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Inne
Interaction of serum amyloid A with human cystatin C–identification of binding sites.
Autorzy
Rok wydania
2012
Czasopismo
Journal of Molecular Recognition
Numer woluminu
25
Strony
513-524
DOI
10.1002/jmr.2220
Kolekcja
Język
Angielski
Typ publikacji
Artykuł
Serum amyloid A (SAA) is a multifunctional acute-phase protein whose natural role seems to be participation in many physiologic and pathological processes. Prolonged increased SAA level in a number of chronic inflammatory and neoplastic diseases gives rise to reactive systemic amyloid A amyloidosis, where the N-terminal 76-amino acid residue-long segment of SAA is deposited as amyloid fibrils. Recently, a specific interaction between SAA and the ubiquitous inhibitor of cysteine proteases--human cystatin C (hCC)--has been described. Here, we report further evidence corroborating this interaction, and the identification of the SAA and hCC binding sites in the SAA-hCC complex, using a combination of selective proteolytic excision and high-resolution mass spectrometry. The shortest binding site in the SAA sequence was determined as SAA(86-104), whereas the binding site in hCC sequence was identified as hCC(96-102). Binding specificities of both interacting sequences were ascertained by affinity experiments (ELISA) and by registration of mass spectrum of SAA-hCC complex.
Adres publiczny
http://dx.doi.org/10.1002/jmr.2220
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