PhD Scientific Days 2026

Poster Session 1.A - Molecular Medicine

The C-terminal Domain Of Peroxidasin As a Novel Matrikine

Előadó neve

Balog, Beáta

Neptune code

A0Z6ZZ

Előadó munkahelye

Semmelweis University, Dept. of Physiology

Előadó telefonszáma

06204908077

Előadó e-mail címe

balog.beata.adel@semmelweis.hu

Az előadás címe

The C-terminal Domain Of Peroxidasin As a Novel Matrikine

Szerző(k) neve és munkahelye

Bea Balog¹, Gábor Sirokmány¹, Panna Keszte¹, Czárán Domonkos¹, Eszter Boros², László Nyitrai², Miklós Geiszt¹

1: Semmelweis University, Dept. of Physiology
2: ELTE TTK, Dept. of Biochemistry

Bemutatás módja

Poszter

Szekció

Poster Session 1.A - Molecular Medicine

Language of the presentation

English

Preferred session

Molecular Medicine

Összefoglaló szövege

The C-terminal Domain Of Peroxidasin As a Novel Matrikine
Introduction:
Peroxidasin (PXDN) is a multi-domain heme peroxidase enzyme that is known to be secreted into the extracellular matrix. The main biochemical function of PXDN, as known so far, is to catalyze the covalent cross-linking of collagen IV protomers through the formation of hypobromous acid. During the secretory process it is cleaved by proprotein convertase enzymes, resulting in a larger, truncated N-terminal part and a 143-amino-acid-long C-terminal part, the latter containing a cysteine-rich von Willebrand C-type domain.
Aim:
Our aim is to demonstrate that this C-terminal fragment (PXDN-CTF) is a stable, soluble secretory product of primary human cells that is glycosylated in a defined manner and proportion. We also aim to analyze its potential for complex formation and its secondary domain structure, as well as to investigate its possible involvement in various biological functions and signaling processes.
Method:
Primary human cell cultures and immortalized cell lines were employed to investigate the posttranslational processing of endogenous and epitope-tagged recombinant PXDN. His-tagged PXDN was purified using nickel-based affinity chromatography and anion-exchange chromatography. Detection of both wild-type and mutant PXDN forms was carried out using a polyclonal antibody directed against the C-terminal region of PXDN, alongside epitope-specific antibodies targeting the respective tags.
Results:
We propose that PXDN-CTF mediates peroxidase-independent effects of PXDN and may act as a previously unrecognized regulator of cellular functions.
Conclusion:
Post-translational processing of PXDN involves distinct glycosylation steps at two different asparagine amino acids of the C-terminal fragment of PXDN. These glycan modifications might also influence the complex formation, molecular interactions, and localization of this protein domain.
Funding:
This study was supported by grants from the National Research, Development and Innovation Office (K133002, K143509). The work was also financed by the Thematic Excellence Program 2021 Health Subprogram of the Ministry for Innovation and Technology in Hungary.

balog.beata.adel@semmelweis.hu
Semmelweis University, Dept. of Physiology
Gábor Sirokmány, Miklós Geiszt

University

Semmelweis University

Supervisor

Gábor Sirokmány, Miklós Geiszt

Publication of my abstract

I do not give consent to the publication of my abstract on the website of the congress.

phd.section.field

in doctoral studies after complex exam (PhD)

Kind

Szabad

Status

elfogadva

Accepted presentation method

poszter

Előadás fájl jóváhagyás

nem rendelkezett róla

Előadó

8103

Start

16:42

End

16:45