Primary cutaneous amyloidosis: A clinico-pathological study with emphasis on polarized microscopy.

Background: Primary localized cutaneous amyloidosis (PCA) is a relatively rare condition characterized by amyloid deposition in dermis without systemic involvement. Although, histopathological examination of the lesion reveals amorphous eosinophilic deposits in papillary dermis examination of congo red stained slides under polarized light will give definitive diagnosis Aims: To study the clinicopathological features of cutaneous amyloidosis emphasizing the utility of polarized light in diagnosis. Materials and Methods : A clinicopathological study of primary cutaneous amyloidosis over a period of 8 years was undertaken. All the cases, clinically diagnosed and histopathologically proven as cutaneous amyloidosis were stained with congo red and studied under polarized light. Results and Conclusions: Of the 45 cases of clinically suspected amyloidosis, 32 cases were proven histopathologically as primary cutaneous amyloidosis and confirmed by congo red stain under polarized light which showed apple green birefringence. Among the two types of PCA, lichen amyloidosis was the most common variant accounting to 65.63% with pure cases of macular amyloidosis accounting for only 15.63%. Biphasic amyloidosis was seen in 18.75%. Knee was the commonest site of involvement with pruritis being the most common symptom. Histopathologically, the most common findings were hyperkeratosis, irregular acanthosis and expansion of dermal papillae by amyloid deposits showing apple green birefringence under polarized microscope with congo red staining. Although, H and E stain gives a clue for the diagnosis of amyloid nevertheless congo red staining under polarized light forms a very sensitive and definitive method for confirmation.

Immunoglobulin light chain amyloidosis associated with multiple myeloma in a young patient: a case report / Amiloidosis de cadenas ligeras de asociada con mieloma múltiple en un paciente joven: reporte de un caso

The authors present an uncommon case of systemic amyloidosis associated with multiple myeloma in a 35-year old woman. Systemic amyloidosis commonly presents in association with clonal plasma cell proliferative disorders, and less frequently as secondary or of a hereditary origin. Amyloidosis is usually associated with multiple myeloma in older patients and frequently has an unfavourable prognosis.

Los autores presentan aquí un caso raro de amiloidosis sistémica asociado con mieloma múltiple en una mujer de 35 años de edad. La amiloidosis sistémica normalmente se presenta asociada con desórdenes proliferativos de las células plasmáticas clonales, y con menor frecuencia con origen secundario o hereditario. Amiloidosis se asocia normalmente con el mieloma múltiple en pacientes de mayor edad y frecuentemente tiene una prognosis desfavorable.

Stabilization of partially folded states in protein folding/misfolding transitions by hydrostatic pressure

In the last few years, hydrostatic pressure has been extensively used in the study of both protein folding and misfolding/aggregation. Compared to other chemical or physical denaturing agents, a unique feature of pressure is its ability to induce subtle changes in protein conformation, which allow the stabilization of partially folded intermediate states that are usually not significantly populated under more drastic conditions (e.g., in the presence of chemical denaturants or at high temperatures). Much of the recent research in the field of protein folding has focused on the characterization of folding intermediates since these species appear to be involved in a variety of disease-causing protein misfolding and aggregation events. The exact mechanisms of these biologicalphenomena, however, are still poorly understood. Here, we review recent examples of the use of hydrostatic pressure as a tool to obtain insight into the forces and energetics governing the productive folding or the misfolding and aggregation of proteins.

Interactions of laminin with the amyloid ß peptide: Implications for Alzheimer's disease

Extensive neuronal cell loss is observed in Alzheimer's disease. Laminin immunoreactivity colocalizes with senile plaques, the characteristic extracellular histopathological lesions of Alzheimer brain, which consist of the amyloid ß (Aß) peptide polymerized into amyloid fibrils. These lesions have neurotoxic effects and have been proposed to be a main cause of neurodegeneration. In order to understand the pathological significance of the interaction between laminin and amyloid, we investigated the effect of laminin on amyloid structure and toxicity. We found that laminin interacts with the Aß1-40 peptide, blocking fibril formation and even inducing depolymerization of preformed fibrils. Protofilaments known to be intermediate species of Aß fibril formation were also detected as intermediate species of laminin-induced Aß fibril depolymerization. Moreover, laminin-amyloid interactions inhibited the toxic effects on rat primary hippocampal neurons. As a whole, our results indicate a putative anti-amyloidogenic role of laminin which may be of biological and therapeutic interest for controlling amyloidosis, such as those observed in cerebral angiopathy and Alzheimer's disease

Senile systemic amyloidosis--a case report.

An 85 years old female presented with acute pain and weakness in left lower extremity and doppler evidence of femoropopliteal block was made which subsequently proved fatal. Necropsy revealed extensive amyloid deposition in the heart and amyloid angiopathy in rest of the organs.