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Study Objectives Sleep deprivation is highly prevalent and caused by conditions such as night shift work or illnesses like obstructive sleep apnea. Compromised sleep affects cardiovascular-, immune-, and neuronal systems. Recently, we published human serum proteome changes after a simulated night shift. This pilot proteomic study aimed to further explore changes in human blood serum after 6 h of sleep deprivation at night. Methods Human blood serum samples from 8 self-declared healthy females were analyzed using Orbitrap Eclipse mass spectrometry (MS-MS) and high-pressure liquid chromatography (HPLC). We used a within-subject design, in which the samples were taken after 6 h of sleep at night and after 6h of sleep deprivation the following night. Systems biological databases and bioinformatic software were used to analyze the data and comparative analysis were done with other published sleep-related proteomic datasets. Results Out of 494 proteins, 66 were found to be differentially expressed proteins (DEPs) after 6 h of sleep deprivation. Functional enrichment analysis revealed the associations of these DEPs with several biological functions related to the altered regulation of cellular processes such as platelet degranulation and blood coagulation, as well as associations with different curated gene sets. Conclusions This study presents serum proteomic changes after 6 h of sleep deprivation, supports previous findings showing that short sleep deprivation affects several biological processes, and revealed a molecular signature of proteins related to pathological conditions such as altered coagulation and platelet function, impaired lipid and immune function, and cell proliferation. Data are available via ProteomeXchange with identifier PXD045729. This paper is part of the Genetic and other molecular underpinnings of sleep, sleep disorders, and circadian rhythms including translational approaches Collection.
Study Objectives Sleep deprivation is highly prevalent and caused by conditions such as night shift work or illnesses like obstructive sleep apnea. Compromised sleep affects cardiovascular-, immune-, and neuronal systems. Recently, we published human serum proteome changes after a simulated night shift. This pilot proteomic study aimed to further explore changes in human blood serum after 6 h of sleep deprivation at night. Methods Human blood serum samples from 8 self-declared healthy females were analyzed using Orbitrap Eclipse mass spectrometry (MS-MS) and high-pressure liquid chromatography (HPLC). We used a within-subject design, in which the samples were taken after 6 h of sleep at night and after 6h of sleep deprivation the following night. Systems biological databases and bioinformatic software were used to analyze the data and comparative analysis were done with other published sleep-related proteomic datasets. Results Out of 494 proteins, 66 were found to be differentially expressed proteins (DEPs) after 6 h of sleep deprivation. Functional enrichment analysis revealed the associations of these DEPs with several biological functions related to the altered regulation of cellular processes such as platelet degranulation and blood coagulation, as well as associations with different curated gene sets. Conclusions This study presents serum proteomic changes after 6 h of sleep deprivation, supports previous findings showing that short sleep deprivation affects several biological processes, and revealed a molecular signature of proteins related to pathological conditions such as altered coagulation and platelet function, impaired lipid and immune function, and cell proliferation. Data are available via ProteomeXchange with identifier PXD045729. This paper is part of the Genetic and other molecular underpinnings of sleep, sleep disorders, and circadian rhythms including translational approaches Collection.
Serum or plasma is frequently utilized in biomedical research; however, its application is impeded by the requirement for invasive sample collection. The non-invasive nature of urine collection makes it an attractive alternative for disease characterization and biomarker discovery. Mass spectrometry-based protein profiling of urine has led to the discovery of several disease-associated biomarkers. Proteomic analysis of urine has not only been applied to disorders of the kidney and urinary bladder but also to conditions affecting distant organs because proteins excreted in the urine originate from multiple organs. This review provides a progress update on urinary proteomics carried out over the past decade. Studies summarized in this review have expanded the catalog of proteins detected in the urine in a variety of clinical conditions. The wide range of applications of urine analysis—from characterizing diseases to discovering predictive, diagnostic and prognostic markers—continues to drive investigations of the urinary proteome.
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