ArticleMolecular biology reports2011
The human lysyl oxidase-like 2 protein functions as an amine oxidase toward collagen and elastin.
Article in Molecular biology reports, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.
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Who cites it
68 citing papers in PubMed, 115 citations in OpenAlex.
- Rare protein-coding variation and the genetic architecture of height in >1.4 million individuals.medRxiv : the preprint server for health sciences · 2026Article
- The extracellular matrix: structure, composition, biological functions, diseases, and therapeutic targets.Molecular biomedicine · 2026Review
- Covalent Inhibitor Screening for Targeting LOXL2: Studied by Virtual Screening and Experimental Validation.Recent patents on anti-cancer drug discovery · 2026Article
- Preoperative serum LOXL2 levels are elevated in patients with pulmonary hypertension undergoing mitral valve surgery in a prospective observational cohort study.Journal of applied physiology (Bethesda, Md. : 1985) · 2025Observational
- Research progress on the role of lipoxygenase and its inhibitors in prostate cancer.Future oncology (London, England) · 2024Review
- LOXL2 inhibition ameliorates pulmonary artery remodeling in pulmonary hypertension.American journal of physiology. Lung cellular and molecular physiology · 2024Article
- Acute exposure to ultraviolet radiation targets proteins involved in collagen fibrillogenesis.Frontiers in physiology · 2024Article
- Extracellular Hsp90 Binds to and Aligns Collagen-1 to Enhance Breast Cancer Cell Invasiveness.Cancers · 2023Article
- Lysyl oxidase like-2 in fibrosis and cardiovascular disease.American journal of physiology. Cell physiology · 2023Review
- Lysyl oxidase-like 2 processing by factor Xa modulates its activity and substrate preference.Communications biology · 2023Article
- Article
- Lysyl Oxidase Family Proteins: Prospective Therapeutic Targets in Cancer.International journal of molecular sciences · 2022Review
- The Extracellular Matrix: A Key Accomplice of Cancer Stem Cell Migration, Metastasis Formation, and Drug Resistance in PDAC.Cancers · 2022Review
- The IRE1α-XBP1s Arm of the Unfolded Protein Response Activates N-Glycosylation to Remodel the Subepithelial Basement Membrane in Paramyxovirus Infection.International journal of molecular sciences · 2022Article
- LOXL2 silencing suppresses angiotensin II-induced cardiac hypertrophy through the EMT process and TGF-β1/Smad3/NF-κB pathway.Iranian journal of basic medical sciences · 2022Article
- Lung Fibrosis and Fibrosis in the Lungs: Is It All about Myofibroblasts?Biomedicines · 2022Review
- Extracellular matrix dynamics: tracking in biological systems and their implications.Journal of biological engineering · 2022Review
- Regulators of collagen crosslinking in developing and adult tendons.European cells & materials · 2022Review
- Implications of lysyl oxidase-like protein 3 expression in the periodontium of diabetic rats.Journal of applied oral science : revista FOB · 2022Article
- An in situ activity assay for lysyl oxidases.Communications biology · 2021Article
8 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The lysyl oxidase-like 2 (LOXL2) protein is a human paralogue of lysyl oxidase (LOX) that functions as an amine oxidase for formation of lysine-derived cross-links found in collagen and elastin. In addition to the C-terminal domains characteristic to the LOX family members, LOXL2 contains four scavenger receptor cysteine-rich (SRCR) domains in the N-terminus. In order to assess the amine oxidase activity of LOXL2, we expressed a series of recombinant LOXL2 proteins with deletions in the SRCR domains, using an Escherichia coli expression system. All of the purified recombinant LOXL2 proteins, with or without the SRCR domains in the N-terminus, showed significant amine oxidase activity toward several different types of collagen and elastin in in vitro amine oxidase assays, indicating deletion of the SRCR domains does not interfere with amine oxidase activity of LOXL2. Further, amine oxidase activity of LOXL2 was not susceptible to inhibition by β-aminopropionitrile, an irreversible inhibitor of LOX, suggesting a different enzymatic mechanism between these two paralogues.
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Registered trials
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.