Immunofluorescence study of “Non-idiopathic” renal amyloidosis

Orfila, Caludine; Rakotoarivony, J; Segonds, A; Suc, J. M.

doi:10.1016/s0046-8177(83)80123-3

Cited by 13 publications

(1 citation statement)

References 18 publications

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“…The presence of early complement factors C1q and C3 has been described in lichen amyloidosis [61,62], several forms of renal amyloidosis [63,64] and amyloid AL neuropathy [65]. The authors of these studies state that the relevance of these complement factors for the formation of the amyloid deposits is yet unclear, but they suggest that their presence represents probably a nonessential absorption and that amyloid material could act as a filamentous sponge [62,66].…”

Section: Microgliamentioning

confidence: 99%

The Neuroinflammatory Response in Plaques and Amyloid Angiopathy in Alzheimers Disease: Therapeutic Implications

2005

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The amyloid plaques in Alzheimer's disease (AD) brains are co-localised with a broad variety of inflammation-related proteins (complement proteins, acute-phase proteins, pro-inflammatory cytokines) and clusters of activated microglia. The present data suggest that the Abeta depositions in the neuroparenchyma are closely associated with a locally-induced, non-immune-mediated chronic inflammatory response. Clinicopathological and neuroradiological data show that activation of microglia are a relatively early pathogenic event that precedes the process of severe neuropil destruction in patients. Recent gene findings (cDNA microarray) confirm the immunohistochemical findings of an early involvement of inflammatory and regenerative pathways in AD pathogenesis. Abeta deposition, inflammation and regenerative mechanisms are also early pathogenic events in transgenic mice models harbouring the pathological AD mutations, while "later" neurodegenerative characteristics are not seen in these models. Next to the plaques, Abeta amyloid deposition is frequently found in the walls of cerebral vessels (cerebral amyloid angiopathy). Most common is the type of amyloid deposition in the walls of meningeal and medium-sized cortical arteries, and more rarely, microcapillary amyloid angiopathy (dyshoric angiopathy). Immunohistochemical studies show that in AD patients, the majority of the amyloid deposits in the walls of the larger vessels is not associated with a chronic inflammatory response in contrast to micro-capillary amyloid angiopathy. In this contribution, we will give an overview of the similarities and differences between the involvement of inflammatory mechanisms in vascular and plaque amyloid in AD and transgenic models. The implications of the reviewed studies for an inflammation-based therapeutical approach in AD will be discussed.

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Section: Microgliamentioning

confidence: 99%

The Neuroinflammatory Response in Plaques and Amyloid Angiopathy in Alzheimers Disease: Therapeutic Implications

2005

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Ultrastructural evidence for colocalization of ? light chain-and ?2-microglobulin-derived amyloids using double labelling immunogold electron microscopy

Takahashi

Hoshii

Kawano

et al. 1996

Vichows Archiv A Pathol Anat

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In systemic amyloidosis, it is essential to decide what type of amyloid protein is deposited in tissues before the therapy can be selected and the prognosis assessed in each patient. We examined tissues affected by amyloid deposition from a patient with multiple myeloma by immunohistochemistry and double labelling immunogold electron microscopy and demonstrated colocalization of kappa light chain- and beta 2-microglobulin-derived amyloids in the same tissue. beta 2-Microglobulin-derived amyloid had ultrastructurally characteristic features that distinguished it from kappa light chain-derived amyloid. This is the first report of the colocalization of two different amyloids by immunoelectron microscopy.

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Diagnosis of the type of amyloid in paraffin wax embedded tissue sections using antisera against human and animal amyloid proteins

Kaa

Hol

Huber

et al. 1986

Vichows Archiv A Pathol Anat

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Different histochemical techniques were compared on paraffin wax embedded tissue sections for routine classification of amyloid; the following methods were used: potassium permanganate, the indirect immunoperoxidase method using polyclonal anti-human amyloid antisera (anti-AA, anti-A lambda, anti-A kappa and anti-AF) and the peroxidase-antiperoxidase (PAP) method using antisera against human, bovine, hamster and canine AA amyloid. Anti-human AA antiserum appeared to be a useful tool in this respect. Polyclonal anti-AL antisera may be helpful in diagnosing AL amyloid, but were less of value than anti-AA serum. Strong cross reactivity between anti-bovine AA antiserum and human AA amyloid deposits was found. This indicates that animal amyloid AA antisera can also be used for the diagnosis of AA amyloid in human tissues.

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Immunofluorescence study of “Non-idiopathic” renal amyloidosis

Cited by 13 publications

References 18 publications

The Neuroinflammatory Response in Plaques and Amyloid Angiopathy in Alzheimers Disease: Therapeutic Implications

The Neuroinflammatory Response in Plaques and Amyloid Angiopathy in Alzheimers Disease: Therapeutic Implications

Ultrastructural evidence for colocalization of ? light chain-and ?2-microglobulin-derived amyloids using double labelling immunogold electron microscopy

Diagnosis of the type of amyloid in paraffin wax embedded tissue sections using antisera against human and animal amyloid proteins

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