The leucine-rich repeat domain of human peroxidasin 1 promotes binding to laminin in basement membranes

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The leucine-rich repeat domain of human peroxidasin 1 promotes binding to laminin in basement membranes. / Sevcnikar, Benjamin; Schaffner, Irene; Chuang, Christine Y.; Gamon, Luke; Paumann-Page, Martina; Hofbauer, Stefan; Davies, Michael J.; Furtmüller, Paul G.; Obinger, Christian.

In: Archives of Biochemistry and Biophysics, Vol. 689, 108443, 15.08.2020.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Sevcnikar, B, Schaffner, I, Chuang, CY, Gamon, L, Paumann-Page, M, Hofbauer, S, Davies, MJ, Furtmüller, PG & Obinger, C 2020, 'The leucine-rich repeat domain of human peroxidasin 1 promotes binding to laminin in basement membranes', Archives of Biochemistry and Biophysics, vol. 689, 108443. https://doi.org/10.1016/j.abb.2020.108443

APA

Sevcnikar, B., Schaffner, I., Chuang, C. Y., Gamon, L., Paumann-Page, M., Hofbauer, S., ... Obinger, C. (2020). The leucine-rich repeat domain of human peroxidasin 1 promotes binding to laminin in basement membranes. Archives of Biochemistry and Biophysics, 689, [108443]. https://doi.org/10.1016/j.abb.2020.108443

Vancouver

Sevcnikar B, Schaffner I, Chuang CY, Gamon L, Paumann-Page M, Hofbauer S et al. The leucine-rich repeat domain of human peroxidasin 1 promotes binding to laminin in basement membranes. Archives of Biochemistry and Biophysics. 2020 Aug 15;689. 108443. https://doi.org/10.1016/j.abb.2020.108443

Author

Sevcnikar, Benjamin ; Schaffner, Irene ; Chuang, Christine Y. ; Gamon, Luke ; Paumann-Page, Martina ; Hofbauer, Stefan ; Davies, Michael J. ; Furtmüller, Paul G. ; Obinger, Christian. / The leucine-rich repeat domain of human peroxidasin 1 promotes binding to laminin in basement membranes. In: Archives of Biochemistry and Biophysics. 2020 ; Vol. 689.

Bibtex

@article{b3d257dfad0340b7af42d99f22257542,
title = "The leucine-rich repeat domain of human peroxidasin 1 promotes binding to laminin in basement membranes",
abstract = "Human peroxidasin 1 (PXDN) is a homotrimeric multidomain heme peroxidase and essential for tissue development and architecture. It has a biosynthetic function and catalyses the hypobromous acid-mediated formation of specific covalent sulfilimine (S[dbnd]N) bonds, which cross-link type IV collagen chains in basement membranes. Currently, it is unknown whether and which domain(s) [i.e. leucine-rich repeat domain (LRR), immunoglobulin domains, peroxidase domain, von Willebrand factor type C domain] of PXDN interact with the polymeric networks of the extracellular matrix (ECM), and how these interactions integrate and regulate the enzyme's cross-linking activity, without imparting oxidative damage to the ECM. In this study, we probed the interactions of four PXDN constructs with different domain compositions with components of a basement membrane extract by immunoprecipitation. Strong binding of the LRR-containing construct was detected with the major ECM protein laminin. Analysis of these interactions by surface plasmon resonance spectroscopy revealed similar kinetics and affinities of binding of the LRR-containing construct to human and murine laminin-111, with calculated dissociation constants of 1.0 and 1.5 μM, respectively. The findings are discussed with respect to the recently published in-solution structures of the PXDN constructs and the proposed biological role of this peroxidase.",
keywords = "Basement membrane, Extracellular matrix, Human peroxidasin 1, Immunoprecipitation, Laminin, Surface plasmon resonance spectroscopy, Type-IV collagen",
author = "Benjamin Sevcnikar and Irene Schaffner and Chuang, {Christine Y.} and Luke Gamon and Martina Paumann-Page and Stefan Hofbauer and Davies, {Michael J.} and Furtm{\"u}ller, {Paul G.} and Christian Obinger",
year = "2020",
month = "8",
day = "15",
doi = "10.1016/j.abb.2020.108443",
language = "English",
volume = "689",
journal = "Archives of Biochemistry and Biophysics",
issn = "0003-9861",
publisher = "Academic Press",

}

RIS

TY - JOUR

T1 - The leucine-rich repeat domain of human peroxidasin 1 promotes binding to laminin in basement membranes

AU - Sevcnikar, Benjamin

AU - Schaffner, Irene

AU - Chuang, Christine Y.

AU - Gamon, Luke

AU - Paumann-Page, Martina

AU - Hofbauer, Stefan

AU - Davies, Michael J.

AU - Furtmüller, Paul G.

AU - Obinger, Christian

PY - 2020/8/15

Y1 - 2020/8/15

N2 - Human peroxidasin 1 (PXDN) is a homotrimeric multidomain heme peroxidase and essential for tissue development and architecture. It has a biosynthetic function and catalyses the hypobromous acid-mediated formation of specific covalent sulfilimine (S[dbnd]N) bonds, which cross-link type IV collagen chains in basement membranes. Currently, it is unknown whether and which domain(s) [i.e. leucine-rich repeat domain (LRR), immunoglobulin domains, peroxidase domain, von Willebrand factor type C domain] of PXDN interact with the polymeric networks of the extracellular matrix (ECM), and how these interactions integrate and regulate the enzyme's cross-linking activity, without imparting oxidative damage to the ECM. In this study, we probed the interactions of four PXDN constructs with different domain compositions with components of a basement membrane extract by immunoprecipitation. Strong binding of the LRR-containing construct was detected with the major ECM protein laminin. Analysis of these interactions by surface plasmon resonance spectroscopy revealed similar kinetics and affinities of binding of the LRR-containing construct to human and murine laminin-111, with calculated dissociation constants of 1.0 and 1.5 μM, respectively. The findings are discussed with respect to the recently published in-solution structures of the PXDN constructs and the proposed biological role of this peroxidase.

AB - Human peroxidasin 1 (PXDN) is a homotrimeric multidomain heme peroxidase and essential for tissue development and architecture. It has a biosynthetic function and catalyses the hypobromous acid-mediated formation of specific covalent sulfilimine (S[dbnd]N) bonds, which cross-link type IV collagen chains in basement membranes. Currently, it is unknown whether and which domain(s) [i.e. leucine-rich repeat domain (LRR), immunoglobulin domains, peroxidase domain, von Willebrand factor type C domain] of PXDN interact with the polymeric networks of the extracellular matrix (ECM), and how these interactions integrate and regulate the enzyme's cross-linking activity, without imparting oxidative damage to the ECM. In this study, we probed the interactions of four PXDN constructs with different domain compositions with components of a basement membrane extract by immunoprecipitation. Strong binding of the LRR-containing construct was detected with the major ECM protein laminin. Analysis of these interactions by surface plasmon resonance spectroscopy revealed similar kinetics and affinities of binding of the LRR-containing construct to human and murine laminin-111, with calculated dissociation constants of 1.0 and 1.5 μM, respectively. The findings are discussed with respect to the recently published in-solution structures of the PXDN constructs and the proposed biological role of this peroxidase.

KW - Basement membrane

KW - Extracellular matrix

KW - Human peroxidasin 1

KW - Immunoprecipitation

KW - Laminin

KW - Surface plasmon resonance spectroscopy

KW - Type-IV collagen

UR - http://www.scopus.com/inward/record.url?scp=85086475596&partnerID=8YFLogxK

U2 - 10.1016/j.abb.2020.108443

DO - 10.1016/j.abb.2020.108443

M3 - Journal article

C2 - 32485152

AN - SCOPUS:85086475596

VL - 689

JO - Archives of Biochemistry and Biophysics

JF - Archives of Biochemistry and Biophysics

SN - 0003-9861

M1 - 108443

ER -

ID: 243999528