Advanced glycation end products in musculoskeletal system and disorders

Suzuki, Akinobu; Yabu, Akito; Nakamura, Hiroaki

doi:10.1016/j.ymeth.2020.09.012

Cited by 48 publications

(44 citation statements)

References 96 publications

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“…Muscular aging is multifactorial, involving extrinsic and intrinsic mechanisms that attack both the cellular components and extracellular matrix (ECM). Advanced glycation end-products (AGEs), the final derivative of the Maillard or browning reaction, are known to accumulate in musculoskeletal tissues in old age and are thought to play a role in the development of sarcopenia [ 9 , 10 , 11 , 12 ]. AGEs preferentially accrue on the long-lived extracellular matrix (ECM) proteins, especially collagens, since their formation relies on its precursors’ stochastic reaction (glucose and proteins) via the Maillard reaction.…”

Section: Introductionmentioning

confidence: 99%

Advanced Glycation End-Products in Skeletal Muscle Aging

et al. 2021

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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.

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Section: Introductionmentioning

confidence: 99%

Advanced Glycation End-Products in Skeletal Muscle Aging

et al. 2021

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“…However, no distinct differences in RAGE distributions were found at the tendon‐to‐bone interfaces among the four age groups in our study. IHC can only evaluate the distribution and accumulation of AGE at the two‐dimensional level without precisely quantitative measurement 46 . The immunological detection method also has the problem of non‐specific binding of the antibody 47 .…”

Section: Discussionmentioning

confidence: 99%

“…IHC can only evaluate the distribution and accumulation of AGE at the two-dimensional level without precisely quantitative measurement. 46 The immunological detection method also has the problem of non-specific binding of the antibody. 47 Thus, other high-accuracy quantitative studies of AGE are needed.…”

Section: Discussionmentioning

confidence: 99%

The effects of maturation and aging on the rotator cuff tendon‐to‐bone interface

et al. 2021

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Rotator cuff tendon injuries often occur at the tendon‐to‐bone interface (i.e., enthesis) area, with a high prevalence for the elderly population, but the underlying reason for this phenomenon is still unknown. The objective of this study is to identify the histological, molecular, and biomechanical alterations of the rotator cuff enthesis with maturation and aging in a mouse model. Four different age groups of mice (newborn, young, adult, and old) were studied. Striking variations of the entheses were observed between the newborn and other matured groups, with collagen content, proteoglycan deposition, collagen fiber dispersion was significantly higher in the newborn group. The compositional and histological features of young, adult, and old groups did not show significant differences, except having increased proteoglycan deposition and thinner collagen fibers at the insertion sites in the old group. Nanoindentation testing showed that the old group had a smaller compressive modulus at the insertion site when compared with other groups. However, tensile mechanical testing reported that the old group demonstrated a significantly higher failure stress when compared with the young and adult groups. The proteomics analysis detected dramatic differences in protein content between newborn and young groups but minor changes among young, adult, and old groups. These results demonstrated: (1) the significant alterations of the enthesis composition and structure occur from the newborn to the young time period; (2) the increased risk of rotator cuff tendon injuries in the elderly population is not solely because of old age alone in the rodent model.

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“…In support of our hypothesis, we observed a significant increase in collagen at 20 months in DMM, indicating that additional age-related cross-links attenuated normal collagen turnover. Skeletal muscle collagen is heavily cross-linked by glycation in aged muscles, stiffening the matrix and causing it to be resistant to enzymatic turn-over [10,19,20]. Furthermore, no considerable differences in enzymatic cross-linking have been observed with age [47,89].…”

Section: Discussionmentioning

confidence: 99%

“…The deterioration of muscle's strength and mass with increasing age culminates in a condition known as sarcopenia, an age-dependent muscle wasting disease [2][3][4][5][6][7]. Advanced glycation end products (AGEs), the final derivative of the Maillard or browning reaction, are known to accumulate in musculoskeletal tissues in old age and are thought to play a role in the development of sarcopenia [8][9][10]. AGEs preferentially accrue on the long-lived extracellular matrix (ECM) proteins, especially collagens, since their formation relies on its precursors' stochastic reaction (glucose and proteins) via the Maillard reaction.…”

Section: Introductionmentioning

confidence: 99%

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

Olson

Nguyen

Heise

et al. 2021

IJMS

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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.

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Advanced glycation end products in musculoskeletal system and disorders

Cited by 48 publications

References 96 publications

Advanced Glycation End-Products in Skeletal Muscle Aging

Advanced Glycation End-Products in Skeletal Muscle Aging

The effects of maturation and aging on the rotator cuff tendon‐to‐bone interface

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

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