Evidence map›Paper›PMID 30676771›Full record

ArticleFASEB journal : official publication of the Federation of American Societies for Experimental Biology2019

Lysyl oxidase-like 2 (LOXL2)-mediated cross-linking of tropoelastin.

Christian E H Schmelzer, Andrea Heinz, Helen Troilo, Michael P Lockhart-Cairns, Thomas A Jowitt, Marion F Marchand, Laurent Bidault, Marine Bignon, Tobias Hedtke, Alain Barret and 6 more

Open access · hybridAbstract read
In one paragraph

Article in FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
3.3field-weighted citation impact, top 7% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

44 citing papers in PubMed, 72 citations in OpenAlex.

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  15. LOXL2 in Cancer: A Two-Decade Perspective.International journal of molecular sciences · 2023
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

16 authors at 8 institutions in 4 countries.

Christian E H SchmelzerFraunhofer Institute for Microstructure of Materials and Systems (IMWS), Halle (Saale), Germany.
Andrea HeinzInstitute of Pharmacy, Martin Luther University Halle-Wittenberg, Halle (Saale), Germany.
Helen TroiloWellcome Trust Centre for Cell-Matrix Research, University of Manchester, Manchester, United Kingdom.
Michael P Lockhart-CairnsWellcome Trust Centre for Cell-Matrix Research, University of Manchester, Manchester, United Kingdom.
Thomas A JowittWellcome Trust Centre for Cell-Matrix Research, University of Manchester, Manchester, United Kingdom.
Marion F MarchandCenter for Interdisciplinary Research in Biology (CIRB), Collège de France, CNRS, INSERM, PSL Research University, Paris, France.
Laurent BidaultCenter for Interdisciplinary Research in Biology (CIRB), Collège de France, CNRS, INSERM, PSL Research University, Paris, France.
Marine BignonCenter for Interdisciplinary Research in Biology (CIRB), Collège de France, CNRS, INSERM, PSL Research University, Paris, France.
Tobias HedtkeFraunhofer Institute for Microstructure of Materials and Systems (IMWS), Halle (Saale), Germany.
Alain BarretCenter for Interdisciplinary Research in Biology (CIRB), Collège de France, CNRS, INSERM, PSL Research University, Paris, France.
James C McConnellDivision of Cell-Matrix Biology and Regenerative Medicine, School of Biological Sciences, Faculty of Biology, Medicine and Health, University of Manchester, Manchester, United Kingdom.
Michael J SherrattDivision of Cell-Matrix Biology and Regenerative Medicine, School of Biological Sciences, Faculty of Biology, Medicine and Health, University of Manchester, Manchester, United Kingdom.
Stéphane GermainCenter for Interdisciplinary Research in Biology (CIRB), Collège de France, CNRS, INSERM, PSL Research University, Paris, France.
David J S HulmesUMR 5305, Centre National de la Recherche Scientifique (CNRS), Laboratoire de Biologie Tissulaire et Ingénierie Thérapeutique (LBTI), Université de Lyon, Lyon, France.
Clair BaldockWellcome Trust Centre for Cell-Matrix Research, University of Manchester, Manchester, United Kingdom.
Laurent MullerCenter for Interdisciplinary Research in Biology (CIRB), Collège de France, CNRS, INSERM, PSL Research University, Paris, France.
University of Manchester · GBCentre Interdisciplinaire de Recherche en Biologie · FRFraunhofer Institute for Microstructure of Materials and Systems · DEInserm · FRBiologie Tissulaire et Ingénierie Thérapeutique · FRCentre National de la Recherche Scientifique · FRCollège de France · FRUniversity of Copenhagen · DK

Funding

Biotechnology and Biological Sciences Research Council BB/L00612X/1
6 · The paper itself

Abstract

Lysyl oxidases (LOXs) play a central role in extracellular matrix remodeling during development and tumor growth and fibrosis through cross-linking of collagens and elastin. We have limited knowledge of the structure and substrate specificity of these secreted enzymes. LOXs share a conserved C-terminal catalytic domain but differ in their N-terminal region, which is composed of 4 repeats of scavenger receptor cysteine-rich (SRCR) domains in LOX-like (LOXL) 2. We investigated by X-ray scattering and electron microscopy the low-resolution structure of the full-length enzyme and the structure of a shorter form lacking the catalytic domain. Our data demonstrate that LOXL2 has a rod-like structure with a stalk composed of the SRCR domains and the catalytic domain at its tip. We detected direct interaction between LOXL2 and tropoelastin (TE) and also LOXL2-mediated deamination of TE. Using proteomics, we identified several allysines together with cross-linked TE peptides. The elastin-like material generated was resistant to trypsin proteolysis and displayed mechanical properties similar to mature elastin. Finally, we detected the codistribution of LOXL2 and elastin in the vascular wall. Altogether, these data suggest that LOXL2 could participate in elastogenesis in vivo and could be used as a means of cross-linking TE in vitro for biomimetic and cell-compatible tissue engineering purposes.-Schmelzer, C. E. H., Heinz, A., Troilo, H., Lockhart-Cairns, M.-P., Jowitt, T. A., Marchand, M. F., Bidault, L., Bignon, M., Hedtke, T., Barret, A., McConnell, J. C., Sherratt, M. J., Germain, S., Hulmes, D. J. S., Baldock, C., Muller, L. Lysyl oxidase-like 2 (LOXL2)-mediated cross-linking of tropoelastin.

Indexed as

Amino Acid OxidoreductasesAnimalsCatalytic DomainCell LineCHO CellsCollagenCricetulusElastinExtracellular MatrixHumansProteolysisSubstrate SpecificityTropoelastinAmino Acid OxidoreductasesCollagenElastinLOXL2 protein, humanTropoelastinelastinmatrix remodelingprotein structureproteomicsSAXS

Identifiers

PMID30676771
PMCPMC6629125
OpenAlexW2907087287

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.