Evidence map›Paper›PMID 35838770›Full record

ArticleAnalytical and bioanalytical chemistry2022

Selective quantification of the 22-kDa isoform of human growth hormone 1 in serum and plasma by immunocapture and LC-MS/MS.

Bas Sleumer, Martijn van Faassen, Michel J Vos, Rainer Bischoff, Ido P Kema, Nico C van de Merbel

Open access · hybridAbstract read
In one paragraph

Article in Analytical and bioanalytical chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
1.5field-weighted citation impact, top 16% 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

3 citing papers in PubMed, 11 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
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 2 institutions in 1 country.

Bas SleumerICON Bioanalytical Laboratories, Amerikaweg 18, 9407 TK, Assen, The Netherlands.
Martijn van FaassenDepartment of Laboratory Medicine, University of Groningen, University Medical Center Groningen, EA61, P.O. Box 30.001, 9700 RB, Groningen, The Netherlands.
Michel J VosDepartment of Laboratory Medicine, University of Groningen, University Medical Center Groningen, EA61, P.O. Box 30.001, 9700 RB, Groningen, The Netherlands.
Rainer BischoffDepartment of Analytical Biochemistry, University of Groningen, A. Deusinglaan 1, 9700 AV, Groningen, The Netherlands.
Ido P KemaDepartment of Laboratory Medicine, University of Groningen, University Medical Center Groningen, EA61, P.O. Box 30.001, 9700 RB, Groningen, The Netherlands.
Nico C van de MerbelICON Bioanalytical Laboratories, Amerikaweg 18, 9407 TK, Assen, The Netherlands. n.c.van.de.merbel@rug.nl.
University of Groningen · NLUniversity Medical Center Groningen · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The human growth hormone GH1 (22 kDa) is a commonly measured biomarker for diagnosis and during treatment of growth disorders, but its quantification by ligand binding assays may be compromised by the occurrence of a number of isoforms. These can interfere in the assays and lead to differences in results between laboratories and potentially even in the treatment of patients. We present an LC-MS/MS method that is able to distinguish the major growth hormone isoform (GH1, 22 kDa) from other isoforms and quantify it without any interference across the clinically relevant concentration range of 0.5 to 50 ng/mL. Analysis involves purification of a 100-µL serum sample by immunocapture using an anti-GH-directed antibody, tryptic digestion, and LC-MS/MS quantification of an isoform-specific signature peptide for GH1 (22 kDa). A tryptic peptide occurring in all GH isoforms is monitored in the same 16-min analytical run as a read-out for total GH. Stable-isotope-labeled forms of these two peptides are included as internal standards. Full validation of the method according to recent guidelines, against a recombinant form of the analyte in rat plasma calibrators, demonstrated intra-assay and inter-assay imprecision below 6% across the calibration range for both signature peptides and recoveries between 94 and 102%. An excellent correlation was found between nominal and measured concentrations of the WHO reference standard for GH1 (22 kDa). Addition of up to 1000 ng/mL biotin or the presence of a 100-fold excess of GH binding protein did not affect the measurement. Equivalent method performance was found for analysis of GH in serum, EDTA, and heparin plasma. Analyte stability was demonstrated during all normal sample storage conditions. Comparison with the IDS-iSYS GH immunoassay showed a good correlation with the LC-MS/MS method for the isoform-specific signature peptide, but a significant positive bias was observed for the LC-MS/MS results of the peptide representing total GH. This seems to confirm the actual occurrence of other GH isoforms in serum. Finally, in serum from pregnant individuals, no quantifiable GH1 (22 kDa) was found, but relatively high concentrations of total GH.

Indexed as

Human Growth HormoneAnimalsChromatography, LiquidGrowth HormoneHumansPeptidesProtein IsoformsRatsRecombinant ProteinsTandem Mass SpectrometryGrowth HormoneHuman Growth HormonePeptidesProtein IsoformsRecombinant ProteinsBiomarkerHuman growth hormoneImmunocaptureIsoformLiquid chromatography-tandem mass spectrometry (LC–MS/MS)

Identifiers

PMID35838770
PMCPMC9314277
OpenAlexW4285590823

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.