Evidence map›Paper›PMID 26739611›Full record

ArticleScientific reports2016

Potential Dual Role of Eugenol in Inhibiting Advanced Glycation End Products in Diabetes: Proteomic and Mechanistic Insights.

Priyanka Singh, Ramesha H Jayaramaiah, Sachin B Agawane, Garikapati Vannuruswamy, Arvind M Korwar, Atul Anand, Vitthal S Dhaygude, Mahemud L Shaikh, Rakesh S Joshi, Ramanamurthy Boppana and 3 more

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed, 1 pooled it
9.5field-weighted citation impact, top 1% 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

41 citing papers in PubMed, 1 synthesis or guideline pooled it, 139 citations in OpenAlex.

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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

13 authors at 4 institutions in 1 country.

Priyanka SinghDivision of Biochemical Sciences, CSIR-National Chemical Laboratory, Pune 411008, Maharashtra, India.
Ramesha H JayaramaiahDivision of Biochemical Sciences, CSIR-National Chemical Laboratory, Pune 411008, Maharashtra, India.
Sachin B AgawaneDivision of Biochemical Sciences, CSIR-National Chemical Laboratory, Pune 411008, Maharashtra, India.
Garikapati VannuruswamyDivision of Biochemical Sciences, CSIR-National Chemical Laboratory, Pune 411008, Maharashtra, India.
Arvind M KorwarDivision of Biochemical Sciences, CSIR-National Chemical Laboratory, Pune 411008, Maharashtra, India.
Atul AnandDivision of Biochemical Sciences, CSIR-National Chemical Laboratory, Pune 411008, Maharashtra, India.
Vitthal S DhaygudeKrantisinh Nana Patil College of Veterinary Science, Shirwal, Satara 412 801, Maharashtra, India.
Mahemud L ShaikhNational Centre for Cell Science, Pune 411007, Maharashtra, India.
Rakesh S JoshiInstitute of Bioinformatics and Biotechnology, Savitribai Phule Pune University, Pune 411007, Maharashtra, India.
Ramanamurthy BoppanaNational Centre for Cell Science, Pune 411007, Maharashtra, India.
Mahesh J KulkarniDivision of Biochemical Sciences, CSIR-National Chemical Laboratory, Pune 411008, Maharashtra, India.
Hirekodathakallu V ThulasiramDivision of Organic Chemistry, CSIR-National Chemical Laboratory, Pune 411008, Maharashtra, India.
Ashok P GiriDivision of Biochemical Sciences, CSIR-National Chemical Laboratory, Pune 411008, Maharashtra, India.
National Chemical Laboratory · INNational Centre for Cell Science · INInstitute of Bioinformatics · INKrantisinh Nana Patil College of Veterinary Science · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Medicinally important genus Ocimum harbors a vast pool of chemically diverse metabolites. Current study aims at identifying anti-diabetic candidate compounds from Ocimum species. Major metabolites in O. kilimandscharicum, O. tenuiflorum, O. gratissimum were purified, characterized and evaluated for anti-glycation activity. In vitro inhibition of advanced glycation end products (AGEs) by eugenol was found to be highest. Preliminary biophysical analysis and blind docking studies to understand eugenol-albumin interaction indicated eugenol to possess strong binding affinity for surface exposed lysines. However, binding of eugenol to bovine serum albumin (BSA) did not result in significant change in secondary structure of protein. In vivo diabetic mice model studies with eugenol showed reduction in blood glucose levels by 38% likely due to inhibition of α-glucosidase while insulin and glycated hemoglobin levels remain unchanged. Western blotting using anti-AGE antibody and mass spectrometry detected notably fewer AGE modified peptides upon eugenol treatment both in vivo and in vitro. Histopathological examination revealed comparatively lesser lesions in eugenol-treated mice. Thus, we propose eugenol has dual mode of action in combating diabetes; it lowers blood glucose by inhibiting α-glucosidase and prevents AGE formation by binding to ε-amine group on lysine, protecting it from glycation, offering potential use in diabetic management.

Indexed as

AnimalsBlood GlucoseDiabetes Mellitus, ExperimentalDrug Evaluation, PreclinicalEugenolGlycated HemoglobinGlycation End Products, AdvancedGlycoside Hydrolase InhibitorsGuanidinesMaleMice, Inbred BALB COcimumPlant ExtractsProteomicsBlood GlucoseEugenolGlycated HemoglobinGlycation End Products, AdvancedGlycoside Hydrolase InhibitorsGuanidinespimagedinePlant Extracts

Identifiers

PMID26739611
PMCPMC4704049
OpenAlexW2225072053

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.