Interaction of serum amyloid A with human cystatin Cuidentification of binding sites
Spodzieja, Marta ; Szymanska, Aneta ; Kolodziejczyk, Aleksandra ; Pradzinska, Martyna ; Maszota, Martyna ; Stefanowicz, Piotr ; Szewczuk, Zbigniew ; Grubb, Anders LU
and Czaplewska, Paulina
(2012)
In Journal of Molecular Recognition
25(10).
p.513-524
- Abstract
- 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 proteaseshuman 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 SAAhCC complex, using a combination of selective proteolytic excision and... (More)
- 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 proteaseshuman 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 SAAhCC 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(86104), whereas the binding site in hCC sequence was identified as hCC(96102). Binding specificities of both interacting sequences were ascertained by affinity experiments (ELISA) and by registration of mass spectrum of SAAhCC complex. Copyright (c) 2012 John Wiley & Sons, Ltd. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/3190037
- author
- Spodzieja, Marta
; Szymanska, Aneta
; Kolodziejczyk, Aleksandra
; Pradzinska, Martyna
; Maszota, Martyna
; Stefanowicz, Piotr
; Szewczuk, Zbigniew
; Grubb, Anders
LU
and Czaplewska, Paulina
- organization
- publishing date
- 2012
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- serum amyloid A, human cystatin C, protein-protein interaction, mass, spectrometry
- in
- Journal of Molecular Recognition
- volume
- 25
- issue
- 10
- pages
- 513 - 524
- publisher
- John Wiley & Sons Inc.
- external identifiers
-
- wos:000309067200004
- scopus:84866426295
- pmid:22996594
- ISSN
- 1099-1352
- DOI
- 10.1002/jmr.2220
- language
- English
- LU publication?
- yes
- id
- fb05286d-4a1d-452e-94a6-0264839ec990 (old id 3190037)
- date added to LUP
- 2016-04-01 11:15:19
- date last changed
- 2023-02-12 04:00:41
@article{fb05286d-4a1d-452e-94a6-0264839ec990,
abstract = {{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 proteaseshuman 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 SAAhCC 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(86104), whereas the binding site in hCC sequence was identified as hCC(96102). Binding specificities of both interacting sequences were ascertained by affinity experiments (ELISA) and by registration of mass spectrum of SAAhCC complex. Copyright (c) 2012 John Wiley & Sons, Ltd.}},
author = {{Spodzieja, Marta and Szymanska, Aneta and Kolodziejczyk, Aleksandra and Pradzinska, Martyna and Maszota, Martyna and Stefanowicz, Piotr and Szewczuk, Zbigniew and Grubb, Anders and Czaplewska, Paulina}},
issn = {{1099-1352}},
keywords = {{serum amyloid A; human cystatin C; protein-protein interaction; mass; spectrometry}},
language = {{eng}},
number = {{10}},
pages = {{513--524}},
publisher = {{John Wiley & Sons Inc.}},
series = {{Journal of Molecular Recognition}},
title = {{Interaction of serum amyloid A with human cystatin Cuidentification of binding sites}},
url = {{http://dx.doi.org/10.1002/jmr.2220}},
doi = {{10.1002/jmr.2220}},
volume = {{25}},
year = {{2012}},
}