Evidence map›Paper›PMID 23319596›Full record

ArticleThe Journal of biological chemistry2013

Post-translational modifications of recombinant human lysyl oxidase-like 2 (rhLOXL2) secreted from Drosophila S2 cells.

Li Xu, Eden P Go, Joel Finney, HeeJung Moon, Mason Lantz, Kathryn Rebecchi, Heather Desaire, Minae Mure

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

23 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Insight into the Spatial Arrangement of the Lysine Tyrosylquinone and CuInternational journal of molecular sciences · 2022
    Article
  5. Article
  6. Mass Spectrometry-Based Disulfide Mapping of Lysyl Oxidase-like 2.International journal of molecular sciences · 2022
    Article
  7. Article
  8. Article
  9. Review
  10. LOXL2 Inhibitors and Breast Cancer Progression.Antioxidants (Basel, Switzerland) · 2021
    Review
  11. Article
  12. Article
  13. Lysyl oxidase-like 2 (LOXL2)-mediated cross-linking of tropoelastin.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019
    Article
  14. Article
  15. Crystal structure of human lysyl oxidase-like 2 (hLOXL2) in a precursor state.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  16. Article
  17. Lysyl Oxidase: Its Diversity in Health and Diseases.Indian journal of clinical biochemistry : IJCB · 2017
    Review
  18. Article
  19. Article
  20. Human lysyl oxidase-like 2.Bioorganic chemistry · 2014
    Review
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

8 authors at 1 institution in 1 country.

Li XuDepartment of Chemistry, The University of Kansas, Lawrence, Kansas 66045, USA.
Eden P Go
Joel Finney
HeeJung Moon
Mason Lantz
Kathryn Rebecchi
Heather Desaire
Minae Mure
University of Kansas · US

Funding

WEIGHT CONTROL, CELL SIGNALING AND CANCER PREVENTIONP20RR015563 · NCRR · UNIVERSITY OF KANSAS LAWRENCE · PI ZUFFEREY, RACHEL · 2000 to 2009
$20.1M
Mechanism and inhibition of collagen prolyl-4-hydroxylasesR01GM079446 · NIGMS · UNIVERSITY OF KANSAS LAWRENCE · PI MURE, MINAE · 2007 to 2011
$1.3M
Development of a rapid glycosylation profiling system using mass spec dataR01RR026061 · NCRR · UNIVERSITY OF KANSAS LAWRENCE · PI DESAIRE, HEATHER R · 2009 to 2011
$935k
NCRR NIH HHS P20 RR015563NCRR NIH HHS R01 RR026061NCRR NIH HHS R01RR026061NIGMS NIH HHS GM079446-02NIGMS NIH HHS R01 GM079446
6 · The paper itself

Abstract

Human lysyl oxidase-like 2 (hLOXL2) is highly up-regulated in metastatic breast cancer cells and tissues and induces epithelial-to-mesenchymal transition, the first step of metastasis/invasion. hloxl2 encodes four N-terminal scavenger receptor cysteine-rich domains and the highly conserved C-terminal lysyl oxidase (LOX) catalytic domain. Here, we assessed the extent of the post-translational modifications of hLOXL2 using truncated recombinant proteins produced in Drosophila S2 cells. The recombinant proteins are soluble, in contrast to LOX, which is consistently reported to require 2-6 m urea for solubilization. The recombinant proteins also show activity in tropoelastin oxidation. After phenylhydrazine derivatization and trypsin digestion, we used mass spectrometry to identify peptides containing the derivatized lysine tyrosylquinone cross-link at Lys-653 and Tyr-689, as well as N-linked glycans at Asn-455 and Asn-644. Disruption of N-glycosylation by site-directed mutagenesis or tunicamycin treatment completely inhibited secretion so that only small quantities of inclusion bodies were detected. The N-glycosylation site at Asn-644 in the LOX catalytic domain is not conserved in human LOX (hLOX), although the LOX catalytic domain of hLOX shares ∼50% identity and ∼70% homology with hLOXL2. The catalytic domain of hLOX was not secreted from S2 cells using the same expression system. These results suggest that the N-glycan at Asn-644 of hLOXL2 enhances the solubility and stability of the LOX catalytic domain.

Indexed as

Protein Processing, Post-TranslationalAmino Acid OxidoreductasesAnimalsBreast NeoplasmsCarbohydratesCatalytic DomainCell LineDrosophila melanogasterGlycosylationHumansLysineMass SpectrometryMutagenesis, Site-DirectedNeoplasm InvasivenessNeoplasm MetastasisPeptidesAmino Acid OxidoreductasesCarbohydratesLOXL2 protein, humanLysinelysine tyrosylquinonePeptidesPolysaccharidesQuinonesRecombinant ProteinsSolvents

Identifiers

PMID23319596
PMCPMC3581389
OpenAlexW2150211037

What OpenQuestion holds

Textmetadata
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.