PhD Scientific Days 2025

Molecular Medicine II.

Exploring the C-terminal domain of Peroxidasin as a novel matrikine

Előadó neve

Balog Beáta

Neptun code

A0Z6ZZ

Előadó munkahelye

Department of Physiology

Előadó telefonszáma

06204908077

Előadó e-mail címe

balog.beata.adel@semmelweis.hu

Az előadás címe

Exploring the C-terminal domain of Peroxidasin as a novel matrikine

Szerző(k) neve és munkahelye

Beáta Balog¹

1: Department of Physiology

Bemutatás módja

Szóbeli

Szekció

Molecular Medicine II.

Language of the presentation

Hungarian

Preferred session

Molecular Medicine

Összefoglaló szövege

Introduction:
Peroxidasin (PXDN) is a multi-domain protein with peroxidase activity.It is secreted into the extracellular space where its known function, is the catalysis of the covalent cross-linking of collagen IV.During the secretory process proprotein convertases can cut off a stable C-terminal fragment (PXDN-CTF) containing an alpha helical part followed by a von Willebrand factor type C (VWFC) domain.We have formerly discovered that PXDN-CTF can be detected at two distinct molecular heights on SDS-PAGE.The structure and function of the PXDN-CTF is largely unknown.
Aim:
We aimed to reveal the exact nature of the posttranslational processing of the C-terminal domain of PXDN.We were also interested in finding possible explanations for the two distinct molecular heights found on SDS-PAGE along with their biological significance.We also investigated the role of glycosylation of PXDN-CTF in the ECM and possible involvement in various biological functions and signaling processes.
Methods:
We used primary human cell cultures and immortalized cells to study the posttranslational processing of endogenous or epitope-tagged, recombinant PXDN.NEBQ5 PCR mutagenesis was used to create epitope-tagged forms of PXDN.We used both a polyclonal antibody against the C-terminal part of PXDN and specific antibodies against the different epitopes to detect wild type and mutated forms of PXDN.
Results:
We were successful in finding multiple pieces of evidence regarding the glycosylation of this domain and characterized this process in detail.We could also exclude the possibility that the C-terminal VWFC domain undergoes additional posttranslational proteolytic processing.We found that the glycosylation was necessary for the proper localisation of PXDN-CTF in the ECM.
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.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
Dept. of Physiology
Gábor Sirokmány

University

Semmelweis University

Supervisor

Gábor Sirokmány

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 before complex exam (PhD)

Kind

Szabad

Status

elfogadva

Accepted presentation method

szóbeli

Előadás fájl jóváhagyás

nem hagyta jóvá

Előadó

8103

Start

09:45

End

10:00