scholarly journals Advanced Glycation End-Products in Skeletal Muscle Aging

2021 ◽  
Vol 8 (11) ◽  
pp. 168
Author(s):  
Lucas C. Olson ◽  
James T. Redden ◽  
Zvi Schwartz ◽  
David J. Cohen ◽  
Michael J. McClure
Keyword(s):  
Skeletal Muscle ◽  
Advanced Glycation End Products ◽  
Future Research ◽  
Cross Linking ◽  
Advanced Glycation ◽  
Muscle Aging ◽  
Glycation End Products ◽  
End Products ◽  
Skeletal Muscle Aging

Advanced age causes skeletal muscle to undergo deleterious changes including muscle atrophy, fast-to-slow muscle fiber transition, and an increase in collagenous material that culminates in the age-dependent muscle wasting disease known as sarcopenia. Advanced glycation end-products (AGEs) non-enzymatically accumulate on the muscular collagens in old age via the Maillard reaction, potentiating the accumulation of intramuscular collagen and stiffening the microenvironment through collagen cross-linking. This review contextualizes known aspects of skeletal muscle extracellular matrix (ECM) aging, especially the role of collagens and AGE cross-linking, and underpins the motor nerve’s role in this aging process. Specific directions for future research are also discussed, with the understudied role of AGEs in skeletal muscle aging highlighted. Despite more than a half century of research, the role that intramuscular collagen aggregation and cross-linking plays in sarcopenia is well accepted yet not well integrated with current knowledge of AGE’s effects on muscle physiology. Furthermore, the possible impact that motor nerve aging has on intramuscular cross-linking and muscular AGE levels is posited.

scholarly journals Advanced Glycation End Products Are Retained in Decellularized Muscle Matrix Derived from Aged Skeletal Muscle

2021 ◽  
Vol 22 (16) ◽  
pp. 8832
Author(s):  
Lucas C. Olson ◽  
Tri M. Nguyen ◽  
Rebecca L. Heise ◽  
Barbara D. Boyan ◽  
Zvi Schwartz ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Advanced Glycation End Products ◽  
Cross Linking ◽  
Advanced Glycation ◽  
Glycation End Products ◽  
End Products ◽  
Age Dependent ◽  
Before And After ◽  
The Matrix ◽  
Cross Links

Decellularized tissues are biocompatible materials that engraft well, but the age of their source has not been explored for clinical translation. Advanced glycation end products (AGEs) are chemical cross-links that accrue on skeletal muscle collagen in old age, stiffening the matrix and increasing inflammation. Whether decellularized biomaterials derived from aged muscle would suffer from increased AGE collagen cross-links is unknown. We characterized gastrocnemii of 1-, 2-, and 20-month-old C57BL/6J mice before and after decellularization to determine age-dependent changes to collagen stiffness and AGE cross-linking. Total and soluble collagen was measured to assess if age-dependent increases in collagen and cross-linking persisted in decellularized muscle matrix (DMM). Stiffness of aged DMM was determined using atomic force microscopy. AGE levels and the effect of an AGE cross-link breaker, ALT-711, were tested in DMM samples. Our results show that age-dependent increases in collagen amount, cross-linking, and general stiffness were observed in DMM. Notably, we measured increased AGE-specific cross-links within old muscle, and observed that old DMM retained AGE cross-links using ALT-711 to reduce AGE levels. In conclusion, deleterious age-dependent modifications to collagen are present in DMM from old muscle, implying that age matters when sourcing skeletal muscle extracellular matrix as a biomaterial.

Collagen, cross-linking, and advanced glycation end products in aging human skeletal muscle

2007 ◽  
Vol 103 (6) ◽  
pp. 2068-2076 ◽  
Author(s):  
Jacob M. Haus ◽  
John A. Carrithers ◽  
Scott W. Trappe ◽  
Todd A. Trappe
Keyword(s):  
Skeletal Muscle ◽  
Advanced Glycation End Products ◽  
Protein Concentration ◽  
Muscle Force ◽  
Cross Linking ◽  
Force Transmission ◽  
Advanced Glycation ◽  
Glycation End Products ◽  
End Products ◽  
Collagen Cross Linking

We examined intramuscular endomysial collagen, cross-linking, and advanced glycation end products, as well as the general and contractile protein concentration of 20 young (25 ± 3 yr) and 22 old (78 ± 6 yr, range: 70–93 yr) sedentary men and women to better understand the underlying basis of changes in skeletal muscle mass and function that occur with aging. The old individuals had an impaired ability (increased time) ( P < 0.05) to climb stairs (80%), rise from a chair (56%), and walk (44%), as well as lower ( P < 0.05) quadriceps muscle volume (−29%), muscle strength (−35%), muscle power (−48%), and strength (−17%) and power (−33%) normalized to muscle size. Vastus lateralis muscle biopsies revealed that intramuscular endomysial collagen (young: 9.6 ± 1.1, old: 10.2 ± 1.2 μg/mg muscle wet wt) and collagen cross-linking (hydroxylysylpyridinoline) (young: 395 ± 65, old: 351 ± 45 mmol hydroxylysylpyridinoline/mol collagen) were unchanged ( P > 0.05) with aging. The advanced glycation end product, pentosidine, was increased ( P < 0.05) by ∼200% (young: 5.2 ± 1.3, old: 15.9 ± 4.5 mmol pentosidine/mol collagen) with aging. While myofibrillar protein concentration was lower (−5%, P < 0.05), the concentration of the main contractile proteins myosin and actin were unchanged ( P > 0.05) with aging. These data suggest that the synthesis and degradation of proteins responsible for the generation (myosin and actin) and transfer (collagen and pyridinoline cross-links) of muscle force are tightly regulated in aging muscle. Glycation-related cross-linking of intramuscular connective tissue may contribute to altered muscle force transmission and muscle function with healthy aging.

scholarly journals Accumulation of Advanced Glycation End-Products and Activation of the SCAP/SREBP Lipogenetic Pathway Occur in Diet-Induced Obese Mouse Skeletal Muscle

PLoS ONE ◽  
2015 ◽  
Vol 10 (3) ◽  
pp. e0119587 ◽  
Author(s):  
Raffaella Mastrocola ◽  
Massimo Collino ◽  
Debora Nigro ◽  
Fausto Chiazza ◽  
Giuseppe D’Antona ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Advanced Glycation End Products ◽  
Obese Mouse ◽  
Advanced Glycation ◽  
Mouse Skeletal Muscle ◽  
Glycation End Products ◽  
End Products

scholarly journals Role of advanced glycation end products in cellular signaling

Redox Biology ◽  
2014 ◽  
Vol 2 ◽  
pp. 411-429 ◽  
Author(s):  
Christiane Ott ◽  
Kathleen Jacobs ◽  
Elisa Haucke ◽  
Anne Navarrete Santos ◽  
Tilman Grune ◽  
...  
Keyword(s):  
Advanced Glycation End Products ◽  
Cellular Signaling ◽  
Advanced Glycation ◽  
Glycation End Products ◽  
End Products

The role of receptor for advanced glycation end products (RAGE) in neuronal differentiation

2012 ◽  
Vol 90 (6) ◽  
pp. 1136-1147 ◽  
Author(s):  
Joanne Kim ◽  
Carthur K. Wan ◽  
Simon J. O'Carroll ◽  
Shamim B. Shaikh ◽  
Louise F.B. Nicholson
Keyword(s):  
Neuronal Differentiation ◽  
Advanced Glycation End Products ◽  
Advanced Glycation ◽  
Glycation End Products ◽  
End Products
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