amyloid/dental caries

We report here a case of mucosa-associated lymphoid tissue (MALT)-type lymphoma arising from the minor salivary gland of the oral cavity exhibiting tumor-forming amyloidosis. The patient was a 64-year-old Japanese woman who presented with 4-year history of a left soft palate mass. Despite multiple

The frequency of amyloid deposits associated with squamous cell carcinoma (SCC) and dysplasia in the oral cavity, pharynx and larynx was examined. In addition, the origin of amyloid proteins by immunohistochemical staining with a panel of anticytokeratin monoclonal antibodies was investigated.

Differential hydration dictates various biological processes, including protein folding, ligand binding, macromolecular assembly, enzyme kinetics and signal transduction. If water is partially or totally removed (experimentally or in silico), the outcome of these processes can be significantly

After a brief examination of the most modern conceptions relating to amyloidosis desease a case of sistemic amyloidosis localized in the oral cavity is presented by the authors. An iconografic series of the lesions affecting the mucous membrane of the lips, checks and tongue is meant to contribute

Bullous amyloidosis (BA) is a rare cutaneous manifestation primarily of systemic amyloidosis, a disease in which abnormal proteinaceous material is formed and deposited in response to inflammatory conditions and plasma cell dyscrasias. Hemorrhagic bullae indicative of BA are usually associated with

Five cases of amyloidosis involving structures in the oral cavity are reported. Three cases appeared to be secondary systemic amyloidosis, one case was the systemic form associated with multiple myeloma, and one case appeared to represent nodular or localized amyloidosis. All cases appeared in

Localized amyloidosis is an uncommon benign disorder. The purpose of this report is to present the case of a 21-year-old man who had localized amyloidosis simultaneously involving the sinonasal cavities and the larynx. The rarer sinonasal lesion demonstrated CT findings of adjacent "fluffy" bone

We examined the distribution patterns of human β-amyloid (1-40) peptide labeled with iodine 125 ((125)I-Aβ40) after injections into the cerebral ventricle or tail vein of rats. In rats receiving an intravenous injection, the radioactive concentration of (125)I-Aβ40 in the nasal area was similar to

OBJECTIVE A retrospective study was conducted to investigate the anatomic location and characteristics of amyloid deposition in the oral cavity. METHODS Seventeen biopsy specimens that were conclusive for a diagnosis of amyloidosis were assessed in terms of their anatomic location and

BACKGROUND Cardiac amyloidosis (CA) is a myocardial disease and commonly under-diagnosed condition. In CA patients, atrial fibrillation might occur in the absence of left atrial (LA) enlargement. OBJECTIVE The aim of this study is to assess LA size and function, and its relationship with atrial

Alzheimer's disease (AD) is associated with the aggregation of amyloid-β (Aβ) peptides into toxic fibrillar aggregates. Finding effective inhibitors of Aβ aggregation is a crucial step for the development of drugs against AD. Recent experiments reported that dihydrochalcone (Dih), a compound

A patient with lesions of the oral mucosa is presented. Biopsy of the lesions showed deposits of amyloid, which lead to further examination of the patient, revealing a generalized amyloidosis.

BACKGROUND Amyloidosis is a disease characterized by deposits of abnormal protein known as amyloid in various organs and tissues. It can be classified into systemic or localized forms, the latter of which is less frequent. Deposition of amyloidogenic monoclonal light chains leads to the most common

Elucidating the structure of Aβ(1-40) fibrils is of interest in Alzheimer's disease research because it is required for designing therapeutics that target Aβ(1-40) fibril formation at an early stage of the disease. M35 is a crucial residue because of its potential oxidation and its strong

The misfolding and self-assembly of human islet amyloid polypeptide (hIAPP or amylin) into amyloid fibrils is pathologically linked to type II diabetes. The polymorphic nature of both hIAPP oligomers and fibrils has been implicated for the molecular origin of hIAPP toxicity to islet β-cells, but