Effects of a soy protein diet on exercise-induced muscle protein catabolism in rats

Nikawa, Takeshi; Ikemoto, Madoka; Sakai, Takashi; Kano, Masashi; Kitano, Takako; Kawahara, Tsukasa; Teshima, Shigetada; Rokutan, Kazuhito; Kishi, Kazushi

doi:10.1016/s0899-9007(02)00744-x

Cited by 32 publications

(19 citation statements)

References 27 publications

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“…Calpastatin expression has the potential to regulate this process. Nikawa et al (2002) reported that, compared with a casein diet, a soy protein diet inhibited exercise-induced activation of calpains and the presence of myosin fragments in rat gastrocnemius. The soy protein diet also increased gastrocnemius calpastatin activity over the casein diet control group.…”

Section: Discussionmentioning

confidence: 99%

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Effect of dietary protein on calpastatin in canine skeletal muscle1

Helman

Huff-Lonergan

Davenport³

et al. 2003

Journal of Animal Science

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The cysteine proteinases, μ-and m-calpain, along with their inhibitor, calpastatin, have been hypothesized to play a role in skeletal muscle protein degradation. Because nutrition has previously been shown to influence the expression of calpastatin, the working hypothesis of this study was that the quantity and source of dietary protein could influence regulation of the calpain system in muscle. The objectives to support this hypothesis were to determine the effects of dietary protein (amount and source) on the expression of calpastatin in canine skeletal muscle. This study comprised eight diets with seven dogs per diet. A biopsy was taken from the biceps femoris of all 56 dogs before and after 10 wk on their respective diets. This experimental design allowed examination of change within individual dogs. Diets 1 to 4 contained 12% total protein derived from chicken and/or corn gluten meal in ratios of 100:0, 67:33, 33:67, and 0:100%, respectively. Diets 5 to 8 contained 28% total protein with protein sources and ratios identical to Diets 1 to 4. Differences in calpastatin were examined qualitatively using SDS-PAGE and immunoblotting, and semiquantitatively with densitometric analyses. The majority of the calpastatin blots showed three distinct calpastatin bands, the uppermost appearing at approximately 110 kDa. Diet 5 (28% CP, 100% chicken) resulted in an increase in the expression of the 110-kDa calpastatin band compared with the other two lower molecular weight bands in the same samples. Muscle from dogs fed Diet 5 showed greater increase in (P < 0.05) calpastatin intensity of the topmost band than those fed Diet 8 (0:100; chicken:corn gluten meal). Diet 5 (100:0; chicken:corn gluten meal) showed greater total calpastatin intensity than Diet 8 (0:100; chicken: corn gluten meal). These data suggest that dogs fed a diet containing a higher total percentage of chicken protein may have a greater potential to regulate calpain-mediated degradation of muscle protein than dogs fed diets containing corn gluten meal. ABSTRACT:The cysteine proteinases, -and m-calpain, along with their inhibitor, calpastatin, have been hypothesized to play a role in skeletal muscle protein degradation. Because nutrition has previously been shown to influence the expression of calpastatin, the working hypothesis of this study was that the quantity and source of dietary protein could influence regulation of the calpain system in muscle. The objectives to support this hypothesis were to determine the effects of dietary protein (amount and source) on the expression of calpastatin in canine skeletal muscle. This study comprised eight diets with seven dogs per diet. A biopsy was taken from the biceps femoris of all 56 dogs before and after 10 wk on their respective diets. This experimental design allowed examination of change within individual dogs. Diets 1 to 4 contained 12% total protein derived from chicken and/or corn gluten meal in ratios of 100:0, 67:33, 33:67, and 0:100%, respectively. Diets 5 to 8 contained 28% total protein wi...

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Section: Discussionmentioning

confidence: 99%

“…influenced by diet (van den Hemel-Grooten et al, 1997;Nikawa et al, 2002). Dietary protein content and quality are of critical importance in muscle growth and maintenance.…”

mentioning

confidence: 99%

Effect of dietary protein on calpastatin in canine skeletal muscle1

Helman

Huff-Lonergan

Davenport³

et al. 2003

Journal of Animal Science

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“…In addition, we demonstrated previously that diet containing soy protein prevents exercise-induced protein degradation in skeletal muscle, through the suppression of calpain-mediated proteolysis [7]. Thus, dietary soy protein affects protein turnover in skeletal muscle.…”

Section: Introductionmentioning

confidence: 95%

Soy Glycinin Contains a Functional Inhibitory Sequence against Muscle-Atrophy-Associated Ubiquitin Ligase Cbl-b

Abe

Kohno

Yama

et al. 2013

International Journal of Endocrinology

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Background. Unloading stress induces skeletal muscle atrophy. We have reported that Cbl-b ubiquitin ligase is a master regulator of unloading-associated muscle atrophy. The present study was designed to elucidate whether dietary soy glycinin protein prevents denervation-mediated muscle atrophy, based on the presence of inhibitory peptides against Cbl-b ubiquitin ligase in soy glycinin protein. Methods. Mice were fed either 20% casein diet, 20% soy protein isolate diet, 10% glycinin diet containing 10% casein, or 20% glycinin diet. One week later, the right sciatic nerve was cut. The wet weight, cross sectional area (CSA), IGF-1 signaling, and atrogene expression in hindlimb muscles were examined at 1, 3, 3.5, or 4 days after denervation. Results. 20% soy glycinin diet significantly prevented denervation-induced decreases in muscle wet weight and myofiber CSA. Furthermore, dietary soy protein inhibited denervation-induced ubiquitination and degradation of IRS-1 in tibialis anterior muscle. Dietary soy glycinin partially suppressed the denervation-mediated expression of atrogenes, such as MAFbx/atrogin-1 and MuRF-1, through the protection of IGF-1 signaling estimated by phosphorylation of Akt-1. Conclusions. Soy glycinin contains a functional inhibitory sequence against muscle-atrophy-associated ubiquitin ligase Cbl-b. Dietary soy glycinin protein significantly prevented muscle atrophy after denervation in mice.

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“…Soy-based diets can have an antihypertensive effect on spontaneously hypertensive rats (45). Male rats on a casein versus soy diet have been shown to exhibit less exercise-induced MyHC degradation in skeletal muscle (46). Diets containing phytoestrogen also appear to play a cardioprotective role in ischemiareperfusion injury in female rats (47).…”

Section: Phytoestrogens and Heart Diseasementioning

confidence: 99%

Sex is a potent modifier of the cardiovascular system

Leinwand¹

2003

J. Clin. Invest.

153

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Despite the growing number of reports in the literature identifying sex-related differences in cardiac function in both rodents and humans, the underlying mechanisms have yet to be determined. Here, variables of experimental studies such as diet, animal model utilized, and age, in addition to sex hormones and other factors that may play a role in sex-related variations in cardiac responses to various pathophysiological conditions are discussed, suggesting that current approaches used in the study of cardiac disease require reevaluation.There are numerous health problems that are affected by gender. Women are more susceptible than men to depression, osteoporosis, asthma, lung cancer due to smoking, and autoimmune disease (1). Gender effects in disease are complex, however, as exemplified by the observation that while the incidence of melanoma is slightly higher among women than men, mortality from melanoma is higher in men. Not all medical problems show gender dimorphism. For example, males do not differ from females in terms of their responses to infection (1). When it comes to heart disease, generally, of those individuals diagnosed with heart disease, women fare much better than men. Little is known about the basis for this difference in cardiovascular disease. Much focus has been placed on the potential cardioprotective role of estrogen. However, the recent finding that estrogen replacement in postmenopausal women actually increased heart disease has challenged this view (2).Deriving a coherent view of potential players in sexdependent differences in the heart requires analysis of both the clinical literature and the literature on sex-dependent differences in the cardiovascular system of laboratory animals. There is a major limiting factor in comparing rodent laboratory studies: the vast majority have been carried out on males only. However, this limitation appears to be changing. In the past year, a number of studies have appeared in which both males and females have been analyzed. An article in a recent issue of the JCI by O'Connell et al. (3) provided a glimpse into what promises to be a new way of thinking about genetic sex. In this report, the authors found that the α 1 -adrenergic receptors are critical in determining heart size and the ability of the heart to respond to both pathologic and physiologic stimuli, but only in male animals. Intriguingly, this sex-related difference did not disappear following ovariectomy of females. This article will discuss the fact that sex is an extremely potent modifier of the myocardium and will identify which pathways have been implicated in some of these differences. I hope it will become clear that future research should focus on the mechanisms by which both sex and diet can modify cardiovascular phenotypes.Sex-related differences in normal male and female hearts in human cardiac disease What are the sexually dimorphic cardiovascular differences to which I refer? Before puberty, there are no statistically significant sex-related differences in heart size (4). After ...

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Effects of a soy protein diet on exercise-induced muscle protein catabolism in rats

Cited by 32 publications

References 27 publications

Effect of dietary protein on calpastatin in canine skeletal muscle1

Effect of dietary protein on calpastatin in canine skeletal muscle1

Soy Glycinin Contains a Functional Inhibitory Sequence against Muscle-Atrophy-Associated Ubiquitin Ligase Cbl-b

Sex is a potent modifier of the cardiovascular system

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