ArticleScientific reports2019
A next generation setup for pre-fractionation of non-denatured proteins reveals diverse albumin proteoforms each carrying several post-translational modifications.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Urinary Protein-Biomarkers Reliably Indicate Very Early Kidney Damage in Children With Alport Syndrome Independently of Albuminuria and Inflammation.Kidney international reports · 2023Article
- Advancements in automation for plasma proteomics sample preparation.Molecular omics · 2022Review
- Glycemic control is not related to cerebral small vessel disease in neurologically asymptomatic individuals with type 1 diabetes.Acta diabetologica · 2022Article
- MicroRNAs as Biomarkers of Charcot-Marie-Tooth Disease Type 1A.Neurology · 2021Article
- Transmembrane protease serine 5: a novel Schwann cell plasma marker for CMT1A.Annals of clinical and translational neurology · 2020Article
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Authors and funding
10 authors.
Funding
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Abstract
Proteomic biomarker search requires the greatest analytical reproducibility and detailed information on altered proteoforms. Our protein pre-fractionation applies orthogonal native chromatography and conserves important features of protein variants such as native molecular weight, charge and major glycans. Moreover, we maximized reproducibility of sample pre-fractionation and preparation before mass spectrometry by parallelization and automation. In blood plasma and cerebrospinal fluid (CSF), most proteins, including candidate biomarkers, distribute into a multitude of chromatographic clusters. Plasma albumin, for example, divides into 15-17 clusters. As an example of our technique, we analyzed these albumin clusters from healthy volunteers and from dogs and identified cluster-typical modification patterns. Renal disease further modifies these patterns. In human CSF, we found only a subset of proteoforms with fewer modifications than in plasma. We infer from this example that our method can be used to identify and characterize distinct proteoforms and, optionally, enrich them, thereby yielding the characteristics of proteoform-selective biomarkers.
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