Age-Related Differences in Plasma Proteins: How Plasma Proteins Change from Neonates to Adults
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The incidence of major diseases such as cardiovascular disease, thrombosis and cancer increases with age and is the major cause of mortality world-wide, with neonates and children somehow protected from such diseases of ageing. We hypothesized that there are major developmental differences in plasma proteins and that these contribute to age-related changes in the incidence of major diseases. We evaluated the human plasma proteome in healthy neonates, children and adults using the 2D-DIGE approach. We demonstrate significant changes in number and abundance of up to 100 protein spots that have marked differences in during the transition of the plasma proteome from neonate and child through to adult. These proteins are known to be involved in numerous physiological processes such as iron transport and homeostasis, immune response, haemostasis and apoptosis, amongst others. Importantly, we determined that the proteins that are differentially expressed with age are not the same proteins that are differentially expressed with gender and that the degree of phosphorylation of plasma proteins also changes with age. Given the multi-functionality of these proteins in human physiology, understanding the differences in the plasma proteome in neonates and children compared to adults will make a major contribution to our understanding of developmental biology in humans.
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Studies using multiple proteomic technologies have shown that thousands of proteins change with age in human plasma and cerebrospinal fluid.
“Studies using multiple proteomic technologies have shown that thousands of proteins change with age in human plasma91–93 and cerebrospinal fluid94, which has recently led to the development of multiple proteomic ageing clocks.”
From Measuring biological age using omics data (2022) · cites this paper as [92]
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- Authors
- Ignjatovic, V., Lai, C., Summerhayes, R., Mathesius, U., Tawfilis, S., Perugini, M. A., & Monagle, P.
- Affiliations
- Royal Children's Hospital (AU)
- Australian National University (AU)
- The University of Melbourne (AU)
- Venue
- PLoS ONE
- Publisher
- Public Library of Science (PLoS)
- Published
- 2011-02-18
- Volume
- 6
- Issue
- 2
- Pages
- e17213
- ISSN
- 1932-6203 (ISSN-L)
- PMC
- PMC3041803
- OpenAlex
- W1971352522
- Cited by
- 132
- References
- 32
- Citations by year
- 2026: 6 · 2025: 8 · 2024: 6 · 2023: 7 · 2022: 5 · 2021: 14 · 2020: 16 · 2019: 11 · 2018: 9 · 2017: 6 · 2016: 7 · 2015: 4 · 2014: 15 · 2013: 6 · 2012: 8
- FWCI
- 4.65
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- PLoS ONE (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Minerva Access (University of Melbourne) (submittedVersion, cc-by)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- ANU Open Research (Australian National University) (submittedVersion, cc-by)
- Funders
- University of Melbourne
- Topics
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Advanced Biosensing Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Aging › Genetics, Aging, and Longevity in Model Organisms
- Keywords
- plasma proteome, age-related changes, neonates, children, developmental differences, protein phosphorylation, iron transport, hemostasis, immune response, apoptosis, sex differences, 2D-DIGE, human development
- MeSH terms
- Adolescent, Adult, Age Factors, Aging, Blood Proteins, Child, Child, Preschool, Female, Humans, Infant, Infant, Newborn, Male, Phosphoproteins, Electrophoresis, Gel, Two-Dimensional, Proteome, Validation Studies as Topic
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