نتایج جستجو برای: ocular amyloidosis
تعداد نتایج: 66866 فیلتر نتایج به سال:
Amyloidosis includes a spectrum of diseases that involve the deposition of misfolded proteins in various tissues throughout the body. There are many different proteins known to cause amyloidosis and the etiology of the amyloid subtype determines where the abnormal proteins deposit. AL, ATTRwt (formerly senile systemic amyloidosis), and ATTRm (formerly familial amyloidosis) are the most common a...
Abstract Background Bone scintigraphy is extremely valuable when assessing patients with suspected cardiac amyloidosis (CA), but the clinical significance and associated phenotype of different degrees myocardial tracer uptake across types yet to be defined. Purpose We sought define phenotypes varying on bone scintigraphy, multiple systemic using extensive characterisation comprising biomarkers,...
Amyloidosis cutis dyschromica is a rare type of primary cutaneous amyloidosis characterized by reticulate hyper-pigmentation with discrete hypopigmented macules. Up to date, about 50 cases of amyloidosis cutis dyschromica have been reported and the majority are familial cases of Asian ethnicity. Various diseases, particularly autoimmune diseases such as systemic sclerosis and systemic lupus ery...
In several families, multiple endocrine neoplasia type 2A (MEN 2A) has been found in association with cutaneous lichen amyloidosis. It has been debated, however, whether the skin amyloidosis found in MEN 2A families, localized exclusively in the interscapular area, represents the same anomaly as that found in autosomal dominant familial cutaneous lichen amyloidosis, which is more generalized. W...
OBJECTIVE To clarify the clinical significance of the SAA1.3 allele in the development and outcome of AA amyloidosis in Japanese patients with rheumatoid arthritis (RA). METHODS One hundred and twenty RA patients (60 alive and 60 dead) fulfilling the 1987 ACR criteria and 62 RA patients with biopsy-confirmed amyloid A (AA) amyloidosis (36 alive and 26 dead) were enrolled. The SAA1 genotypes w...
protein aggregation is a serious problem for both biotechnology and cell biology. diseases such as prion misfolding, alzheimer’s, and other amyloidosis are phenomena for which protein aggregation in our living cells is of considerable relevance. human lysozyme has been shown to form amyloid fibrils in individuals suffering from nonneuropathic systemic amyloidosis, all of which have point mutati...
BACKGROUND Systemic amyloidoses include immunoglobulin light chain (AL) amyloidosis, serum amyloid (AA)-related amyloidosis and senile systemic amyloidosis (SSA). AL amyloidosis is associated with myeloma, and we showed recently that transthyretin-related hereditary amyloidosis was related to non-Hodgkin lymphoma (NHL). In SSA, amyloids constitute wild-type transthyretin. We wanted to analyze c...
The amyloidoses are a group of protein-misfolding disorders characterized by the accumulation of amyloid fibrils formed from a variety of proteins. Currently, twentyeight different kinds of human and animal proteins, in intact or fragmented forms, have been found to be associated with pathological disorders such as Alzheimer’s disease, type II diabetes, prion diseases, dialysis-related amyloido...
The median survival in primary systemic (AL) amyloidosis is less than 18 months. No published series of patients with AL amyloidosis have reported survival of more than 10 years. The records of all Mayo Clinic patients with a diagnosis of AL amyloidosis between January 1, 1966 and March 1, 1987 were reviewed. Patients with secondary amyloidosis, familial amyloidosis, senile systemic amyloidosis...
Amyloidosis is a rare, mysterious and serious disorder. The extracellular deposition of seemingly homogenous and amorphous material actually represents the expression of very diverse pathologies. All amyloid fibrils share apple green birefringence under polarized light with Congo-red staining, and are arranged in beta-pleated structure on electron microscopy. More than 21 proteins have been ide...
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