Journal of Mass Spectrometry and Advances in the Clinical Lab最新文献

{"title":"Corrigendum to “Observation of a positive interference in LC-MS/MS measurement of d6-25-OH-vitamin D3” [Clin. Mass Spectrom. 3 (2017) 22–24]","authors":"Danielle Fortuna , Warren R. Korn , Matthew J. Brune , Xiang He , Alexandre Y. Wang , John M. Hevko , Douglas F. Stickle","doi":"10.1016/j.jmsacl.2022.09.002","DOIUrl":"10.1016/j.jmsacl.2022.09.002","url":null,"abstract":"","PeriodicalId":52406,"journal":{"name":"Journal of Mass Spectrometry and Advances in the Clinical Lab","volume":null,"pages":null},"PeriodicalIF":2.2,"publicationDate":"2022-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/52/6f/main.PMC9471964.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40368541","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Corrigendum to “Use of the tau protein-to-peptide ratio in CSF to improve diagnostic classification of Alzheimer’s disease” [Clin. Mass Spectrom. 14 (Part B) (2019) 74–82]","authors":"Karl Hansson , Rahil Dahlén , Oskar Hansson , Elin Pernevik , Ross Paterson , Jonathan M. Schott , Nadia Magdalinou , Henrik Zetterberg , Kaj Blennow , Johan Gobom","doi":"10.1016/j.jmsacl.2022.08.002","DOIUrl":"10.1016/j.jmsacl.2022.08.002","url":null,"abstract":"","PeriodicalId":52406,"journal":{"name":"Journal of Mass Spectrometry and Advances in the Clinical Lab","volume":null,"pages":null},"PeriodicalIF":2.2,"publicationDate":"2022-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/f7/7d/main.PMC9523399.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40391841","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Critical need to assess modified and un-modified peptides in C-peptide standard materials","authors":"Zengru Wu, Kuanysh Kabytaev, Jianying Mu, Shawn Connolly, Nigel J. Clarke, Randie Little, Michael J. McPhaul","doi":"10.1016/j.jmsacl.2022.07.003","DOIUrl":"10.1016/j.jmsacl.2022.07.003","url":null,"abstract":"","PeriodicalId":52406,"journal":{"name":"Journal of Mass Spectrometry and Advances in the Clinical Lab","volume":null,"pages":null},"PeriodicalIF":2.2,"publicationDate":"2022-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9440418/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40352874","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Molecular phenotyping approaches for the detection and monitoring of carbapenem-resistant Enterobacteriaceae by mass spectrometry","authors":"Breanna Dixon ,&nbsp;Waqar M Ahmed ,&nbsp;Tim Felton ,&nbsp;Stephen J Fowler","doi":"10.1016/j.jmsacl.2022.09.001","DOIUrl":"10.1016/j.jmsacl.2022.09.001","url":null,"abstract":"<div><p>Antimicrobial resistance is increasing in prevalence and there is a clear need for the development of rapid detection methods in clinical diagnostics. This review explores –omics studies utilising mass spectrometry to investigate the molecular phenotype associated with carbapenem resistance. Whilst the specific mechanisms of carbapenem resistance are well characterised, the resistant phenotype is poorly understood. Understanding how the acquisition of resistance affects cellular physiology and cell metabolism through molecular phenotyping is a necessary step towards detecting resistance by diagnostic means. In addition, this article examines the potential of mass spectrometry for the identification of resistance biomarkers through molecular profiling of bacteria. Developments in mass spectrometry platforms are expanding the biomarker-based diagnostic landscape. Targeted measures, such as high-resolution mass spectrometry coupled with chromatographic separation show considerable promise for the identification of molecular signatures and the development of a rapid diagnostic assay for the detection of carbapenem resistance.</p></div>","PeriodicalId":52406,"journal":{"name":"Journal of Mass Spectrometry and Advances in the Clinical Lab","volume":null,"pages":null},"PeriodicalIF":2.2,"publicationDate":"2022-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/14/a4/main.PMC9464899.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40359223","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Corrigendum to “Mass spectrometry for therapeutic drug monitoring of anti-tuberculosis drugs” [Clin. Mass Spectrom. 14(Part A) (2019) 34–45]","authors":"Johanna Kuhlin ,&nbsp;Marieke G.G. Sturkenboom ,&nbsp;Samiksha Ghimire ,&nbsp;Ioana Margineanu ,&nbsp;Simone H.J. van den Elsen ,&nbsp;Noviana Simbar ,&nbsp;Onno W. Akkerman ,&nbsp;Erwin M. Jongedijk ,&nbsp;Remco A. Koster ,&nbsp;Judith Bruchfeld ,&nbsp;Daan J. Touw ,&nbsp;Jan-Willem C. Alffenaar","doi":"10.1016/j.jmsacl.2022.08.001","DOIUrl":"10.1016/j.jmsacl.2022.08.001","url":null,"abstract":"","PeriodicalId":52406,"journal":{"name":"Journal of Mass Spectrometry and Advances in the Clinical Lab","volume":null,"pages":null},"PeriodicalIF":2.2,"publicationDate":"2022-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/e5/f5/main.PMC9400071.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"33444768","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Multiplexed quantification of insulin and C-peptide by LC-MS/MS without the use of antibodies","authors":"North Foulon ,&nbsp;Elisha Goonatilleke ,&nbsp;Michael J. MacCoss ,&nbsp;Michelle A. Emrick ,&nbsp;Andrew N. Hoofnagle","doi":"10.1016/j.jmsacl.2022.06.003","DOIUrl":"10.1016/j.jmsacl.2022.06.003","url":null,"abstract":"<div><h3>Introduction</h3><p>The measurement of insulin and C-peptide provides a valuable tool for the clinical evaluation of hypoglycemia. In research, these biomarkers are used together to better understand hyperinsulinemia, hepatic insulin clearance, and beta cell function. Liquid chromatography-tandem mass spectrometry (LC-MS/MS) is an attractive approach for the analysis of insulin and C-peptide because the platform is specific, can avoid certain limitations of immunoassays, and can be multiplexed. Previously described LC-MS/MS methods for the simultaneous quantification of insulin and C-peptide measure the intact analytes and most have relied on immunoaffinity enrichment. These approaches can be limited in terms of sensitivity and interference from auto-antibodies, respectively. We have developed a novel method that does not require antibodies and uses proteolytic digestion to yield readily ionizable proteotypic peptides that enables the sensitive, specific, and simultaneous quantitation of insulin and C-peptide.</p></div><div><h3>Methods</h3><p>Serum samples were precipitated with acetonitrile. Analytes were enriched using solid phase extraction and then digested with endoproteinase Glu-C. Surrogate peptides for insulin and C-peptide were analyzed using targeted LC-MS/MS.</p></div><div><h3>Results</h3><p>Inter-day imprecision was below 20 %CV and linearity was observed down to the lower limit of quantitation for both analytes (insulin = 0.09 ng/mL, C-peptide = 0.06 ng/mL). Comparison to a commercially available insulin immunoassay (Beckman Coulter UniCel DxI 600 Access) revealed a 30% bias between methods.</p></div><div><h3>Conclusion</h3><p>A novel LC-MS/MS method for the simultaneous analysis of insulin and C-peptide using Glu-C digestion was developed and evaluated. A detailed standard operating procedure is provided to help facilitate implementation in other laboratories.</p></div>","PeriodicalId":52406,"journal":{"name":"Journal of Mass Spectrometry and Advances in the Clinical Lab","volume":null,"pages":null},"PeriodicalIF":2.2,"publicationDate":"2022-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/e5/9e/main.PMC9207678.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40238936","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Quantitation of non-derivatized free amino acids for detecting inborn errors of metabolism by incorporating mixed-mode chromatography with tandem mass spectrometry","authors":"Patrick D. DeArmond ,&nbsp;Dustin R. Bunch","doi":"10.1016/j.jmsacl.2022.05.002","DOIUrl":"10.1016/j.jmsacl.2022.05.002","url":null,"abstract":"<div><h3>Introduction</h3><p>Amino acids are critical biomarkers for many inborn errors of metabolism, but amino acid analysis is challenging due to the range of chemical properties inherent in these small molecules. Techniques are available for amino acid analysis, but they can suffer from long run times, laborious derivatization, and/or poor resolution of isobaric compounds.</p></div><div><h3>Objective</h3><p>To develop and validate a method for the quantitation of a non-derivatized free amino acid profile in both plasma and urine samples using mixed-mode chromatography and tandem mass spectrometry.</p></div><div><h3>Methods</h3><p>Chromatographic conditions were optimized to separate leucine, isoleucine, and allo-isoleucine and maintain analytical runtime at less than 15 min. Sample preparation included a quick protein precipitation followed by LC-MS/MS analysis. Matrix effects, interferences, linearity, carryover, acceptable dilution limits, precision, accuracy, and stability were evaluated in both plasma and urine specimen types.</p></div><div><h3>Results</h3><p>A total of 38 amino acids and related compounds were successfully quantitated with this method. In addition, argininosuccinic acid was qualitatively analyzed. A full clinical validation was performed that included method comparison to a reference laboratory for plasma and urine with Deming regression slopes ranging from 0.38 to 1.26.</p></div><div><h3>Conclusion</h3><p>This method represents an alternative to derivatization-based methods, especially in urine samples where interference from metabolites and medications is prevalent.</p></div>","PeriodicalId":52406,"journal":{"name":"Journal of Mass Spectrometry and Advances in the Clinical Lab","volume":null,"pages":null},"PeriodicalIF":2.2,"publicationDate":"2022-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2667145X22000153/pdfft?md5=d9c392ee9a08d22e45e619410635f8bc&pid=1-s2.0-S2667145X22000153-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"76651043","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Targeted metabolic profiling of urinary steroids with a focus on analytical accuracy and sample stability","authors":"Nora Vogg ,&nbsp;Tobias Müller ,&nbsp;Andreas Floren ,&nbsp;Thomas Dandekar ,&nbsp;Oliver Scherf-Clavel ,&nbsp;Martin Fassnacht ,&nbsp;Matthias Kroiss ,&nbsp;Max Kurlbaum","doi":"10.1016/j.jmsacl.2022.07.006","DOIUrl":"10.1016/j.jmsacl.2022.07.006","url":null,"abstract":"<div><h3>Introduction</h3><p>Preoperative diagnostic workup of adrenal tumors is based on imaging and hormone analyses, but charged with uncertainties. Steroid profiling by liquid chromatography tandem mass spectrometry (LC-MS/MS) in 24-h urine has shown potential to discriminate benign and malignant adrenal tumors. Our aim was to develop and validate a specific and accurate LC-MS/MS method for the quantification of deconjugated urinary marker steroids, to evaluate their pre-analytical stability and to apply the method to clinical samples of patients with adrenal tumors.</p></div><div><h3>Methods</h3><p>A method for the quantification of 11 deconjugated steroids (5-pregnenetriol, dehydroepiandrosterone, cortisone, cortisol, α-cortolone, tetrahydro-11-deoxycortisol, etiocholanolone, pregnenolone, pregnanetriol, pregnanediol, and 5-pregnenediol) in human urine was developed and validated based on international guidelines. Steroids were enzymatically deconjugated and extracted by solid phase extraction before LC-MS/MS quantification in positive electrospray ionization mode.</p></div><div><h3>Results</h3><p>Excellent linearity with R² &gt; 0.99 and intra- and inter-day precisions of &lt; 10.1 % were found. Relative matrix effects were between 96.4 % and 101.6 % and relative recovery was between 98.2 % and 115.0 %. Sufficient pre-freeze stability for all steroids in urine was found at 20–25 °C for seven days and at 4–6 °C for up to 28 days. Samples were stable during long-term storage at −20 °C and −80 °C for 6 months.</p></div><div><h3>Conclusions</h3><p>A sensitive and robust LC-MS/MS method for the quantification of 11 urinary steroids was developed and validated according to international guidelines. Pre-analytical matrix stability was evaluated and the suitability of the method for the analysis of clinical samples and prospective validation studies was shown.</p></div>","PeriodicalId":52406,"journal":{"name":"Journal of Mass Spectrometry and Advances in the Clinical Lab","volume":null,"pages":null},"PeriodicalIF":2.2,"publicationDate":"2022-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/33/df/main.PMC9334310.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40589851","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Haptoglobin polymorphism affects its N-glycosylation pattern in serum","authors":"M. Kohansal-Nodehi,&nbsp;M. Swiatek-de Lange,&nbsp;G. Tabarés,&nbsp;H. Busskamp","doi":"10.1016/j.jmsacl.2022.07.001","DOIUrl":"10.1016/j.jmsacl.2022.07.001","url":null,"abstract":"<div><h3>Introduction</h3><p>Haptoglobin (Hp) is an abundant acute-phase protein secreted mainly by the liver into the bloodstream. There are three Hp protein phenotypes (Hp type 1–1, 2–1, and 2–2), which differ in the number of α- and β-chains, type of α-chain (the β-chain type remains the same in all the Hp phenotypes), and the polymers that they form via disulfide bonds. Hp has four N-glycosylation sites on the β-chain. Glycosylation of Hp has been reported frequently as a potential glycobiomarker for many diseases; however, whether Hp polymorphism affects its glycosylation has not yet been addressed extensively or in depth.</p></div><div><h3>Objectives</h3><p>This study investigated the differences between the glycosylation patterns of Hp phenotypes using serum from 12 healthy individuals (four for each Hp phenotype).</p></div><div><h3>Method</h3><p>An efficient method for isolating Hp from serum was established and subsequently the Hp phenotype of each sample was characterized by immunoblotting. Then, LC-MS/MS analysis of isolated Hp after treatment with three exoglycosidases (sialidase, α2-3 neuraminidase, Endo F3) was performed to characterize the glycosylation pattern of Hp for each individual sample.</p></div><div><h3>Results</h3><p>The data reveal significant differences among the branching, sialylation, and fucosylation of Hp types, documenting the effect of Hp polymorphism on its glycosylation.</p></div><div><h3>Conclusion</h3><p>Overall, the study suggests that Hp phenotype characterization should be considered during the investigation of Hp glycosylation.</p></div>","PeriodicalId":52406,"journal":{"name":"Journal of Mass Spectrometry and Advances in the Clinical Lab","volume":null,"pages":null},"PeriodicalIF":2.2,"publicationDate":"2022-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/a6/08/main.PMC9352458.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40594166","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Corrigendum to “Analytical validation of protein biomarkers for risk of spontaneous preterm birth” [Clin. Mass Spectrom. 3 (2017) 25–38]","authors":"Chad Bradford ,&nbsp;Rob Severinsen ,&nbsp;Trina Pugmire ,&nbsp;Matison Rasmussen ,&nbsp;Kathryn Stoddard ,&nbsp;Yuta Uemura ,&nbsp;Spencer Wheelwright ,&nbsp;Marija Mentinova ,&nbsp;Daniel Chelsky ,&nbsp;Stephen W. Hunsucker ,&nbsp;Paul Kearney ,&nbsp;Durlin Hickok ,&nbsp;Tracey C. Fleischer ,&nbsp;Ilia Ichetovkin ,&nbsp;J. Jay Boniface ,&nbsp;Gregory C. Critchfield ,&nbsp;John M. Peltier","doi":"10.1016/j.jmsacl.2022.07.007","DOIUrl":"10.1016/j.jmsacl.2022.07.007","url":null,"abstract":"","PeriodicalId":52406,"journal":{"name":"Journal of Mass Spectrometry and Advances in the Clinical Lab","volume":null,"pages":null},"PeriodicalIF":2.2,"publicationDate":"2022-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/cc/4b/main.PMC9372730.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40700462","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}