scholarly journals Undulating changes in human plasma proteome across lifespan are linked to disease

2019 ◽  
Author(s):  
Benoit Lehallier ◽  
David Gate ◽  
Nicholas Schaum ◽  
Tibor Nanasi ◽  
Song Eun Lee ◽  
...  
Keyword(s):  
Human Plasma ◽  
Plasma Proteins ◽  
Biological Pathways ◽  
Phenotypic Traits ◽  
Plasma Proteome ◽  
New Approach ◽  
Disease Biology ◽  
Age Related ◽  
Insight Into ◽  
Human Plasma Proteome

Aging is the predominant risk factor for numerous chronic diseases that limit healthspan. Mechanisms of aging are thus increasingly recognized as therapeutic targets. Blood from young mice reverses aspects of aging and disease across multiple tissues, pointing to the intriguing possibility that age-related molecular changes in blood can provide novel insight into disease biology. We measured 2,925 plasma proteins from 4,331 young adults to nonagenarians and developed a novel bioinformatics approach which uncovered profound non-linear alterations in the human plasma proteome with age. Waves of changes in the proteome in the fourth, seventh, and eighth decades of life reflected distinct biological pathways, and revealed differential associations with the genome and proteome of age-related diseases and phenotypic traits. This new approach to the study of aging led to the identification of unexpected signatures and pathways of aging and disease and offers potential pathways for aging interventions.

scholarly journals An Insight into the Changes in Human Plasma Proteome on Adaptation to Hypobaric Hypoxia

PLoS ONE ◽  
2013 ◽  
Vol 8 (7) ◽  
pp. e67548 ◽  
Author(s):  
Yasmin Ahmad ◽  
Narendra K. Sharma ◽  
Iti Garg ◽  
Mohammad Faiz Ahmad ◽  
Manish Sharma ◽  
...  
Keyword(s):  
Human Plasma ◽  
Hypobaric Hypoxia ◽  
Plasma Proteome ◽  
Insight Into ◽  
Human Plasma Proteome

scholarly journals Global chemical modifications comparison of human plasma proteome from two different age groups

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Yongtao Liu ◽  
Xuanzhen Pan ◽  
Mindi Zhao ◽  
Youhe Gao
Keyword(s):  
Human Plasma ◽  
Metabolic Diseases ◽  
Age Groups ◽  
Young Group ◽  
Tandem Mass ◽  
Plasma Proteome ◽  
Chemical Modifications ◽  
Old People ◽  
Age Related ◽  
Human Plasma Proteome

Abstract In this study, two groups of human plasma proteome at different age groups (old and young) were used to perform a comparison of global chemical modifications, as determined by tandem mass spectrometry (MS/MS) combined with non-limiting modification identification algorithms. The sulfhydryl in the cysteine A total of 4 molecular modifications were found to have significant differences passing random grouping tests: the succinylation and phosphorylation modification of cysteine (Cys, C) and the modification of lysine (Lys, K) with threonine (Thr, T) were significantly higher in the old group than in the young group, while the carbamylation of lysine was lower in the young group. We speculate that there is an increase in certain modified proteins in the blood of the old people which, in turn, changes the function of those proteins. This change may be one of the reasons why old people are more likely than young people to be at risk for age-related diseases, such as metabolic diseases, cerebral and cardiovascular diseases, and cancer.

Detectability of Plasma Proteins in SRM Measurements

2018 ◽  
Vol 16 (1) ◽  
pp. 74-81 ◽  
Author(s):  
Olga I. Kiseleva ◽  
Elena A. Ponomarenko ◽  
Yulia A. Romashova ◽  
Ekaterina V. Poverennaya ◽  
Andrey V. Lisitsa
Keyword(s):  
Blood Plasma ◽  
Human Plasma ◽  
Limit Of Detection ◽  
Human Blood Plasma ◽  
Analytical Sensitivity ◽  
Plasma Proteome ◽  
Protein Targets ◽  
Blood Plasma Sample ◽  
Specificity And Sensitivity ◽  
Human Plasma Proteome

Background: Liquid chromatography coupled with targeted mass spectrometry underwent rapid technical evolution during last years and has become widely used technology in clinical laboratories. It offers confident specificity and sensitivity superior to those of traditional immunoassays. However, due to controversial reports on reproducibility of SRM measurements, the prospects of clinical appliance of the method are worth discussing. </P><P> Objective: The study was aimed at assessment of capabilities of SRM to achieve a thorough assembly of the human plasma proteome. </P><P> Method: We examined set of 19 human blood plasma samples to measure 100 proteins, including FDA-approved biomarkers, via SRM-assay. </P><P> Results: Out of 100 target proteins 43 proteins were confidently detected in at least two blood plasma sample runs, 36 and 21 proteins were either not detected in any run or inconsistently detected, respectively. Empiric dependences on protein detectability were derived to predict the number of biological samples required to detect with certainty a diagnostically relevant quantum of the human plasma proteome. </P><P> Conclusion: The number of samples exponentially increases with an increase in the number of protein targets, while proportionally decreasing to the logarithm of the limit of detection. Analytical sensitivity and enormous proteome heterogeneity are major bottlenecks of the human proteome exploration.

Study of the human plasma proteome of rheumatoid arthritis

2009 ◽  
Vol 1216 (16) ◽  
pp. 3538-3545 ◽  
Author(s):  
Xiaoyang Zheng ◽  
Shiaw-lin Wu ◽  
Marina Hincapie ◽  
William S. Hancock
Keyword(s):  
Rheumatoid Arthritis ◽  
Human Plasma ◽  
Plasma Proteome ◽  
Human Plasma Proteome

scholarly journals Site specific modification of the human plasma proteome by methylglyoxal

2015 ◽  
Vol 289 (2) ◽  
pp. 155-162 ◽  
Author(s):  
Michael J. Kimzey ◽  
Owen R. Kinsky ◽  
Hussein N. Yassine ◽  
George Tsaprailis ◽  
Craig S. Stump ◽  
...  
Keyword(s):  
Human Plasma ◽  
Plasma Proteome ◽  
Site Specific ◽  
Specific Modification ◽  
Human Plasma Proteome
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