Evidence map›Paper›PMID 35027593›Full record

ArticleScientific reports2022

Extension of human GCSF serum half-life by the fusion of albumin binding domain.

Fatemeh Yadavar Nikravesh, Samira Shirkhani, Elham Bayat, Yeganeh Talebkhan, Esmat Mirabzadeh, Masoumeh Sabzalinejad, Hooman Aghamirza Moghim Aliabadi, Leila Nematollahi, Yalda Hosseinzadeh Ardakani, Soroush Sardari

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In one paragraph

Article in Scientific reports, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
4.3field-weighted citation impact, top 4% 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

17 citing papers in PubMed, 42 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

10 authors at 2 institutions in 1 country.

Fatemeh Yadavar NikraveshBiotechnology Research Center, Pasteur Institute of Iran, Tehran, Iran.
Samira ShirkhaniBiotechnology Research Center, Pasteur Institute of Iran, Tehran, Iran.
Elham BayatBiotechnology Research Center, Pasteur Institute of Iran, Tehran, Iran.
Yeganeh TalebkhanBiotechnology Research Center, Pasteur Institute of Iran, Tehran, Iran. talebkhan@pasteur.ac.ir.
Esmat MirabzadehDepartment of Molecular Medicine, Pasteur Institute of Iran, Tehran, Iran.
Masoumeh SabzalinejadBiotechnology Research Center, Pasteur Institute of Iran, Tehran, Iran.
Hooman Aghamirza Moghim AliabadiBiotechnology Research Center, Pasteur Institute of Iran, Tehran, Iran.
Leila NematollahiBiotechnology Research Center, Pasteur Institute of Iran, Tehran, Iran.
Yalda Hosseinzadeh ArdakaniBiopharmaceutics and Pharmacokinetic Division, Department of Pharmaceutics, Faculty of Pharmacy, Tehran, Iran. yh-ardakani@tums.ac.ir.
Soroush SardariBiotechnology Research Center, Pasteur Institute of Iran, Tehran, Iran.
Biotechnology Research Center · IRPasteur Institute of Iran · IR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Granulocyte colony stimulating factor (GCSF) can decrease mortality of patients undergo chemotherapy through increasing neutrophil counts. Many strategies have been developed to improve its blood circulating time. Albumin binding domain (ABD) was genetically fused to N-terminal end of GCSF encoding sequence and expressed as cytoplasmic inclusion bodies within Escherichia coli. Biological activity of ABD-GCSF protein was assessed by proliferation assay on NFS-60 cells. Physicochemical properties were analyzed through size exclusion chromatography, circular dichroism, intrinsic fluorescence spectroscopy and dynamic light scattering. Pharmacodynamics and pharmacokinetic properties were also investigated in a neutropenic rat model. CD and IFS spectra revealed that ABD fusion to GCSF did not significantly affect the secondary and tertiary structures of the molecule. DLS and SEC results indicated the absence of aggregation formation. EC50 value of the ABD-GCSF in proliferation of NFS-60 cells was 75.76 pg/ml after 72 h in comparison with control GCSF molecules (Filgrastim: 73.1 pg/ml and PEG-Filgrastim: 44.6 pg/ml). Animal studies of ABD-GCSF represented improved serum half-life (9.3 ± 0.7 h) and consequently reduced renal clearance (16.1 ± 1.4 ml/h.kg) in comparison with Filgrastim (1.7 ± 0.1 h). Enhanced neutrophils count following administration of ABD-GCSF was comparable with Filgrastim and weaker than PEG-Filgrastim treated rats. In vitro and in vivo results suggested the ABD fusion as a potential approach for improving GCSF properties.

Indexed as

Protein DomainsAlbuminsAnimalsCell LineCell ProliferationChemical PhenomenaDisease Models, AnimalEscherichia coliGranulocyte Colony-Stimulating FactorHalf-LifeHumansInclusion BodiesLeukocyte CountNeutropeniaNeutrophilsProtein BindingAlbuminsGranulocyte Colony-Stimulating Factor

Identifiers

PMID35027593
PMCPMC8758692
OpenAlexW4206427243

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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.