The extent and nature of protein degradation in the tissues during development

Millward, D. J.; Bates, P. C.; Rosochacki, Stanislav

doi:10.1051/rnd:19810210

Cited by 25 publications

(15 citation statements)

References 24 publications

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“…d-1 (Pencharz, Farri & Papageorgiou, 1983), which is twice as high as in the1 year old child and 3-4 times as high as in the adult. With increasing maturity, the fall in intensity of whole body protein turnover is greater than can be accounted for simply by the increase in body size (Millward, Bates & Rosochaki, 1981 a).…”

Section: Protein Turnover Body Size and Maturitymentioning

confidence: 99%

Protein Turnover With Special Reference to Man

1984

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This review is concerned with rates of N flux in the living animal rather than with mechanisms of protein synthesis and breakdown at the cellular level. Methods of measuring protein turnover in the whole body are discussed, with special emphasis on studies in man, and results obtained by different methods have been compared. Aspects of whole body protein turnover which are of physiological interest include its relation to body size, growth and development, energy metabolism and food intake. There are substantial increases in protein turnover in injury, and changes that occur in exercise are beginning to be explored. From the physiological point of view these results point the need for future research along two main lines. The first is that of regulation: a wide variety of hormones stimulate or repress protein synthesis and breakdown, with varying actions in different tissues. These effects, however, do not in themselves explain the mechanism by which a balance between synthesis and breakdown is maintained. Secondly, the fact that all cellular proteins are in a dynamic state poses questions about the relation between structure and function in tissues such as muscle and brain, which physiologists have hardly begun to tackle.

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Section: Protein Turnover Body Size and Maturitymentioning

confidence: 99%

Protein Turnover With Special Reference to Man

1984

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“…While rates of protein synthesis are readily measurable by time‐course experiments utilising radioisotopes and protein quantification, the rate of degradation ( k deg ) is often more difficult to determine especially in vivo (Millward et al. ; Pratt et al. ).…”

Section: Introductionmentioning

confidence: 99%

Incompatibility of chemical protein synthesis inhibitors with accurate measurement of extended protein degradation rates

Chan

Martin

Liptrott

et al. 2017

Pharmacology Res & Perspec

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Protein synthesis inhibitors are commonly used for measuring protein degradation rates, but may cause cytotoxicity via direct or indirect mechanisms. This study aimed to identify concentrations providing optimal inhibition in the absence of overt cytotoxicity. Actinomycin D, cycloheximide, emetine, and puromycin were assessed individually, and in two‐, three‐, and four‐drug combinations for protein synthesis inhibition (IC 50) and cytotoxicity (CC 50) over 72 h. Experiments were conducted in HepG2 cells and primary rat hepatocytes (PRH). IC 50 for actinomycin D, cycloheximide, emetine, and puromycin were 39 ± 7.4, 6600 ± 2500, 2200 ± 1400, and 1600 ± 1200 nmol/L; with corresponding CC 50 values of 6.2 ± 7.3, 570 ± 510, 81 ± 9, and 1300 ± 64 nmol/L, respectively, in HepG2 cells. The IC 50 were 1.7 ± 1.8, 290 ± 90, 620 ± 920, and 2000 ± 2000 nmol/L, with corresponding CC 50 values of 0.98 ± 1.8, 680 ± 1300, 180 ± 700, and 1600 ± 1000 (SD) nmol/L, respectively, in PRH. CC 50 were also lower than the IC 50 for all drug combinations in HepG2 cells. These data indicate that using pharmacological interference is inappropriate for measuring protein degradation over a protracted period, because inhibitory effects cannot be extricated from cytotoxicity.

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“…Animal growth rate is one of the most important and can be modulated by nutrition, eg. food restriction during a certain period followed by re-feeding provoking compensating growth (MILLWARD et al, 1980(MILLWARD et al, , 1981 or breeding and environment (FIEDLER et al, 1998). In this experiment, the selection for low and high body weight over 108 generation was done being the only factor that influenced the growth of animals (WIRTH-DZIĘCIOŁOWSKA et al, 1997.…”

Section: +mentioning

confidence: 99%

“…ATP-ubiquitin (Ub)-dependent pathway is responsible for the degradation of short-lived and abnormal proteins and myofibrils disassembling (THOMPSON and PALMER, 1998). There is a lot of evidence, that rate of protein degradation varies in the same way as activity of cathepsin D in various rat (MILLWARD et al, 1981) and chicken muscle (LAURENT et al, 1978;ROSOCHACKI, 1985). GOLDSPINK and LEWIS (1985) demonstrated that cathepsin B could be the rate of protein degradation indicator.…”

Section: Introductionmentioning

confidence: 99%

“…These changes in the kinetics on both sides of the equilibrium will result in an increased or a decreased muscle' growth, thus changing the final muscle weight gain (SHMIDT et al, 2000) which is strongly connected with the remodeling of the fibrils. There are some evidences concerning remarkable sensitivity of the overall rate of protein degradation in muscle and liver to nutritional factors (MILLWARD et al, 1980(MILLWARD et al, , 1981. In some physiological and mainly pathological states muscle growth is determined solely at the catabolic side (eg.…”

Section: Introductionmentioning

confidence: 99%

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Skeletal muscle and liver protein degradation in mice divergently selected for low and high body weight over 108 generations

Rosochacki

Wirth-Dzieciolowska

Zimowska³

et al. 2005

Arch. Anim. Breed.

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Experiment was carried out on 111 and 13-14 weeks old mice divergently selected for low (L) and high (C) body weight over 108 generations. In leg muscle and liver cathepsin D (CatD) was determined as pepstatin sensitive activity (PSCatD), and as pepstatin-insensitive (PIA) and leupeptin-insensitive (LIA) acid autolytic activities (AAA) were measured. In leg muscle and liver all measured activities were higher in L as compared to C and control (K) mice. The percent of inhibition of LIA was lower in L then C mice in both examined tissues. In the leg muscles, in L mice protein catabolism was mostly influenced by CatD, but in the liver CatD was mostly active in K mice. CatD, PSCatD, AAA and LIA in leg muscle of L mice as compare to K were higher in female (F) by 68 %, 68.5 %, 91.3 % and 94.5 %, respectively, and in male (M) mice by 43.4 %, 54 %, 47.1 % and 64 %, respectively. The percent of inhibition by leupeptin in AAA was higher in C mice by 61.9 % in F and by 40 % in M mice. In the liver, PIA was higher by about 45 % in L and by 28.5 % in C mice as compare to K ones. There were about 36% of 30.00-39.99 µm muscle fibrils in M mice and in males of L group 40.00-49.99 µm fibrils appeared at 25% (absent in 3 weeks mice). In female, all measured fibril diameters were in higher percent in L than in C group. RNA variables were higher by about 25% (in average) in C as compare to K and L groups. Functional cell size (FCS) was lowered in L and C group as compared to K by about 10 % (in average). These results indicate on faster proteins turnover in L than in C group of mice. Key Words: mice; long term selection, body weight, proteolytic enzyme activity, muscle DNA-RNA, liver DNA-RNA, fibre size Die prozentuale Hemmung der LIA-Werte war in beiden Geweben in der L-Gruppe niedriger als in der C-Gruppe. Im Schenkelmuskel der L-Mäuse wurde der Proteinkatabolismus überwiegend durch die CatD beeinflusst. In der Leber war die CatD aktiver in der K-Gruppe. Die Aktivität von CatD, PSCatD, AAA und LIA war im Schenkelmuskel der L-Mäuse höher als bei den K-Mäusen. Bei den weiblichen Tieren der L-Gruppe waren die entsprechenden Messwerte um 68,0%, 68,5%, 91,3% bzw. 94,5% höher als bei der Kontrollgruppe. Bei den männlichen Tieren der gleichen Gruppe erhöhten sich die analogen Werte jedoch nur um 43,3%, 54,0%, 47,1%, bzw. 64,0%. Die prozentuale Hemmung der LIA bezüglich der AAA war in der C-Gruppe höher (Weibchen 61,9%; Männchen 40,0%). In der Leber war die Aktivität der PIA bei der L-Gruppe um 45,0% und bei der C-Gruppe um 28,5% höher als bei der Kontrollgruppe. Im Alter von drei Monaten fanden sich in der K-Gruppe bei den männlichen Mäusen 36,0% mehr Fibrillen in der Muskelfaser mit einem Durchmesser von 30,00-39,99 µm, bei der L-Gruppe nur * Supported by Projects No PBZ-KBN-036/P06/07, S.V.9 and S/IIŚ/26/01 ROSOCHACKI et al.: Skeletal muscle and liver protein degradation in mice divergently selected for low and high body weight 506 25,0% mehr Fasern mit einem Durchmesser von 40,00-49,99 µm, die bei den Mäusen im Alter von dre...

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The extent and nature of protein degradation in the tissues during development

Abstract: Summary. Protein Introduction.

Cited by 25 publications

References 24 publications

Protein Turnover With Special Reference to Man

Protein Turnover With Special Reference to Man

Incompatibility of chemical protein synthesis inhibitors with accurate measurement of extended protein degradation rates

Skeletal muscle and liver protein degradation in mice divergently selected for low and high body weight over 108 generations

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