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Age‐related expression, enzymatic solubility and modification with advanced glycation end‐products of fibrillar collagens in mouse lung
Abstract
Changes in the expression of fibrillar collagens and post-translational modifications with advanced glycation end-products (AGEs) are often associated with tissue aging. Less is known about age-related changes in mouse lung tissue. Therefore, we studied the expression level and AGE load of fibrillar collagens in lungs from young (≤6 months), adult (15 months) and old (≥25 months) mice. The mRNA expression level was reduced in adult and old mice compared with the young. Old mice also showed a reduced protein level, whereas the adults even had more collagen protein. Fractionating of the fibrillar collagens into enzyme-soluble and insoluble collagens revealed a reduced solubility of collagens in old age. The enzymatic solubility of fibrillar collagens correlated inversely with the AGE load in the insoluble collagen as detected by the AGE-related fluorescence. While the intensity of the AGE-related fluorescence was increased in fibrillar collagens in response to age, the fluorescing AGE variant argpyrimidine was less affected. In summary, aging causes a reduced expression, lower enzymatic solubility and increased AGE load of fibrillar collagens in mouse lung tissue, but not all changes occur gradually with age.
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“One significant disadvantage of using human organs is the age-related changes of the extracellular matrix (ECM) [[30], [31], [32]].”
From Liver tissue engineering using decellularized scaffolds: Current progress, challenges, and opportunities (2024) · cites this paper as [31]
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“These changes in ECM microstructure can increase resistance to enzymatic digestion of the ECM and lead to significant discrepancies between human livers [30,31,35 – 38].”
Background
Metadata
- Authors
- Rolewska, P., Al-Robaiy, S., Navarrete Santos, A., Simm, A., Silber, R.-E., & Bartling, B.
- Affiliations
- University Hospital in Halle (DE)
- Corresponding author
- Bartling, Babett
- Venue
- Experimental Gerontology
- Publisher
- Elsevier BV
- Published
- 2013-01
- Volume
- 48
- Issue
- 1
- Pages
- 29-37
- ISSN
- 0531-5565 (ISSN-L)
- OpenAlex
- W1987081805
- Cited by
- 25
- References
- 0
- Citations by year
- 2025: 2 · 2024: 1 · 2023: 2 · 2022: 2 · 2021: 1 · 2019: 1 · 2018: 1 · 2017: 3 · 2015: 6 · 2014: 1 · 2013: 4
- FWCI
- 2.45
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Experimental Gerontology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Wilhelm Roux program at the Medical Faculty Halle (Saale) (VFI/A7)
- Deutsche Forschungsgemeinschaft (DFG (BA 2077/4-1)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Advanced Glycation End Products research
- Physical Sciences › Materials Science › Biomaterials › Collagen: Extraction and Characterization
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Aging › Genetics, Aging, and Longevity in Model Organisms
- Keywords
- fibrillar collagen, advanced glycation end products, lung aging, tissue aging, collagen expression, collagen solubility, post-translational modification, argpyrimidine, mouse lung
- MeSH terms
- Aging, Animals, Cells, Cultured, Female, Gene Expression Regulation, Lung, Male, Mice, Inbred C57BL, Protein Processing, Post-Translational, RNA, Messenger, Solubility, Glycation End Products, Advanced, Fibrillar Collagens, Mice
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