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737 results on '"Wisniewski T."'

58. Amyloid-beta immunisation for Alzheimer's disease

Author

Wisniewski, T, Konietzko, U, University of Zurich, and Wisniewski, T

Subjects
2728 Neurology (clinical), 610 Medicine & health, 11359 Institute for Regenerative Medicine (IREM)
Published
2008

64. Pain Functional Impairment and Quality of Life (P-FIQ): an assessment of reliability of five patient reported outcome (PRO) instruments in Adult People with Hemophilia (PWH)

Author

Kempton, C.L., primary, Wang, M., additional, Recht, M., additional, Neff, A., additional, Shapiro, A.D., additional, Buckner, T., additional, Kulkarni, R., additional, Nugent, D., additional, Batt, K., additional, Wisniewski, T., additional, and Cooper, D.L., additional

Published
2015
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68. Light and electron microscopic immunolocalization of presenilin 1 in abnormal muscle fibers of patients with sporadic inclusion-body myositis and autosomal-recessive inclusion-body myopathy

Author

Askanas, V., Engel, W. K., Chih-Chao Yang, Alvarez, R. B., Lee, V. M. -Y, and Wisniewski, T.

Subjects
Adult, education, mental disorders, Muscle Fibers, Skeletal, Presenilin-1, Humans, Membrane Proteins, Middle Aged, Microscopy, Immunoelectron, Immunohistochemistry, Research Article, Aged, Myositis, Inclusion Body
Abstract

Sporadic inclusion-body myositis (s-IBM) is the most common progressive muscle disease of older persons. The muscle biopsy demonstrates mononuclear cell inflammation and vacuolated muscle fibers containing paired helical filaments and 6- to 10-nm fibrils, both resembling those of Alzheimer disease brain and Congo red positivity. The term hereditary inclusion-body myopathies (h-IBMs) designates autosomal-recessive or autosomal-dominant disorders with muscle biopsies cytopathologically similar to s-IBM but without inflammation. Vacuolated muscle fibers of both s-IBM and the h-IBMs contain accumulations of several "Alzheimer-characteristic proteins" including beta-amyloid protein and beta-amyloid precursor protein, and their paired helical filaments are composed of phosphorylated tau. We used six well characterized antibodies against several residues of presenilin 1 (PS1) to immunostain muscle biopsies of 12 patients with s-IBM, 5 patients with autosomal-recessive inclusion-body myopathy, and 16 normal and disease controls. Seventy to eighty percent of the vacuolated muscle fibers of both s-IBM and autosomal-recessive inclusion-body myopathy had inclusions that were strongly PS1-immunoreactive, which by immunoelectron microscopy localized mainly to paired helical filaments and 6- to 10-nm filaments. None of the control biopsies had PS1-positive inclusions characteristic of the s- and h-IBM abnormal muscle fibers. Mutations of the newly discovered PS1 gene are responsible for early-onset familial Alzheimer disease (AD), and PS1 is abnormally accumulated in sporadic and familial AD brain. Our study provides the first demonstration of PS1 abnormality in non-neural tissue and in diseases other than AD and suggests that the cytopathogenesis in AD brain and IBM muscle may share similarities.

Published
1998

71. Meningocerebrovascular amyloidosis associated with a novel transthyretin mis-sense mutation at codon 18 (TTRD 18G)

Author

Vidal, R., Garzuly, F., Herbert Budka, Lalowski, M., Linke, R. P., Brittig, F., Frangione, B., and Wisniewski, T.

Subjects
Amyloid, Cerebral Amyloid Angiopathy, Meninges, Genotype, mental disorders, Mutation, nutritional and metabolic diseases, Humans, Prealbumin, Amyloid Neuropathies, nervous system diseases, Research Article, Genes, Dominant
Abstract

We describe a novel transthyretin mutation at codon 18 where Asp is replaced by Gly (D18G) in a Hungarian kindred. This mutation is associated with meningocerebrovascular amyloidosis, producing dementia, ataxia, and spasticity. Fifty different transthyretin mutations are related to amyloid deposition, typically producing a peripheral neuropathy or cardiac dysfunction. These symptoms are absent in this family. Up to now, amyloid-beta (A beta), cystatin C, and prion proteins have been known to be deposited as amyloid in the brain, leading to stroke or dementia. With this report we establish that transthyretin amyloid deposition can also produce central nervous system dysfunction as the major clinical symptom.

Published
1996

79. Conformational mimicry in Alzheimer's disease. Role of apolipoproteins in amyloidogenesis

Author

Wisniewski, T., Golabek, A. A., Kida, E., Wisniewski, K. E., and Frangione, B.

Subjects
Amyloid, Microscopy, Electron, Apolipoproteins, Apolipoprotein A-I, Alzheimer Disease, mental disorders, Molecular Mimicry, Molecular Conformation, Humans, lipids (amino acids, peptides, and proteins), Congo Red, Immunohistochemistry, Research Article
Abstract

Several apolipoproteins are known to be closely associated with amyloid fibrillogenesis. Serum amyloid A, apolipoprotein (apo) AII and apo A1 are each deposited as biochemically distinct forms of amyloid. Late-onset Alzheimer's disease is linked to one isotype of apo E, apo E4. Apo E and apo E4 in particular have been shown to modulate amyloid fibril formation by amyloid-beta peptides in vitro. Furthermore, the carboxy terminus of apo E has been shown to be a constituent of plaque amyloid. We show immunohistochemically and electron microscopically the presence of apo A1 in senile plaques. The intact apo A1 can itself form amyloid-like fibrils in vitro that are Congo Red positive. We propose that some proteins when misfolded can propagate this misfolding to identical units, either autocatalytically or to other proteins that are induced to fold into the same abnormal conformation. This conformational mimicry may initiate and/or augment fibrillogenesis in Alzheimer's disease.

Published
1995

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