Dialysis-Associated Amyloidosis

Drüeke, Tilman B.; Touam, Malik; Zingraff, J.

doi:10.1016/s1073-4449(12)80069-0

Cited by 15 publications

(7 citation statements)

References 96 publications

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“…THP-1 cells (∼10 6 ), seeded on six-well plates or 60-mm dishes, were transfected with pre-miR-214 or miR-214 ASOs using Lipofectamine 2000 (Invitrogen), according to the manufacturer's instructions (22). For miR-214 overexpression, 100 pmol pre-miR-214 or scrambled control oligonucleotide was used.…”

Section: Overexpression or Knockdown Of Mir-214mentioning

confidence: 99%

Role of MicroRNA-214–Targeting Phosphatase and Tensin Homolog in Advanced Glycation End Product-Induced Apoptosis Delay in Monocytes

Liu

Hou

Guo

et al. 2011

The Journal of Immunology

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Advanced glycation end products (AGEs) delay spontaneous apoptosis of monocytes and contribute to the development of inflammatory responses. However, the mechanism by which AGEs affect monocyte apoptosis is unclear. We studied the role of microRNA-214 (miR-214) and its target gene in AGE-induced monocytic apoptosis delay. Using microRNA (miRNA) microarray and stem-loop, quantitative RT-PCR assay, we studied genome-wide miRNA expression in THP-1 cells treated with or without AGEs. Significant upregulation of miR-214 was consistently observed in THP-1 and human monocytes treated with various AGEs, and AGE-induced monocytic miR-214 upregulation was likely through activation of receptor for AGEs. A striking increase in miR-214 was also detected in monocytes from patients with chronic renal failure. Luciferase reporter assay showed that miR-214 specifically binds to the phosphatase and tensin homolog (PTEN) mRNA 3′-untranslated region, implicating PTEN as a target gene of miR-214. PTEN expression is inversely correlated with miR-214 level in monocytes. Compared with normal monocytes, AGE-treated monocytes and monocytes from chronic renal failure patients exhibited lower PTEN levels and delayed apoptosis. Overexpression of pre–miR-214 led to impaired PTEN expression and delayed apoptosis of THP-1 cells, whereas knockdown of miR-214 level largely abolished AGE-induced cell survival. Our findings define a new role for miR-214–targeting PTEN in AGE-induced monocyte survival.

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Section: Overexpression or Knockdown Of Mir-214mentioning

confidence: 99%

Role of MicroRNA-214–Targeting Phosphatase and Tensin Homolog in Advanced Glycation End Product-Induced Apoptosis Delay in Monocytes

Liu

Hou

Guo

et al. 2011

The Journal of Immunology

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“…This is reflected by the number of scientific publications issued on amyloid; according to a search in Medline, 298 publications were registered in 1985, while in 1995 the number ascended p 1068. Moreover, amyloid has been associated nith other diseases such as adult onset diabetes (Lorenzo & Yankner, 1996), dialysis-associated arnropathy (Drueke et al, 1995), chronic inflammatory diseases (Perez-Villa et al, 1989), tumours and familial neuropathies. These findings further contributed to the increased interest in studying me pathology of amyloids, in general, and the mec ¡llanisrris governing amyloid fibrillogenesis in particular.…”

Section: Definition and Historymentioning

confidence: 99%

Avian amyloidosis

Landman¹,

Gruys

Gielkens

1998

Avian Pathology

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Although amyloid deposits have been described for more than a century and a half, its proteinaceous and fibrillar nature was not revealed until after 1950. Biochemical characterization of amyloids has brought to light that several non-related proteins can re-organize into amyloid fibrils. In some domestic and caged wild birds, and especially waterfowl, amyloidosis is a well recognized pathological disorder and is an important cause of death in Anseriformes. Its regular occurrence in Galliformes has been recognized more recently, where amyloid deposits occur mainly in the joints in contrast to other species studied so far. Avian amyloidosis is systemic in nature, being classified by amino acid sequencing and, monoclonal and polyclonal antibodies as of the AA-type amyloid, also named reactive or secondary amyloid. The pathogenesis of both AA and other types of amyloidosis is a complex phenomenon that is not well understood. It has been shown that the occurrence of certain predisposing conditions and chronic infections, inflammations or tumours increase strongly the serum levels of the hepatic acute phase reactant serum amyloid A (SAA), the precursor protein of amyloid protein A (AA). Although an increased pool of precursor protein is necessary for amyloid to develop and while certain amino acid substitutions may favour amyloidogenicity giving rise to unstable intermediate protein conformations that easily re-organize into fibrils, the action of other factors which are discussed in this review, seems of vital importance at the initiation of fibrillogenesis. As the clinical symptoms of amyloidosis generally are non-specific, diagnosis requires histopathology following biopsy or necropsy. AA-amyloidosis is a fatal progressive disease in birds and other species. Currently no curative treatment is available, therefore special attention should be paid to prevention focusing on hygiene and avoidance of stress.

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confidence: 99%

“…␤2-microglobulin amyloidosis (A␤ 2 m) is a progressive and incapacitating comorbid condition affecting patients with chronic renal failure [1][2][3]. Amyloid deposits are predominantly found in tendons, synovium, and bone, resulting in shoulder periarthritis, hand flexor tenosynovitis, carpal tunnel syndrome, destructive spondyloarthropathy, and cystic bone lesions [1][2][3]. Recent biochemical and immunochemical studies have demonstrated that ␤2-microglobulin modified with advanced glycation end products (␤ 2 m-AGE) is a major component of the amyloid fibrils in A␤ 2 m [4].…”

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confidence: 99%

β2-microglobulin modified with advanced glycation end products modulates collagen synthesis by human fibroblasts

Owen¹,

Hou²,

Stuart³

et al. 1998

Kidney International

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Beta 2-microglobulin amyloidosis (A beta 2m) is a serious complication for patients undergoing long-term dialysis. beta 2-microglobulin modified with advanced glycation end products (beta 2m-AGE) is a major component of the amyloid in A beta 2m. It is not completely understood whether beta 2m-AGE plays an active role in the pathogenesis of A beta 2m, or if its presence is a secondary event of the disease. beta 2-microglobulin amyloid is mainly located in tendon and osteo-articular structures that are rich in collagen, and local fibroblasts constitute the principal cell population in the synthesis and metabolism of collagen. Recent identification of AGE binding proteins on human fibroblasts lead to the hypothesis that the fibroblast may be a target for the biological action of beta 2m-AGE. The present study demonstrated that two human fibroblast cell lines exhibited a decrease in procollagen type I mRNA and type I collagen synthesis after exposure to beta 2m-AGE for 72 hours. Similar results were observed using AGE-modified albumin. Antibody against the RAGE, the receptor for AGE, attenuated this decrease in synthesis, indicating that the response was partially mediated by RAGE. In addition, antibody against epidermal growth factor (EGF) attenuated the decrease in type I procollagen mRNA and type I collagen induced by beta 2m-AGE, suggesting that EGF acts as an intermediate factor. These findings support the hypothesis that beta 2m-AGE actively participates in connective tissue and bone remodeling via a pathway involving fibroblast RAGE, and at least one interposed mediator, the growth factor EGF.

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Dialysis-Associated Amyloidosis

Cited by 15 publications

References 96 publications

Role of MicroRNA-214–Targeting Phosphatase and Tensin Homolog in Advanced Glycation End Product-Induced Apoptosis Delay in Monocytes

Role of MicroRNA-214–Targeting Phosphatase and Tensin Homolog in Advanced Glycation End Product-Induced Apoptosis Delay in Monocytes

Avian amyloidosis

β2-microglobulin modified with advanced glycation end products modulates collagen synthesis by human fibroblasts

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