PXD075502

PXD075502 is an original dataset announced via ProteomeXchange.

Title	Comparison of the reactivity of hypochlorous acid (HOCl) and hyposelenocyanous acid (HOSeCN) with elastase: role of amino acid modification and structural changes in loss of activity.
Description	Elastase is a serine protease that plays a key role in intracellular and extracellular neutrophil-driven immune responses. There is a synergistic relationship between elastase and myeloperoxidase (MPO), which can boost pathogen killing and limit collateral proteolytic damage to host tissue. However, both proteins are strongly implicated in disease pathology, leading to interest in the design of therapeutic strategies to modulate their activity in vivo, particularly in chronic inflammatory settings. In this study, we examine whether the alternative MPO substrate selenocyanate (SeCN-), can modulate the modification of elastase by hypochlorous acid (HOCl), by the favouring the formation of hyposelenocyanous acid (HOSeCN), as a potential therapeutic strategy. Exposure of elastase to HOCl results in significant loss of function, amino acid modification, fragmentation and aggregation. Trp and Tyr are readily modified, forming hydroxytryptophan derivatives, kynurenine and 3-chlorotyrosine, respectively. Loss of cystine, Met, His and Arg was also observed, together with the formation of N-chloramines, which did not appear to cause secondary oxidation. Inactivation of elastase was observed on exposure to HOSeCN, which correlated with strongly with unfolding. With HOSeCN, there was less extensive modification and loss of amino acid residues, with Trp and cystine residues shown to be the main targets. Fragmentation of elastase was observed under reducing conditions, shown by the presence of multiple low molecular mass bands, whereas a band at 50 kDa was seen in the absence of reducing agent, suggesting formation of a dimer. Supplementation of HOCl with sub-stoichiometric amounts of SeCN- prevented elastase inactivation but resulted in structural changes to elastase consistent with HOSeCN formation.
HostingRepository	PRIDE
AnnounceDate	2026-06-22
AnnouncementXML	Submission_2026-06-22_02:55:14.265.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Helen Hemmling
SpeciesList	scientific name: Sus scrofa domesticus (domestic pig); NCBI TaxID: NEWT:9825;
ModificationList	L-cysteine sulfenic acid; L-methionine sulfone; L-methionine sulfoxide; N'-formyl-L-kynurenine; monochlorinated L-tryptophan; chlorinated tyrosine; dichlorinated tyrosine
Instrument	impact II

Revision	Datetime	Status	ChangeLog Entry
0	2026-03-11 08:39:46	ID requested
⏵ 1	2026-06-22 02:55:14	announced

10.1016/J.FREERADBIOMED.2026.06.033;

submitter keyword: inflammation, protease, protein oxidation,Selenocyanate, myeloperoxidase

Clare Louise Hawkins
contact affiliation	University of Copenhagen, Faculty of Health and Medical Sciences, Department of Biomedical Sciences
contact email	clare.hawkins@sund.ku.dk
lab head
Helen Hemmling
contact affiliation	University of Copenhagen, Faculty of Health and Medical Sciences, Department of Biomedical Sciences
contact email	helen@sund.ku.dk
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD075502
     1. Label: PRIDE project
     2. Name: Comparison of the reactivity of hypochlorous acid (HOCl) and hyposelenocyanous acid (HOSeCN) with elastase: role of amino acid modification and structural changes in loss of activity.