Evidence map›Paper›PMID 22745359›Full record

ArticleMolecular pharmacology2012

Anacardic acid inhibits the catalytic activity of matrix metalloproteinase-2 and matrix metalloproteinase-9.

Athira Omanakuttan, Jyotsna Nambiar, Rodney M Harris, Chinchu Bose, Nanjan Pandurangan, Rebu K Varghese, Geetha B Kumar, John A Tainer, Asoke Banerji, J Jefferson P Perry and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in Molecular pharmacology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed, 1 pooled it
1.2field-weighted citation impact, top 19% 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, 1 synthesis or guideline pooled it, 68 citations in OpenAlex.

  1. Pooled it
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  13. Saudi journal of biological sciences · 2019
    Article
  14. (I-3,II-3)-Biacacetin-mediated cell death involves mitochondria.Molecular and cellular biochemistry · 2019
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Antioxidant and Anti-Inflammatory Properties ofEvidence-based complementary and alternative medicine : eCAM · 2017
    Article
  20. Article
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

11 authors at 3 institutions in 2 countries.

Athira OmanakuttanAmrita School of Biotechnology, Amrita Vishwa Vidyapeetham, Amritapuri, Kollam, Kerala, India.
Jyotsna Nambiar
Rodney M Harris
Chinchu Bose
Nanjan Pandurangan
Rebu K Varghese
Geetha B Kumar
John A Tainer
Asoke Banerji
J Jefferson P Perry
Bipin G Nair
Amrita Vishwa Vidyapeetham · INLawrence Berkeley National Laboratory · USScripps Research Institute · US

Funding

Transcription-Coupled & Replication-Associated Excision RepairP01CA092584 · NCI · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI John A. Tainer · 2001 to 2026
$89.6M
Structural biochemistry studies on MAP kinase allosteric binding sitesR03AR059968 · NIAMS · SCRIPPS RESEARCH INSTITUTE, THE · PI PERRY, JOHN JEFFERSON · 2011 to 2013
$280k
NCI NIH HHS CA92584NCI NIH HHS P01 CA092584NIAMS NIH HHS AR059968NIAMS NIH HHS R03 AR059968
6 · The paper itself

Abstract

Cashew nut shell liquid (CNSL) has been used in traditional medicine for the treatment of a wide variety of pathophysiological conditions. To further define the mechanism of CNSL action, we investigated the effect of cashew nut shell extract (CNSE) on two matrix metalloproteinases, MMP-2/gelatinase A and MMP-9/gelatinase B, which are known to have critical roles in several disease states. We observed that the major constituent of CNSE, anacardic acid, markedly inhibited the gelatinase activity of 3T3-L1 cells. Our gelatin zymography studies on these two secreted gelatinases, present in the conditioned media from 3T3-L1 cells, established that anacardic acid directly inhibited the catalytic activities of both MMP-2 and MMP-9. Our docking studies suggested that anacardic acid binds into the MMP-2/9 active site, with the carboxylate group of anacardic acid chelating the catalytic zinc ion and forming a hydrogen bond to a key catalytic glutamate side chain and the C15 aliphatic group being accommodated within the relatively large S1' pocket of these gelatinases. In agreement with the docking results, our fluorescence-based studies on the recombinant MMP-2 catalytic core domain demonstrated that anacardic acid directly inhibits substrate peptide cleavage in a dose-dependent manner, with an IC₅₀ of 11.11 μM. In addition, our gelatinase zymography and fluorescence data confirmed that the cardol-cardanol mixture, salicylic acid, and aspirin, all of which lack key functional groups present in anacardic acid, are much weaker MMP-2/MMP-9 inhibitors. Our results provide the first evidence for inhibition of gelatinase catalytic activity by anacardic acid, providing a novel template for drug discovery and a molecular mechanism potentially involved in CNSL therapeutic action.

Indexed as

3T3-L1 CellsAnacardic AcidsAnacardiumAnimalsCatalysisMatrix Metalloproteinase 2Matrix Metalloproteinase 9Matrix Metalloproteinase InhibitorsMiceMolecular Docking SimulationPlant ExtractsAnacardic AcidsMatrix Metalloproteinase 2Matrix Metalloproteinase 9Matrix Metalloproteinase InhibitorsPlant Extracts

Identifiers

PMID22745359
PMCPMC3463216
OpenAlexW2125695529

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.