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  • Cereal and nonfat milk support muscle recovery following exercise. 19442266

    ABSTRACT: BACKGROUND: This study compared the effects of ingesting cereal and nonfat milk (Cereal) and a carbohydrate-electrolyte sports drink (Drink) immediately following endurance exercise on muscle glycogen synthesis and the phosphorylation state of proteins controlling protein synthesis: Akt, mTOR, rpS6 and eIF4E. METHODS: Trained cyclists or triathletes (8 male: 28.0 +/- 1.6 yrs, 1.8 +/- 0.0 m, 75.4 +/- 3.2 kg, 61.0 +/- 1.6 ml O2*kg-1*min-1; 4 female: 25.3 +/- 1.7 yrs, 1.7 +/- 0.0 m, 66.9 +/- 4.6 kg, 46.4 +/- 1.2 mlO2*kg-1*min-1) completed two randomly-ordered trials serving as their own controls. After 2 hours of cycling at 60-65% VO2MAX, a biopsy from the vastus lateralis was obtained (Post0), then subjects consumed either Drink (78.5 g carbohydrate) or Cereal (77 g carbohydrate, 19.5 g protein and 2.7 g fat). Blood was drawn before and at the end of exercise, and at 15, 30 and 60 minutes after treatment. A second biopsy was taken 60 minutes after supplementation (Post60). Differences within and between treatments were tested using repeated measures ANOVA. RESULTS: At Post60, blood glucose was similar between treatments (Drink 6.1 +/- 0.3, Cereal 5.6 +/- 0.2 mmol/L, p .05), but after Cereal, plasma insulin was significantly higher (Drink 123.1 +/- 11.8, Cereal 191.0 +/- 12.3 pmol/L, p .05), and plasma lactate significantly lower (Drink 1.4 +/- 0.1, Cereal 1.00 +/- 0.1 mmol/L, p .05). Except for higher phosphorylation of mTOR after Cereal, glycogen and muscle proteins were not statistically different between treatments. Significant Post0 to Post60 changes occurred in glycogen (Drink 52.4 +/- 7.0 to 58.6 +/- 6.9, Cereal 58.7 +/- 9.6 to 66.0 +/- 10.0 mumol/g, p .05) and rpS6 (Drink 17.9 +/- 2.5 to 35.2 +/- 4.9, Cereal 18.6 +/- 2.2 to 35.4 +/- 4.4 %Std, p .05) for each treatment, but only Cereal significantly affected glycogen synthase (Drink 66.6 +/- 6.9 to 64.9 +/- 6.9, Cereal 61.1 +/- 8.0 to 54.2 +/- 7.2%Std, p .05), Akt (Drink 57.9 +/- 3.2 to 55.7 +/- 3.1, Cereal 53.2 +/- 4.1 to 60.5 +/- 3.7 %Std, p .05) and mTOR (Drink 28.7 +/- 4.4 to 35.4 +/- 4.5, Cereal 23.0 +/- 3.1 to 42.2 +/- 2.5 %Std, p .05). eIF4E was unchanged after both treatments. CONCLUSION: These results suggest that Cereal is as good as a commercially-available sports drink in initiating post-exercise muscle recovery.
    Tipo de documento:
    Referencia
    Referencia del producto:
    05-736
    Nombre del producto:
    Anti-phospho-Akt1/PKBα (Ser473) Antibody, clone SK703, rabbit monoclonal

  • SV40-transformed human lung fibroblasts secrete a 92-kDa type IV collagenase which is identical to that secreted by normal human macrophages. 2551898

    We have reported that SV40-transformed human lung fibroblasts secrete a 92-kDa metalloprotease which is not detectable in the parental cell line IMR-90. We now present the complete structure of this enzyme along with the evidence that it is identical to the 92-kDa metalloprotease secreted by normal human alveolar macrophages, phorbol ester-differentiated monocytic leukemia U937 cells, fibrosarcoma HT1080 cells, and cultured human keratinocytes. A similar, perhaps identical, enzyme can be released by polymorphonuclear cells. The preproenzyme is synthesized as a polypeptide of predicted Mr 78,426 containing a 19 amino-acid-long signal peptide and secreted as a single 92,000 glycosylated proenzyme. The purified proenzyme complexes noncovalently with the tissue inhibitor of metalloproteases (TIMP) and can be activated by organomercurials. Activation with phenylmercuric chloride results in removal of 73 amino acids from the NH2 terminus of the proenzyme, yielding an active form capable of digesting native types IV and V collagen. The in vitro substrate specificity of the enzyme using these substrates was indistinguishable from that of the 72-kDa type IV collagenase. The 92-kDa type IV collagenase consists of five domains; the amino-terminal and zinc-binding domains shared by all members of the secreted metalloprotease gene family, the collagen-binding fibronectin-like domain also present in the 72-kDa type IV collagenase, a carboxyl-terminal hemopexin-like domain shared by all known enzymes of this family with the exception of PUMP-1, and a unique 54-amino-acid-long proline-rich domain homologous to the alpha 2 chain of type V collagen.
    Tipo de documento:
    Referencia
    Referencia del producto:
    CC1048
    Nombre del producto:
    MMP-9, human, proform
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