Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0162871 (abdominal aortic aneurysm)
8,664 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Immunoglobulin G (IgG) from human aneurysmal aorta was used to partially purify an aortic protein with an apparent MW approximately 80 kDa. Amino acid sequencing of a tryptic digest revealed two sequences with homology to mouse tenascin-X. The autoimmune IgG was then shown to react with purified human tenascin, and a rabbit polyclonal anti-human tenascin antibody was found to react with the purified autoantigen. These observations suggest that the autoantigen of abdominal aortic aneurysm disease may be homologous to a calcium-binding member of the tenascin superfamily that has been identified by others in pig and cow.
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PMID:Similarities of an autoantigen in aneurysmal disease of the human abdominal aorta to a 36-kDa microfibril-associated bovine aortic glycoprotein. 763 59

The pathogenesis of abdominal aortic aneurysms (AAAs) is unknown. We hypothesize that the autoimmune disease process plays a key role in the development of AAAs. Both cellular and humoral immunity is involved in the pathogenesis of AAAs. Triggers of autoimmunity are multifactorial. Certain HLA typing is closely related to AAAs, and a certain viral infection may have a potential role in the etiology of AAA via a molecular mimicry mechanism. The autoantigen is located in the microfibrillar compartment of the aortic wall as a normal structure. Patients with AAA are immunoreactive with this novel structural protein. If in the future the autoantigen is fully elucidated, serum testing to detect antibody against the autoantigen can be performed.
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PMID:Abdominal aortic aneurysm as an autoimmune disease. 1179 4

The AAA (ATPase-associated with various cellular activities) ATPase p97 acts on diverse substrate proteins to partake in various cellular processes such as membrane fusion and endoplasmic reticulum-associated degradation (ERAD). In membrane fusion, p97 is thought to function in analogy to the related ATPase NSF (N-ethylmaleimide-sensitive fusion protein), which promotes membrane fusion by disassembling a SNARE complex. In ERAD, p97 dislocates misfolded proteins from the ER membrane to facilitate their turnover by the proteasome. Here, we identify a novel function of p97 in endocytic trafficking by establishing the early endosomal autoantigen 1 (EEA1) as a new p97 substrate. We demonstrate that a fraction of p97 is localized to the early endosome membrane, where it binds EEA1 via the N-terminal C2H2 zinc finger domain. Inhibition of p97 either by siRNA or a pharmacological inhibitor results in clustering and enlargement of early endosomes, which is associated with an altered trafficking pattern for an endocytic cargo. Mechanistically, we show that p97 inhibition causes increased EEA1 self-association at the endosome membrane. We propose that p97 may regulate the size of early endosomes by governing the oligomeric state of EEA1.
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PMID:The p97 ATPase associates with EEA1 to regulate the size of early endosomes. 2155 36