Serum amyloid A protein in the course of infectious mononucleosis. [PDF]
Serum amyloid A (SAA) protein is a major acute phase protein. Increased concentrations have been reported in many inflammatory diseases. In bacterial infections, high levels correlate with those of C-reactive protein (CRP). In viral infections, where CRP changes are weaker, SAA is of value for establishing early diagnosis, monitoring the severity, and ...
Todorov I+3 more
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Serum amyloid A protein in acute viral infections. [PDF]
Concentrations of serum amyloid A protein (SAA) were measured in 254 children with viral diseases, including measles, varicella, rubella, mumps, echo-30 meningitis, chronic hepatitis B and C, and in eight with Kawasaki disease. Latex agglutination nephelometric immunoassay was used for assaying SAA.
T Kudo+5 more
semanticscholar +6 more sources
Aggregation of Mouse Serum Amyloid A Protein Was Promoted by Amyloid-Enhancing Factors with the More Genetically Homologous Serum Amyloid A. [PDF]
Amyloid A (AA) amyloidosis is a condition in which amyloid fibrils characterized by a linear morphology and a cross-β structure accumulate and are deposited extracellularly in organs, resulting in chronic inflammatory diseases and infections. The incidence of AA amyloidosis is high in humans and several animal species.
Lin X+3 more
europepmc +4 more sources
Presence of a SARS-CoV-2 Protein Enhances Amyloid Formation of Serum Amyloid A [PDF]
ABSTRACTA marker for the severeness and disease progress of COVID-19 is overexpression of serum amyloid A (SAA) to levels that in other diseases are associated with a risk for SAA amyloidosis. In order to understand whether SAA amyloidosis could also be a long-term risk of SARS-COV-2 infections we have used long all-atom molecular dynamic simulations ...
Asis K. Jana+2 more
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Interaction of the serum amyloid A proteins with phospholipid.
The serum amyloid A proteins (SAA) are transported in plasma in association with the high density lipoproteins. We have studied the solution properties of two of the polymorphic forms of SAA, SAA1 and SAA4, and compared the lipid-binding properties of SAA4 to those of the well characterized apolipoproteins, apo-A-I, apo-A-II, and apo-C-III.
Keith P. W. J. McAdam+6 more
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Influence of polymorphism on glycosylation of serum amyloid a4 protein. [PDF]
Serum amyloid A4 (SAA4) is a constitutive apolipoprotein of high-density lipoprotein. It exhibits N-linked glycosylation in its second half. There are both glycosylated and nonglycosylated forms in plasma and the ratio of these two forms varies among individuals.
Yamada T, Sato J, Kotani K, Tanaka M.
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Binding of serum-derived amyloid-associated proteins to amyloid fibrils
Amyloid signature proteins such as serum amyloid P component, apolipoprotein E (ApoE), and ApoA-IV generally co-localise with amyloid, regardless of the types of amyloid precursor protein or the organs. Most of these proteins derive from serum and have reportedly been involved in amyloid fibril formation and stabilisation, as well as in excretion and ...
Yohei, Misumi+6 more
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Heterogeneity of human serum amyloid A proteins. [PDF]
Serum amyloid A proteins (SAA), presumed precursors of the tissue amyloid A proteins (AA) characteristic of secondary amyloidosis, have been isolated from the plasma high-density lipoproteins (HDL) of normals after etiocholanolone-induced inflammation and from patients with Wegener's granulomatosis, systemic lupus erythematosis, juvenile rheumatoid ...
P N Herbert+2 more
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Serum Amyloid A proteins take retinol for a ride [PDF]
Vitamin A plays pleiotropic roles in the immune system. A recent eLife paper by Hooper and colleagues shows that hepatic and intestinal serum amyloid A proteins, which are induced in response to infection, can transport vitamin A metabolites to tissues and thus impact immune responses both locally and systemically.
Esterházy Daria, Mucida Daniel
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Adenoviral expression of murine serum amyloid A proteins to study amyloid fibrillogenesis [PDF]
Serum amyloid A (SAA) proteins are one of the most inducible acute-phase reactants and are precursors of secondary amyloidosis. In the mouse, SAA1 and SAA2 are induced in approximately equal quantities in response to amyloid induction models. These two isotypes differ in only 9 of 103 amino acid residues; however, only SAA2 is selectively deposited ...
C. Gerardot+6 more
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