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001-es BibID:BIBFORM064340
035-os BibID:(WoS)000382077800015 (Scopus)85013262896
Első szerző:Csomós Krisztián (molekuláris biológus)
Cím:Protein cross-linking by chlorinated polyamines and transglutamylation stabilizes neutrophil extracellular traps / Krisztián Csomós, Endre Kristóf, Bernadett Jakob, István Csomós, György Kovács, Omri Rotem, Judit Hodrea, Zsuzsa Bagoly, Laszlo Muszbek, Zoltán Balajthy, Éva Csősz, László Fésüs
Dátum:2016
ISSN:2041-4889
Megjegyzések:Neutrophil extracellular trap (NET) ejected from activated dying neutrophils is a highly ordered structure of DNA and selected proteins capable to eliminate pathogenic microorganisms. Biochemical determinants of the non-randomly formed stable NETs have not been revealed so far. Studying the formation of human NETs we have observed that polyamines were incorporated into the NET. Inhibition of myeloperoxidase, which is essential for NET formation and can generate reactive chlorinated polyamines through hypochlorous acid, decreased polyamine incorporation. Addition of exogenous primary amines that similarly to polyamines inhibit reactions catalyzed by the protein cross-linker transglutaminases (TGases) has similar effect. Proteomic analysis of the highly reproducible pattern of NET components revealed cross-linking of NET proteins through chlorinated polyamines and epsilon(gamma-glutamyl) lysine as well as bis-gamma-glutamyl polyamine bonds catalyzed by the TGases detected in neutrophils. Competitive inhibition of protein cross-linking by monoamines disturbed the cross-linking pattern of NET proteins, which resulted in the loss of the ordered structure of the NET and significantly reduced capacity to trap bacteria. Our findings provide explanation of how NETs are formed in a reproducible and ordered manner to efficiently neutralize microorganisms at the first defense line of the innate immune system.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
NET
Megjelenés:Cell Death & Disease. - 7 : 8 (2016), p. e2332. -
További szerzők:Kristóf Endre (1987-) (általános orvos) Márkus Bernadett (1989-) (molekuláris biológus) Csomós István (1983-) (molekuláris biológus) Kovács György (1984-) (programtervező matematikus, fizikus) Rotem, Omri Hodrea Judit (1978-) (vegyész) Bagoly Zsuzsa (1978-) (orvos) Muszbek László (1942-) (haematológus, kutató orvos) Balajthy Zoltán (1957-) (biokémikus, sejtbiológus) Csősz Éva (1977-) (biokémikus, molekuláris biológus) Fésüs László (1947-) (orvos biokémikus)
Pályázati támogatás:TÁMOP-4.2.2.A-11/1/KONV-2012-0023
TÁMOP
TÁMOP-4.2.4.A/ 2-11/1-2012-0001
TÁMOP
OTKA NK 105046
OTKA
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001-es BibID:BIBFORM070868
Első szerző:Márkus Bernadett (molekuláris biológus)
Cím:Analysis of the protein crosslink-profile changes and the neutrophil extracellular trap patterns elicited by different stimuli / Bernadett Márkus, Endre Kristóf, István Csomós, László Fésüs, Éva Csősz
Dátum:2017
Megjegyzések:Mature neutrophils act as a first line of defence migrating to the site of infection in response to microbial invasion. They are able to attack pathogen directly in three different ways: phagocytosis, release of antimicrobial peptides and formation of neutrophil extracellular traps (NETs). NET is the result of a unique form of cell death in which neutrophils eject their mixture of nucleoplasm and cytoplasm into the extracellular space forming a web-like structure. Hereby the invaded pathogens are trapped, neutralized therefore their dissemination is inhibited. Several antimicrobial proteins and proteases (such as neutrophil elastase, myeloperoxidase, cathepsin G, azurocidin, lactoferrin) are essential elements of the NET contributing to direct and indirect antimicrobial activities. Based on MS/MS data of protein cross-links formed in the differently treated NETs we could observe protein cross-linking by chlorinated polyamines and transglutaminases and we could demonstrate that both myeloperoxidase and TG1 are required for the stabilization of NET (Csomos et al. Cell Death Dis. 2016). Various bacteria, fungi and viruses can induce NET formation therefore we aimed to investigate the changes in the protein crosslink-profile and in the complex web-like structure during NET formation elicited by different pathogens.
Tárgyszavak:Orvostudományok Elméleti orvostudományok előadáskivonat
Megjelenés:Transglutaminases in Medicine. - p. 83.
További szerzők:Kristóf Endre (1987-) (általános orvos) Csomós István (1983-) (molekuláris biológus) Fésüs László (1947-) (orvos biokémikus) Csősz Éva (1977-) (biokémikus, molekuláris biológus)
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
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