Primary structure of human J chain: isolation and characterization of tryptic and chymotryptic peptides of human J chain

As, Bhown; Je, Mole; Jc, Bennett

doi:10.1021/bi00635a001

Cited by 3 publications

(2 citation statements)

References 17 publications

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“…Collins et al [6] conducted mass-spectrometry-based biomarker discovery using ALS CSF and reported that FSTL4 was decreased in ALS CSF in consistency with our result. JCHAIN, which was increased in ALS in our study, is a protein component of immunoglobulins A and M working as a glue for the formation of multimeric immunoglobulins [58]. However, its relationship with ALS is not known yet.…”

Section: Discussionmentioning

confidence: 49%

Discovery of Biomarkers for Amyotrophic Lateral Sclerosis from Human Cerebrospinal Fluid Using Mass-Spectrometry-Based Proteomics

Jang

2023

Biomedicines

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Amyotrophic lateral sclerosis (ALS) is a progressive neurodegenerative disease characterized by the loss of upper and lower motor neurons, which eventually may lead to death. Critical to the mission of developing effective therapies for ALS is the discovery of biomarkers that can illuminate mechanisms of neurodegeneration and have diagnostic, prognostic, or pharmacodynamic value. Here, we merged unbiased discovery-based approaches and targeted quantitative comparative analyses to identify proteins that are altered in cerebrospinal fluid (CSF) from patients with ALS. Mass spectrometry (MS)-based proteomic approaches employing tandem mass tag (TMT) quantification methods from 40 CSF samples comprising 20 patients with ALS and 20 healthy control (HC) individuals identified 53 proteins that are differential between the two groups after CSF fractionation. Notably, these proteins included both previously identified ones, validating our approach, and novel ones that have the potential for expanding biomarker repertoire. The identified proteins were subsequently examined using parallel reaction monitoring (PRM) MS methods on 61 unfractionated CSF samples comprising 30 patients with ALS and 31 HC individuals. Fifteen proteins (APOB, APP, CAMK2A, CHI3L1, CHIT1, CLSTN3, ERAP2, FSTL4, GPNMB, JCHAIN, L1CAM, NPTX2, SERPINA1, SERPINA3, and UCHL1) showed significant differences between ALS and the control. Taken together, this study identified multiple novel proteins that are altered in ALS, providing the foundation for developing new biomarkers for ALS.

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Section: Discussionmentioning

confidence: 49%

Discovery of Biomarkers for Amyotrophic Lateral Sclerosis from Human Cerebrospinal Fluid Using Mass-Spectrometry-Based Proteomics

Jang

2023

Biomedicines

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“…In one, samples were dialyzed against 0.1 M acetic acid at 40C, lyophilized and processed in a B3eckman 890C sequencer with a 1M Quadrol program. Phenylthiohydantion derivatives were identified by high-pressure liquid chromatography as described by Bhown et al (1). In the second procedure, the sample, dialyzed against 10%o acetic acid at 4°C and lyophilized, was dissolved in 0.4 M N,N-dimethyl-N-allylamide/pyridine buffer, attached to isothiocyanato glass (2), and run on a Sequemat model 12 sequencer with a P-6 autoconverter.…”

mentioning

confidence: 99%