA fibrils intravenously (21/26: 81%) and orally (8/12: 67%). These results suggest that chicken AA Amyloidosis can be induced by vaccinations, and may be transmitte...
