Biomaterial Database

Systemic amyloidosis associated with factor X deficiency. 1984

H Shibuya, and N Azumi, and F Abe, and M Deno, and S Sakurama

An autopsy case of amyloidosis associated with factor X deficiency is reported. The patient showed a markedly decreased level of factor X (9% normal) and an extremely shortened half-life of intravenously infused factor X. Amyloid deposition was present in most of the visceral organs with special involvement of the liver and spleen. The amyloid in this case was thought to be AL protein, since it was potassium-permanganate-resistant and a small amount of Bence Jones protein was detected after dimethyl sulfoxide therapy. Electron microscopic study revealed a typical appearance of amyloid fibrils radiating from invaginated cell membrane of Kupffer cells, which may indicate rather rapid turnover of the amyloid. Rapidity and severity of amyloid deposition, especially in the liver and spleen, may play an important role in the development of the factor X deficiency associated with systemic amyloidosis.

UI	MeSH Term	Description	Entries
D007020	Hypoprothrombinemias	Absence or reduced levels of PROTHROMBIN in the blood.	Factor II Deficiency,Prothrombin Deficiency,Deficiency, Factor II,Hypoprothrombinemia,Deficiencies, Factor II,Deficiencies, Prothrombin,Deficiency, Prothrombin,Factor II Deficiencies,Prothrombin Deficiencies
D007728	Kupffer Cells	Specialized phagocytic cells of the MONONUCLEAR PHAGOCYTE SYSTEM found on the luminal surface of the hepatic sinusoids. They filter bacteria and small foreign proteins out of the blood and dispose of worn out red blood cells.	Kupffer Cell,Cell, Kupffer,Cells, Kupffer
D008099	Liver	A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.	Livers
D008297	Male		Males
D008875	Middle Aged	An adult aged 45 - 64 years.	Middle Age
D005171	Factor X Deficiency	Blood coagulation disorder usually inherited as an autosomal recessive trait, though it can be acquired. It is characterized by defective activity in both the intrinsic and extrinsic pathways, impaired thromboplastin time, and impaired prothrombin consumption.	Deficiency, Factor 10,Deficiency, Factor Ten,Deficiency, Factor X,Deficiency, Stuart-Prower,Deficiency, Stuart-Prower Factor,Factor 10 Deficiency,Factor Ten Deficiency,Stuart-Prower Deficiency,Stuart-Prower Factor Deficiency,Deficiencies, Factor 10,Deficiencies, Factor Ten,Deficiencies, Factor X,Deficiency, Stuart Prower,Deficiency, Stuart Prower Factor,Factor 10 Deficiencies,Factor Ten Deficiencies,Factor X Deficiencies,Stuart Prower Deficiency,Stuart Prower Factor Deficiency,Ten Deficiencies, Factor
D006801	Humans	Members of the species Homo sapiens.	Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000682	Amyloid	A fibrous protein complex that consists of proteins folded into a specific cross beta-pleated sheet structure. This fibrillar structure has been found as an alternative folding pattern for a variety of functional proteins. Deposits of amyloid in the form of AMYLOID PLAQUES are associated with a variety of degenerative diseases. The amyloid structure has also been found in a number of functional proteins that are unrelated to disease.	Amyloid Fibril,Amyloid Fibrils,Amyloid Substance,Fibril, Amyloid,Fibrils, Amyloid,Substance, Amyloid
D000686	Amyloidosis	A group of sporadic, familial and/or inherited, degenerative, and infectious disease processes, linked by the common theme of abnormal protein folding and deposition of AMYLOID. As the amyloid deposits enlarge they displace normal tissue structures, causing disruption of function. Various signs and symptoms depend on the location and size of the deposits.	Amyloidoses