Age and training alter collagen characteristics in fast- and slow-twitch rat limb muscle

Zimmerman, Scott; McCormick, Richard J.; Vadlamudi, Ratna K.; Thomas, D. P.

doi:10.1152/jappl.1993.75.4.1670

Cited by 85 publications

(94 citation statements)

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“…In rats, there is an increase in total collagen concentration in muscles with age (9,16,29). However, in our study we saw no increase in total protein or total collagen concentration per muscle wet weight in healthy elderly muscle.…”

Section: Effect Of Age On Skeletal Muscle Collagen Synthesis and Conccontrasting

confidence: 81%

“…In rat muscle, an increase in cross-linking with age has been reported (17,29), and this increase has been correlated with decreased viscoelastic and plastic properties of the whole muscle (17). We also found a reduced ratio of proline to hydroxyproline in the elderly muscle insoluble collagen, which may be indicative of increased synthesis of type III collagen or type I collagen homotrimers (14) with a decrease in type I collagen heterotrimers.…”

Section: Effect Of Age On Skeletal Muscle Collagen Synthesis and Concmentioning

confidence: 97%

“…It has been demonstrated that the concentration of collagen in skeletal muscle increases (16,29) in aging rats, whereas in tendon and ligament there is a decrease (13). In the collagen found in tendon, ligament, and skeletal muscle, there is an increase in the nonreducible collagen cross-linking with aging, possibly resulting in stiffer, less compliant tissues (17,23,13).…”

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confidence: 99%

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Collagen synthesis in human musculoskeletal tissues and skin

Babraj¹,

Cuthbertson²,

Smith³

et al. 2005

American Journal of Physiology-Endocrinology and Metabolism

133

131

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We have developed a direct method for the measurement of human musculoskeletal collagen synthesis on the basis of the incorporation of stable isotope-labeled proline or leucine into protein and have used it to measure the rate of synthesis of collagen in tendon, ligament, muscle, and skin. In postabsorptive, healthy young men (28 Ϯ 6 yr) synthetic rates for tendon, ligament, muscle, and skin collagen were 0.046 Ϯ 0.005, 0.040 Ϯ 0.006, 0.016 Ϯ 0.002, and 0.037 Ϯ 0.003%/h, respectively (means Ϯ SD). In postabsorptive, healthy elderly men (70 Ϯ 6 yr) the rate of skeletal muscle collagen synthesis is greater than in the young (0.023 Ϯ 0.002%/h, P Ͻ 0.05 vs. young). The rates of synthesis of tendon and ligament collagen are similar to those of mixed skeletal muscle protein in the postabsorptive state, whereas the rate for muscle collagen synthesis is much lower in both young and elderly men. After nutritient provision, collagen synthesis was unaltered in tendon and skeletal muscle, remaining at postabsorptive values (young: tendon, 0.045 Ϯ 0.008%/h; muscle, 0.016 Ϯ 0.003%/h; elderly: muscle, 0.024 Ϯ 0.003%/h). These results demonstrate that the rate of human musculoskeletal tissue collagen synthesis can be directly and robustly measured using stable isotope methodology. stable-isotope tracers; musculoskeletal collagen synthesis; nutrition; aging THE EXTRACELLULAR MATRIX of skeletal muscle, tendon, ligament, and bone is important for maintaining tissue structure and vital for transmission of force during muscular contraction (15). Collagen is the major protein in the extracellular matrix of the musculoskeletal tissue, but despite its importance to tissue function, knowledge of the physiological regulation of the amount and turnover of collagen in human beings is poor, partly due to the absence of direct methods for determination of collagen turnover in vivo under different conditions. The overall contribution of collagen to whole body protein turnover is unknown, despite the fact that collagen probably contributes 3.5 kg to the lean body mass compared with 12 kg for muscle myocellular protein, about which much more is known (22).It has been demonstrated that the concentration of collagen in skeletal muscle increases (16, 29) in aging rats, whereas in tendon and ligament there is a decrease (13). In the collagen found in tendon, ligament, and skeletal muscle, there is an increase in the nonreducible collagen cross-linking with aging, possibly resulting in stiffer, less compliant tissues (17, 23, 13). Direct measurements of collagen synthesis in rats (6 and 15 mo old), using a flooding dose of radioactive [14 C]proline (19), have shown increased turnover, including both a greater collagen fractional synthetic rate and an increased degradation rate of newly synthesized collagen, with maturity. It might be expected that a similar temporal change might exist in human beings. Unfortunately, little is known about human musculoskeletal collagen metabolism and aging in vivo.Feeding of protein or amino acids is a major, dose-de...

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Section: Effect Of Age On Skeletal Muscle Collagen Synthesis and Conccontrasting

confidence: 81%

Section: Effect Of Age On Skeletal Muscle Collagen Synthesis and Concmentioning

confidence: 97%

mentioning

confidence: 99%

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Collagen synthesis in human musculoskeletal tissues and skin

Babraj¹,

Cuthbertson²,

Smith³

et al. 2005

American Journal of Physiology-Endocrinology and Metabolism

133

131

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“…We report here, TIMP-2 in Neuromuscular Junction Developmentfor the first time to our knowledge, an age-related increase in MMP activity that is greatest for fast-twitch muscle. Because fast-twitch fibers contain less collagen than slow-twitch fibers (Zimmerman et al, 1993), fasttwitch fibers are even more susceptible to the damaging effects of increased MMP activity. Many cell types contribute to the MMPs present in muscle, including motor neurons (Platt et al, 2003), Schwann cells (Muir and Manthorpe, 1992), myocytes (Demestre et al, 2005), satellite cells (Guerin and Holland, 1995), and fibroblasts (Ogawa et al, 2005).…”

Section: Mmp-mediated Proteolysis As the Foundation For The Timp-2mentioning

confidence: 99%

Tissue inhibitor of metalloproteinase‐2 (TIMP‐2) regulates neuromuscular junction development via a β1 integrin‐mediated mechanism

et al. 2006

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Extracellular matrix (ECM) molecules play critical roles in muscle function by participating in neuromuscular junction (NMJ) development and the establishment of stable, cytoskeleton-associated adhesions required for muscle contraction. Matrix metalloproteinases (MMPs) are neutral endopeptidases that degrade all ECM components. While the role of MMPs and their inhibitors, the tissue inhibitor of metalloproteinases (TIMPs), has been investigated in many tissues, little is known about their role in muscle development and mature function. TIMP-2 -/- mice display signs of muscle weakness. Here, we report that TIMP-2 is expressed at the NMJ and its expression is greater in fast-twitch (extensor digitorum longus, EDL) than slow-twitch (soleus) muscle. EDL muscle mass is reduced in TIMP-2-/- mice without a concomitant change in fiber diameter or number. The TIMP-2-/- phenotype is not likely due to increased ECM proteolysis because net MMP activity is actually reduced in TIMP-2-/- muscle. Most strikingly, TIMP-2 colocalizes with beta1 integrin at costameres in the wild-type EDL and beta1 integrin expression is significantly reduced in TIMP-2-/- EDL. We propose that reduced beta1 integrin in fast-twitch muscle may be associated with destabilized ECM-cytoskeletal interactions required for muscle contraction in TIMP-2-/- muscle; thus, explaining the muscle weakness. Given that fast-twitch fibers are lost in muscular dystrophies and age-related sarcopenia, if TIMP-2 regulates mechanotransduction in an MMP-independent manner it opens new potential therapeutic avenues.

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“…Morphologically, slow muscles are abundant in extracellular collagenous matrices (Zimmerman et al 1993), capillary vessels, myoglobin, and mitochondria (Campbell et al 2001). Their sarcomeres show wider Z-disks and diffuse M-lines on electron micrographs (Sjöström et al 1982;Agarkova et al 2004).…”

Section: Two Types Of Muscle-related Force Energy and Adaptabilitymentioning

confidence: 99%

Gravitational Effects on Human Physiology

Atomi

2015

Subcellular Biochemistry

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Physical working capacity decreases with age and also in microgravity. Regardless of age, increased physical activity can always improve the physical adaptability of the body, although the mechanisms of this adaptability are unknown. Physical exercise produces various mechanical stimuli in the body, and these stimuli may be essential for cell survival in organisms. The cytoskeleton plays an important role in maintaining cell shape and tension development, and in various molecular and/or cellular organelles involved in cellular trafficking. Both intra and extracellular stimuli send signals through the cytoskeleton to the nucleus and modulate gene expression via an intrinsic property, namely the "dynamic instability" of cytoskeletal proteins. αB-crystallin is an important chaperone for cytoskeletal proteins in muscle cells. Decreases in the levels of αB-crystallin are specifically associated with a marked decrease in muscle mass (atrophy) in a rat hindlimb suspension model that mimics muscle and bone atrophy that occurs in space and increases with passive stretch. Moreover, immunofluorescence data show complete co-localization of αB-crystallin and the tubulin/microtubule system in myoblast cells. This association was further confirmed in biochemical experiments carried out in vitro showing that αB-crystallin acts as a chaperone for heat-denatured tubulin and prevents microtubule disassembly induced by calcium. Physical activity induces the constitutive expression of αB-crystallin, which helps to maintain the homeostasis of cytoskeleton dynamics in response to gravitational forces. This relationship between chaperone expression levels and regulation of cytoskeletal dynamics observed in slow anti-gravitational muscles as well as in mammalian striated muscles, such as those in the heart, diaphragm and tongue, may have been especially essential for human evolution in particular. Elucidation of the intrinsic properties of the tubulin/microtubule and chaperone αB-crystallin protein complex systems is expected to provide valuable information for high-pressure bioscience and gravity health science.

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Age and training alter collagen characteristics in fast- and slow-twitch rat limb muscle

Cited by 85 publications

References 0 publications

Collagen synthesis in human musculoskeletal tissues and skin

Collagen synthesis in human musculoskeletal tissues and skin

Tissue inhibitor of metalloproteinase‐2 (TIMP‐2) regulates neuromuscular junction development via a β1 integrin‐mediated mechanism

Gravitational Effects on Human Physiology

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