Evidence map›Paper›PMID 37029269›Full record

ArticleCommunications biology2023

Lysyl oxidase-like 2 processing by factor Xa modulates its activity and substrate preference.

Huilei Wang, Alan Poe, Marta Martinez Yus, Lydia Pak, Kavitha Nandakumar, Lakshmi Santhanam

Abstract read
In one paragraph

Article in Communications biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
–field-weighted citation impact
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

11 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Hyperglycemia inhibits AAA expansion: examining the role of lysyl oxidase.American journal of physiology. Heart and circulatory physiology · 2025
    Article
  7. LOXL2 inhibition ameliorates pulmonary artery remodeling in pulmonary hypertension.American journal of physiology. Lung cellular and molecular physiology · 2024
    Article
  8. Sex differences and role of lysyl oxidase-like 2 in angiotensin II-induced hypertension in mice.American journal of physiology. Heart and circulatory physiology · 2024
    Article
  9. LOXL2 in Cancer: A Two-Decade Perspective.International journal of molecular sciences · 2023
    Review
  10. Lysyl oxidase like-2 in fibrosis and cardiovascular disease.American journal of physiology. Cell physiology · 2023
    Review
  11. 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

6 authors.

Huilei WangDepartment of Biomedical Engineering, Johns Hopkins University School of Medicine, 733 N Broadway, Baltimore, MD, 21205, USA.
Alan PoeDepartment of Biomedical Engineering, Johns Hopkins University School of Medicine, 733 N Broadway, Baltimore, MD, 21205, USA.
Marta Martinez YusDepartment of Chemical and Biomolecular Engineering, Johns Hopkins University Whiting School of Engineering, 3400 N Charles St, Baltimore, MD, 21218, USA.
Lydia PakDepartment of Biomedical Engineering, Johns Hopkins University School of Medicine, 733 N Broadway, Baltimore, MD, 21205, USA.
Kavitha NandakumarDepartment of Anesthesiology and CCM, Johns Hopkins University School of Medicine, 733 N Broadway, Baltimore MD, 21205, Baltimore, MD, USA.
Lakshmi SanthanamDepartment of Biomedical Engineering, Johns Hopkins University School of Medicine, 733 N Broadway, Baltimore, MD, 21205, USA. Lsantha1@jhmi.edu.ORCID 0000-0002-2097-9397

Funding

Lysyl Oxidase Like 2: A Novel Target in Aging Associated Vascular StiffeningR01HL148112 · NHLBI · JOHNS HOPKINS UNIVERSITY · PI SANTHANAM, LAKSHMI · 2020 to 2023
$1.9M
NHLBI NIH HHS R01 HL148112
6 · The paper itself

Abstract

Lysyl oxidase-like 2 (LOXL2) has been identified as an essential mediator of extracellular matrix (ECM) remodeling in several disease processes including cardiovascular disease. Thus, there is growing interest in understanding the mechanisms by which LOXL2 is regulated in cells and tissue. While LOXL2 occurs both in full length and processed forms in cells and tissue, the precise identity of the proteases that process LOXL2 and the consequences of processing on LOXL2's function remain incompletely understood. Here we show that Factor Xa (FXa) is a protease that processes LOXL2 at Arg-338. Processing by FXa does not affect the enzymatic activity of soluble LOXL2. However, in situ in vascular smooth muscle cells, LOXL2 processing by FXa results in decreased cross-linking activity in the ECM and shifts substrate preference of LOXL2 from type IV collagen to type I collagen. Additionally, processing by FXa increases the interactions between LOXL2 and prototypical LOX, suggesting a potential compensatory mechanism to preserve total LOXs activity in the vascular ECM. FXa expression is prevalent in various organ systems and shares similar roles in fibrotic disease progression as LOXL2. Thus, LOXL2 processing by FXa could have significant implications in pathologies where LOXL2 is involved.

Indexed as

Factor XaProtein-Lysine 6-OxidaseExtracellular MatrixMyocytes, Smooth MuscleFactor XaProtein-Lysine 6-Oxidase

Identifiers

PMID37029269
PMCPMC10082071

What OpenQuestion holds

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Registered trials

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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.