COLLAGEN AND NON–COLLAGEN PROTEIN TURNOVER IN SKELETAL MUSCLE OF GROWTH HORMONE–TREATED LAMBS
Authors:
- P. C. BatesPBP. C. Bates
- 1 October 1987
- journal article
- research article
- Published by Bioscientifica in Journal of Endocrinology
- Vol. 115 (1) , R1-R4
Abstract
Long–term administration of GH to normal, well–fed lambs caused a significant increase in net muscle growth. This could be accounted for by increased rates of muscle protein synthesis, although red and white muscles responded differently. The increased rate of protein synthesis was due to an increased protein synthetic capacity (increased muscle RNA content) but efficiency per unit of RNA also tended to increase in red muscle. For similar increases in net growth, protein turnover was increased to a much greater extent in red than in white muscle. The ratio of collagen to non–collagen protein was unaffected in both muscle types by GH treatment, even though collagen synthesis rates were significantly increased in red muscle. To date, GH is the only anabolic agent in ruminants which acts via increased rates of protein synthesis rather than by decreased rates of protein degradation.Keywords
This publication has 10 references indexed in Scilit:
- Muscle growth and distribution of muscle weight in Clun and Southdown sheepAnimal Science, 1987
- The effect of the β-2-adrenergic agonist clenbuterol or implantation with oestradiol plus trenbolone acetate on protein metabolism in wether lambsBritish Journal of Nutrition, 1987
- Inhibition and reversal of denervation-induced atrophy by the β-agonist growth promoter, clenbuterolBioscience Reports, 1986
- The effects of exogenous bovine growth hormone and bromocriptine on growth, body development, fleece weight and plasma concentrations of growth hormone, insulin and prolactin in female lambsAnimal Science, 1985
- Changes in collagen synthesis and degradation during skeletal muscle growthAmerican Journal of Physiology-Cell Physiology, 1985
- Protein synthesis in skeletal muscle of the perfused rat hemicorpus compared with rates in the intact animalBiochemical Journal, 1983
- Rapid Modulation of Protein Synthesis in Normal Rats by Specific Neutralization and Replacement of Growth Hormone*Endocrinology, 1982
- Rates of collagen synthesis in lung, skin and muscle obtained in vivo by a simplified method using [3H]prolineBiochemical Journal, 1982
- Anomalous tritium loss in the measurement of tissue hydroxy-[5-3H]proline specific activity following chloramine-T oxidationAnalytical Biochemistry, 1982
- Analysis of Early Responses to Growth Hormone on Amino Acid Transport and Protein Synthesis in Diaphragms of Young Normal Rats*Endocrinology, 1980