Evidence map›Paper›PMID 37446164›Full record

ReviewInternational journal of molecular sciences2023

Exploring the Interplay between Polyphenols and Lysyl Oxidase Enzymes for Maintaining Extracellular Matrix Homeostasis.

Carolina Añazco, Janin Riedelsberger, Lorenzo Vega-Montoto, Armando Rojas

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed, 1 pooled it
3.8field-weighted citation impact, top 6% 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

21 citing papers in PubMed, 1 synthesis or guideline pooled it, 25 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Review
  4. Article
  5. Review
  6. Review
  7. Review
  8. Potential of Orally Administered Quercetin, Hesperidin, andInternational journal of molecular sciences · 2025
    Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Exploiting Matrix Stiffness to Overcome Drug Resistance.ACS biomaterials science & engineering · 2024
    Review
  16. Review
  17. Use of Collagen in Cosmetic Products.Current issues in molecular biology · 2024
    Review
  18. Review
  19. Article
  20. 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

4 authors at 4 institutions in 2 countries.

Carolina AñazcoLaboratorio de Bioquímica Nutricional, Escuela de Nutrición y Dietética, Carrera de Nutrición y Dietética, Facultad de Ciencias para el Cuidado de la Salud, Universidad San Sebastián, General Lagos #1190, Valdivia 5110773, Chile.ORCID 0000-0003-1311-9492
Janin RiedelsbergerCentro de Bioinformática, Simulación y Modelado (CBSM), Facultad de Ingeniería, Universidad de Talca, 1 Poniente 1141, Talca 3462227, Chile.ORCID 0000-0002-4687-7495
Lorenzo Vega-MontotoChemical and Radiation Measurement, Idaho National Laboratory (INL), 1705 N. Yellowstone Hwy, Idaho Falls, ID 83415, USA.ORCID 0000-0002-4096-1100
Armando RojasBiomedical Research Laboratories, Medicine Faculty, Catholic University of Maule, Talca 3480112, Chile.ORCID 0000-0001-9911-7142
Catholic University of the Maule · CLIdaho National Laboratory · USSan Sebastián University · CLUniversity of Talca · CL

Funding

Agencia Nacional de Investigación y Desarrollo 1212026
6 · The paper itself

Abstract

Collagen, the most abundant structural protein found in mammals, plays a vital role as a constituent of the extracellular matrix (ECM) that surrounds cells. Collagen fibrils are strengthened through the formation of covalent cross-links, which involve complex enzymatic and non-enzymatic reactions. Lysyl oxidase (LOX) is responsible for catalyzing the oxidative deamination of lysine and hydroxylysine residues, resulting in the production of aldehydes, allysine, and hydroxyallysine. These intermediates undergo spontaneous condensation reactions, leading to the formation of immature cross-links, which are the initial step in the development of mature covalent cross-links. Additionally, non-enzymatic glycation contributes to the formation of abnormal cross-linking in collagen fibrils. During glycation, specific lysine and arginine residues in collagen are modified by reducing sugars, leading to the creation of Advanced Glycation End-products (AGEs). These AGEs have been associated with changes in the mechanical properties of collagen fibers. Interestingly, various studies have reported that plant polyphenols possess amine oxidase-like activity and can act as potent inhibitors of protein glycation. This review article focuses on compiling the literature describing polyphenols with amine oxidase-like activity and antiglycation properties. Specifically, we explore the molecular mechanisms by which specific flavonoids impact or protect the normal collagen cross-linking process. Furthermore, we discuss how these dual activities can be harnessed to generate properly cross-linked collagen molecules, thereby promoting the stabilization of highly organized collagen fibrils.

Indexed as

LysineProtein-Lysine 6-OxidaseAminesAnimalsCollagenExtracellular MatrixGlycation End Products, AdvancedHomeostasisMammalsPolyphenolsAminesCollagenGlycation End Products, AdvancedLysinePolyphenolsProtein-Lysine 6-Oxidasecollagen cross-linkingextracellular matrixfibrosisglycationlysyl oxidasepolyphenols

Identifiers

PMID37446164
PMCPMC10342021
OpenAlexW4382981987

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.