Advanced glycation end products increases in aging human skeletal muscle
PhysiologicalData Availability
22
to
93
years
Tissue
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muscle
Changes
⇩
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anatomical site
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thorax
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- leukocyte
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thymus
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anatomical site
-
Anatomical System
References
- Haus, JM et al. (2007) "Collagen, cross-linking, and advanced glycation end products in aging human skeletal muscle." J. Appl. Physiol. 103(6):2068-2076 (PubMed)
External Links
Description
Study of young (22-30 years old; mean 25) and old (70-93 years old; mean 78) healthy sedentary individuals showed that the amount of advanced glycation end products increases by ~200% with ageing. In contrast, collagen concentration and pyridinoline cross-links are not significantly changed with aging. Additionally, all general skeletal muscle protein pools are reduced with aging (myofibrillar by 5%, sarcoplasmic by 8%), while the two main contractile proteins, myosin and actin, are not significantly changed. The proportion of MHC I in the muscle increases with aging, whereas MHC IIa and IIx are reduced.