Evidence map›Paper›PMID 34678250›Full record

ArticleAnalytical biochemistry2021

Analysis of N

Ninad Varkhede, Peters Björn-Hendrik, K Ryan Moulder, Philip Gao, Christian Schöneich, M Laird Forrest

Open access · greenAbstract read
In one paragraph

Article in Analytical biochemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact, top 79% 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

0 citing papers in PubMed, 0 citations in OpenAlex.

No citing paper in PubMed yet.

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

6 authors at 1 institution in 2 countries.

Ninad VarkhedeDepartment of Pharmaceutical Chemistry, The University of Kansas, Kansas, 66047, Lawrence, USA; Current: Pharmacokinetics, Pharmacodynamics and Drug Metabolism (PPDM), Merck Research Laboratories, West Point, 19486, Pennsylvania, USA.
Peters Björn-HendrikDepartment of Pharmaceutical Chemistry, The University of Kansas, Kansas, 66047, Lawrence, USA; Sterile Product Development, Bristol Myers Squibb, New Jersey, 08901, New Brunswick, USA.
K Ryan MoulderDepartment of Pharmaceutical Chemistry, The University of Kansas, Kansas, 66047, Lawrence, USA.
Philip GaoCOBRE Protein Production Group, University of Kansas, Kansas, 66047, Lawrence, USA.
Christian SchöneichDepartment of Pharmaceutical Chemistry, The University of Kansas, Kansas, 66047, Lawrence, USA.
M Laird ForrestDepartment of Pharmaceutical Chemistry, The University of Kansas, Kansas, 66047, Lawrence, USA. Electronic address: lforrest@ku.edu.
University of Kansas · US

Funding

Biomaterials for treatment of head and neck cancerR01CA173292 · NCI · UNIVERSITY OF KANSAS LAWRENCE · PI FORREST, MARCUS LAIRD · 2013 to 2017
$1.4M
NCI NIH HHS R01 CA173292
6 · The paper itself

Abstract

Therapeutic proteins (TPs) are exposed to various immune cells like macrophages and neutrophils, especially after subcutaneous (SC) administration. It is well known that the immune cells can generate reactive oxygen species (ROS) and this may lead to oxidation of TPs. The oxidation can occur in the SC tissue after SC administration, during distribution to the immune organs like lymph nodes and spleen, and even in the blood circulation. The oxidation can lead to alteration of their pharmacokinetics and efficacy. Therefore, it is important to study the oxidation of TPs in the biological matrices using ultra-pressure chromatography-mass spectrometry. Rat growth hormone (rGH) was selected as a test protein due to its similarity with human growth hormone (hGH), which is widely used for treatment of growth hormone deficiency. In this manuscript, we have summarized sample processing strategy and ultra-pressure chromatography-mass spectrometry methodology to identify rGH and its degradation products after ex-vivo incubation with rat SC tissue, and in vitro incubation with rat splenocytes and canine peripheral blood mononuclear cells (cPBMCs) as a model foreign host species. We did not observe oxidation of rGH in these biological matrices. This could be due to very minor yields of oxidation products, lack of sensitivity of the mass spectrometry method, loss of protein during sample processing, rapid turnover of oxidized protein or a combination of all factors.

Indexed as

AnimalsChromatographyDogsGrowth HormoneHuman Growth HormoneHumansImmune SystemInjections, SubcutaneousLeukocytes, MononuclearMaleMass SpectrometryOxidation-ReductionRatsReactive Oxygen SpeciesSpleenSubcutaneous TissueGrowth HormoneHuman Growth HormoneReactive Oxygen SpeciesImmune cellsMass spectrometryProteomicsRat growth hormoneSubcutaneous tissueTherapeutic protein

Identifiers

PMID34678250
PMCPMC8599641
OpenAlexW3207946139

What OpenQuestion holds

Textmetadata
LicenceTDM
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.