Evidence map›Paper›PMID 34471403›Full record

ArticleThe journal of venomous animals and toxins including tropical diseases2021

P-I metalloproteinases and L-amino acid oxidases from

Shreesha K Bhat, Manjunath B Joshi, Sampara Vasishta, Rajesh N Jagadale, Setlur G Biligiri, Monika A Coronado, Raghuvir K Arni, Kapaettu Satyamoorthy

Open access · goldAbstract read
In one paragraph

Article in The journal of venomous animals and toxins including tropical diseases, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.9field-weighted citation impact, top 13% 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

7 citing papers in PubMed, 18 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

8 authors at 3 institutions in 2 countries.

Shreesha K BhatManipal School of Life Sciences, Manipal Academy of Higher Education, Manipal, India.ORCID 0000-0002-8279-278X
Manjunath B JoshiManipal School of Life Sciences, Manipal Academy of Higher Education, Manipal, India.
Sampara VasishtaManipal School of Life Sciences, Manipal Academy of Higher Education, Manipal, India.
Rajesh N JagadaleJuggat Pharma, Jagadale Industries, Bangalore, India.
Setlur G BiligiriJuggat Pharma, Jagadale Industries, Bangalore, India.
Monika A CoronadoMultiuser Center for Biomolecular Innovation, Department of Physics, São Paulo State University (UNESP), São José do Rio Preto, SP, Brazil.
Raghuvir K ArniMultiuser Center for Biomolecular Innovation, Department of Physics, São Paulo State University (UNESP), São José do Rio Preto, SP, Brazil.
Kapaettu SatyamoorthyManipal School of Life Sciences, Manipal Academy of Higher Education, Manipal, India.ORCID 0000-0002-2368-5490
Manipal Academy of Higher Education · INCentro Universitário de Rio Preto · BRReliance Industries (India) · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundSnake venoms are composed of pharmacologically active proteins that are evolutionarily diverse, stable and specific to targets. Hence, venoms have been explored as a source of bioactive molecules in treating numerous diseases. Recent evidences suggest that snake venom proteins may affect the formation of new blood vessels. Excessive angiogenesis has been implicated in several pathologies including tumours, diabetic retinopathy, arthritis,

methodsP-I metalloproteinases and LAAO were purified from venom by molecular size exclusion and ion-exchange chromatography and subsequently confirmed using mass spectrometry. The P-I metalloproteinases were characterized by azocaseinolytic, fibrinogenolytic and gelatinase activity and LAAO activity was assessed by enzyme activity on L-amino acids. Influence of these proteins on apoptosis and cell cycle in endothelial cells was analysed by flow cytometry. The angiogenic activity was determined by

resultsP-I metalloproteinases exhibited azocaseinolytic activity, cleaved α and partially β chain of fibrinogen, and displayed catalytic activity on gelatin. LAAO showed differential activity on L-amino acids. Flow cytometry analysis indicated that both P-I metalloproteinases and LAAO arrested the cells in G0/G1 phase and further induced both necrosis and apoptosis in endothelial cells.

conclusionOur research suggests that P-I metalloproteinases and LAAO exhibit anti-angiogenic properties

Indexed as

Anti-angiogenicBothropsLAAOP-I metalloproteinasesSnake venom

Identifiers

PMID34471403
PMCPMC8381740
OpenAlexW3195403605

What OpenQuestion holds

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LicenceCC BY
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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.