نتایج جستجو برای: amyloidosis
تعداد نتایج: 11011 فیلتر نتایج به سال:
Introduction: Amyloid diseases have been known to be hereditary, including transthyretin (TTR) amyloidosis where subunit protein mutations may occur in genes for TTR leading to the deposition of fibrils (low molecular weight subunits (5 to 25 kD) of proteins) in extracellular tissues. By reducing the formation of TTR amyloid, diflunisal, a nonsteroidal anti-inflammatory drug (NSAID), has shown ...
Amyloid is an eosinophilic substance which appears “apple-green birefringence” in Congo red stained tissue sections under polarized light. This standard histological analysis is supported with immunochemistry technic using specific antibodies directed against most of the common human amyloid proteins, and also amyloid proteins can be identified with characteristic fibrillar appearance by electr...
Immunoglobulin-derived light chain amyloidosis can occasionally be associated with localized disease. We present a patient with localized lymph node light chain amyloidosis without an underlying monoclonal protein or lymphoproliferative disorder and review the literature of lymph node amyloidosis discussing work-up and risk factors for systemic progression.
Background Cardiac MRI (CMR) is increasingly used to further investigate patients in whom amyloidosis is suspected on echocardiography. Late gadolinium enhancement (LGE) reflects expansion of the interstitium, and circumferential subendocardial LGE has been reported to be a typical finding in AL amyloidosis; by contrast, a more diffuse transmural LGE pattern has been associated with ATTR (trans...
BACKGROUND AL amyloidosis is an acquired systemic disease in which a pathologic amorphous substance produced as a result of abnormal protein metabolism is deposited in the extracellular space of various tissues. OBJECTIVES The aim of the study was to investigate the relationship between the kappa and lambda serum free light chains (sFLCs) and the development of AL amyloidosis in patients suff...
position of insoluble fibrillar proteins in various organs [1]. In humans, more than 23 different and unrelated proteins are known to form amyloid fibrils [2]. Amyloidosis is divided into primary (i. e. idiopathic) and secondary amyloidosis (i. e. associated with chronic inflammatory conditions, and infectious and neoplastic disorders) [1]. Primary amyloidosis is extremely rare in the gastroint...
Amyloidosis of the gastrointestinal tract, with biopsy-proven disease, is rare. We reviewed a series of patients who presented with biopsy-proven gastrointestinal amyloidosis and report their clinical characteristics, treatments, and survival. This is a retrospective review of data prospectively collected from January 1998 to December 2011 in a tertiary referral center; 2,334 patients with all ...
Amyloid A (AA) amyloidosis, a fatal systemic amyloid disease, occurs secondary to chronic inflammatory conditions in humans. Although persistently elevated serum amyloid A (SAA) levels are required for its pathogenesis, not all individuals with chronic inflammation necessarily develop AA amyloidosis. Furthermore, many diseases in cats are associated with the elevated production of SAA, whereas ...
Cardiac amyloidosis is a prognostically critical condition, since it is a frequent cause of death in patients with systemic amyloidosis. Lee et al. reported, for the first time, describing systemic amyloidosis in Korea from the perspective of cardiologists. In this paper, the authors enrolled 129 systemic amyloidosis patients retrospectively from 1999 to 2011. They showed that cardiac involve w...
AMA Milewska J, Małachowska U, Czuwara Rudnicka L, Olszewska M. Lichen amyloidosis. Dermatology Review/Przegląd Dermatologiczny. 2023;110(1):37-42. doi:10.5114/dr.2023.127656. APA Milewska, J., Małachowska, U., Czuwara, Rudnicka, L., & Olszewska, (2023). Dermatologiczny, 110(1), 37-42. https://doi.org/10.5114/dr.2023.127656 Chicago Justyna, Urszula Joanna Lidia and Małgorzata Olszewska. 2023. "...
نمودار تعداد نتایج جستجو در هر سال
با کلیک روی نمودار نتایج را به سال انتشار فیلتر کنید