Expanding the citrullinome of synovial fibrinogen from rheumatoid arthritis patients

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00023728%3A_____%2F19%3AN0000021" target="_blank" >RIV/00023728:_____/19:N0000021 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/00216208:11110/19:10400666

Výsledek na webu

<a href="https://doi.org/10.1016/j.jprot.2019.103484" target="_blank" >https://doi.org/10.1016/j.jprot.2019.103484</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.jprot.2019.103484" target="_blank" >10.1016/j.jprot.2019.103484</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Expanding the citrullinome of synovial fibrinogen from rheumatoid arthritis patients

Popis výsledku v původním jazyce

Citrullination is a post-translational protein modification, which is associated with inflammation in general and is thought to play an important pathogenic role in rheumatoid arthritis (RA). Here a mass spectrometry-based proteomics approach was applied to identify citrullination sites in synovial fluid fibrinogen from four RA patients. In general, high disease activity correlated with increased number of identified citrullination sites and higher relative citrulline occupancy. Altogether, 23 sites were identified, of which 9 have not been previously reported to be citrullinated in vivo. Citrullination at site alpha 84, alpha 123, alpha 129, alpha 547, alpha 573, alpha 591, beta 334 and gamma 134 was identified in more than one patient, and these positions were therefore regarded as hotspots. Following citrullination of fibrinogen in vitro using human recombinant peptidylarginine deiminase 2 (PAD2), a total of 46 citrullination sites were identified, including 6 hitherto unreported in vitro citrullination sites. Twenty-two out of the 23 citrullination sites identified in vivo were also detected in vitro, supporting the validity of the identifications

Název v anglickém jazyce

Expanding the citrullinome of synovial fibrinogen from rheumatoid arthritis patients

Popis výsledku anglicky

Citrullination is a post-translational protein modification, which is associated with inflammation in general and is thought to play an important pathogenic role in rheumatoid arthritis (RA). Here a mass spectrometry-based proteomics approach was applied to identify citrullination sites in synovial fluid fibrinogen from four RA patients. In general, high disease activity correlated with increased number of identified citrullination sites and higher relative citrulline occupancy. Altogether, 23 sites were identified, of which 9 have not been previously reported to be citrullinated in vivo. Citrullination at site alpha 84, alpha 123, alpha 129, alpha 547, alpha 573, alpha 591, beta 334 and gamma 134 was identified in more than one patient, and these positions were therefore regarded as hotspots. Following citrullination of fibrinogen in vitro using human recombinant peptidylarginine deiminase 2 (PAD2), a total of 46 citrullination sites were identified, including 6 hitherto unreported in vitro citrullination sites. Twenty-two out of the 23 citrullination sites identified in vivo were also detected in vitro, supporting the validity of the identifications

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

30226 - Rheumatology

Projekt

—

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2019

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

JOURNAL OF PROTEOMICS

ISSN

1874-3919

e-ISSN

1876-7737

Svazek periodika

208

Číslo periodika v rámci svazku

Art. Nr.103484

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

7

Strana od-do

1-7

Kód UT WoS článku

000487172100013

EID výsledku v databázi Scopus

2-s2.0-85071238575