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2016 ; 35
(9
): 2185-94
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Identification of citrullinated peptides in the synovial fluid of patients with
rheumatoid arthritis using LC-MALDI-TOF/TOF
#MMPMID27060082
Wang F
; Chen FF
; Gao WB
; Wang HY
; Zhao NW
; Xu M
; Gao DY
; Yu W
; Yan XL
; Zhao JN
; Li XJ
Clin Rheumatol
2016[Sep]; 35
(9
): 2185-94
PMID27060082
show ga
The objective of the study is to investigate potential citrullinated autoantigens
as targets of anti-citrullinated protein antibodies (ACPAs) response in synovial
fluids (SFs) of patients with rheumatoid arthritis (RA). SFs from six RA patients
and six osteoarthritis (OA) patients as controls were collected. The
citrullinated proteins in SFs were extracted by immunoprecipitation with rabbit
anti-citrulline antibodies. Matrix-assisted laser desorption/ionization time of
flight mass spectrometry/time of flight mass spectrometry (MALDI-TOF/TOF) mass
spectrometry was subsequently performed to discover a characteristic neutral loss
to finally determine citrullinated autoantigens. A total of 182 citrullinated
peptides and 200 citrullinated sites were identified in RA SFs, while 3
citrullinated peptides and 4 citrullinated sites were identified in OA SFs. The
182 citrullinated peptides from RA SFs and the 3 citrullinated peptides from OA
SFs were derived from 83 and 3 autoantigens, respectively. Eighty-three
autoantigens except protein-arginine deiminase type-2 (PADI2) and
protein-arginine deiminase type-2 (PADI4) were over-citrullinated compared with
controls, and the citrullinated sites of PADI2 and PADI4 were different in two
groups. Interestingly, citrullinated histone H3.3 (H3F3A) was found in OA
controls, but not in RA groups. The differential citrullinated proteins
identified in RA SFs suggested potential autoantigens were targeted for ACPAs
response and might contribute to the induction and perpetuation of complement
activation and joint inflammation in RA.