TPT
05-24-2010, 08:44 PM
the following study suggests that growth hormone does not affect muscle protein synthesis, but does affect tendon and collagen synthesis.
http://jp.physoc.org/content/588/2/341.short
these data and others might further direct bodybuilders to avoid gh as an effective drug for muscle hypertrophy and towards using gh for injuries or tendon healing.
Growth hormone stimulates the collagen synthesis in human tendon and skeletal muscle without affecting myofibrillar protein synthesis
<LI id=contrib-1>Simon Doessing (http://jp.physoc.org/search?author1=Simon+Doessing&sortspec=date&submit=Submit)1 (http://jp.physoc.org/content/588/2/341.short#target-1), <LI id=contrib-2>Katja M. Heinemeier (http://jp.physoc.org/search?author1=Katja+M.+Heinemeier&sortspec=date&submit=Submit)1 (http://jp.physoc.org/content/588/2/341.short#target-1), <LI id=contrib-3>Lars Holm (http://jp.physoc.org/search?author1=Lars+Holm&sortspec=date&submit=Submit)1 (http://jp.physoc.org/content/588/2/341.short#target-1), <LI id=contrib-4>Abigail L. Mackey (http://jp.physoc.org/search?author1=Abigail+L.+Mackey&sortspec=date&submit=Submit)1 (http://jp.physoc.org/content/588/2/341.short#target-1), <LI id=contrib-5>Peter Schjerling (http://jp.physoc.org/search?author1=Peter+Schjerling&sortspec=date&submit=Submit)1 (http://jp.physoc.org/content/588/2/341.short#target-1), <LI id=contrib-6>Michael Rennie (http://jp.physoc.org/search?author1=Michael+Rennie&sortspec=date&submit=Submit)3 (http://jp.physoc.org/content/588/2/341.short#target-3), <LI id=contrib-7>Kenneth Smith (http://jp.physoc.org/search?author1=Kenneth+Smith&sortspec=date&submit=Submit)3 (http://jp.physoc.org/content/588/2/341.short#target-3), <LI id=contrib-8>Søren Reitelseder (http://jp.physoc.org/search?author1=S%C3%B8ren+Reitelseder&sortspec=date&submit=Submit)1 (http://jp.physoc.org/content/588/2/341.short#target-1), <LI id=contrib-9>Anne-Marie Kappelgaard (http://jp.physoc.org/search?author1=Anne-Marie+Kappelgaard&sortspec=date&submit=Submit)4 (http://jp.physoc.org/content/588/2/341.short#target-4), <LI id=contrib-10>Michael Højby Rasmussen (http://jp.physoc.org/search?author1=Michael+H%C3%B8jby+Rasmussen&sortspec=date&submit=Submit)4 (http://jp.physoc.org/content/588/2/341.short#target-4), <LI id=contrib-11>Allan Flyvbjerg (http://jp.physoc.org/search?author1=Allan+Flyvbjerg&sortspec=date&submit=Submit)5 (http://jp.physoc.org/content/588/2/341.short#target-5) and
Michael Kjaer (http://jp.physoc.org/search?author1=Michael+Kjaer&sortspec=date&submit=Submit)1 (http://jp.physoc.org/content/588/2/341.short#target-1)
+ (http://jp.physoc.org/content/588/2/341.short#) Author Affiliations
1Institute of Sports Medicine, Bispebjerg Hospital, Center of Healthy Aging, Faculty of Health Sciences, University of Copenhagen, Bispebjerg Bakke 23, DK-2400 Copenhagen NV, Denmark2Department of Endocrinology, Copenhagen University Hospital Rigshospitalet, Blegdamsvej 9, DK-2100 Copenhagen Ø, Denmark3School of Biomedical Sciences, University of Nottingham Medical School, Derby City General Hospital, Derby DE22 3DT, UK4Medical & Science, Global Development, Novo Nordisk, DK-2880 Bagsvaerd, Denmark5The Medical Research Laboratories, Clinical Institute and Medical Department M (Diabetes and Endocrinology), Aarhus University Hospital, Aarhus C, Denmark
Corresponding author
S. Doessing: Institute of Sports Medicine, Bispebjerg Hospital, Center of Healthy Aging, Faculty of Health Sciences, University of Copenhagen, Bispebjerg Bakke 23, DK-2400 Copenhagen NV, Denmark. Email: [email protected] ([email protected])
Abstract
In skeletal muscle and tendon the extracellular matrix confers important tensile properties and is crucially important for tissue regeneration after injury. Musculoskeletal tissue adaptation is influenced by mechanical loading, which modulates the availability of growth factors, including growth hormone (GH) and insulin-like growth factor-I (IGF-I), which may be of key importance. To test the hypothesis that GH promotes matrix collagen synthesis in musculotendinous tissue, we investigated the effects of 14 day administration of 33–50 μg kg−1 day−1 recombinant human GH (rhGH) in healthy young individuals. rhGH administration caused an increase in serum GH, serum IGF-I, and IGF-I mRNA expression in tendon and muscle. Tendon collagen I mRNA expression and tendon collagen protein synthesis increased by 3.9-fold and 1.3-fold, respectively (P < 0.01 and P = 0.02), and muscle collagen I mRNA expression and muscle collagen protein synthesis increased by 2.3-fold and 5.8-fold, respectively (P < 0.01 and P = 0.06). Myofibrillar protein synthesis was unaffected by elevation of GH and IGF-I. Moderate exercise did not enhance the effects of GH manipulation. Thus, increased GH availability stimulates matrix collagen synthesis in skeletal muscle and tendon, but without any effect upon myofibrillar protein synthesis. The results suggest that GH is more important in strengthening the matrix tissue than for muscle cell hypertrophy in adult human musculotendinous tissue.
Footnotes
(Received 25 July 2009; accepted after revision 22 November 2009; first published online 23 November 2009)
© 2010 The Authors. Journal compilation © 2010 The Physiological Society
http://jp.physoc.org/content/588/2/341.short
these data and others might further direct bodybuilders to avoid gh as an effective drug for muscle hypertrophy and towards using gh for injuries or tendon healing.
Growth hormone stimulates the collagen synthesis in human tendon and skeletal muscle without affecting myofibrillar protein synthesis
<LI id=contrib-1>Simon Doessing (http://jp.physoc.org/search?author1=Simon+Doessing&sortspec=date&submit=Submit)1 (http://jp.physoc.org/content/588/2/341.short#target-1), <LI id=contrib-2>Katja M. Heinemeier (http://jp.physoc.org/search?author1=Katja+M.+Heinemeier&sortspec=date&submit=Submit)1 (http://jp.physoc.org/content/588/2/341.short#target-1), <LI id=contrib-3>Lars Holm (http://jp.physoc.org/search?author1=Lars+Holm&sortspec=date&submit=Submit)1 (http://jp.physoc.org/content/588/2/341.short#target-1), <LI id=contrib-4>Abigail L. Mackey (http://jp.physoc.org/search?author1=Abigail+L.+Mackey&sortspec=date&submit=Submit)1 (http://jp.physoc.org/content/588/2/341.short#target-1), <LI id=contrib-5>Peter Schjerling (http://jp.physoc.org/search?author1=Peter+Schjerling&sortspec=date&submit=Submit)1 (http://jp.physoc.org/content/588/2/341.short#target-1), <LI id=contrib-6>Michael Rennie (http://jp.physoc.org/search?author1=Michael+Rennie&sortspec=date&submit=Submit)3 (http://jp.physoc.org/content/588/2/341.short#target-3), <LI id=contrib-7>Kenneth Smith (http://jp.physoc.org/search?author1=Kenneth+Smith&sortspec=date&submit=Submit)3 (http://jp.physoc.org/content/588/2/341.short#target-3), <LI id=contrib-8>Søren Reitelseder (http://jp.physoc.org/search?author1=S%C3%B8ren+Reitelseder&sortspec=date&submit=Submit)1 (http://jp.physoc.org/content/588/2/341.short#target-1), <LI id=contrib-9>Anne-Marie Kappelgaard (http://jp.physoc.org/search?author1=Anne-Marie+Kappelgaard&sortspec=date&submit=Submit)4 (http://jp.physoc.org/content/588/2/341.short#target-4), <LI id=contrib-10>Michael Højby Rasmussen (http://jp.physoc.org/search?author1=Michael+H%C3%B8jby+Rasmussen&sortspec=date&submit=Submit)4 (http://jp.physoc.org/content/588/2/341.short#target-4), <LI id=contrib-11>Allan Flyvbjerg (http://jp.physoc.org/search?author1=Allan+Flyvbjerg&sortspec=date&submit=Submit)5 (http://jp.physoc.org/content/588/2/341.short#target-5) and
Michael Kjaer (http://jp.physoc.org/search?author1=Michael+Kjaer&sortspec=date&submit=Submit)1 (http://jp.physoc.org/content/588/2/341.short#target-1)
+ (http://jp.physoc.org/content/588/2/341.short#) Author Affiliations
1Institute of Sports Medicine, Bispebjerg Hospital, Center of Healthy Aging, Faculty of Health Sciences, University of Copenhagen, Bispebjerg Bakke 23, DK-2400 Copenhagen NV, Denmark2Department of Endocrinology, Copenhagen University Hospital Rigshospitalet, Blegdamsvej 9, DK-2100 Copenhagen Ø, Denmark3School of Biomedical Sciences, University of Nottingham Medical School, Derby City General Hospital, Derby DE22 3DT, UK4Medical & Science, Global Development, Novo Nordisk, DK-2880 Bagsvaerd, Denmark5The Medical Research Laboratories, Clinical Institute and Medical Department M (Diabetes and Endocrinology), Aarhus University Hospital, Aarhus C, Denmark
Corresponding author
S. Doessing: Institute of Sports Medicine, Bispebjerg Hospital, Center of Healthy Aging, Faculty of Health Sciences, University of Copenhagen, Bispebjerg Bakke 23, DK-2400 Copenhagen NV, Denmark. Email: [email protected] ([email protected])
Abstract
In skeletal muscle and tendon the extracellular matrix confers important tensile properties and is crucially important for tissue regeneration after injury. Musculoskeletal tissue adaptation is influenced by mechanical loading, which modulates the availability of growth factors, including growth hormone (GH) and insulin-like growth factor-I (IGF-I), which may be of key importance. To test the hypothesis that GH promotes matrix collagen synthesis in musculotendinous tissue, we investigated the effects of 14 day administration of 33–50 μg kg−1 day−1 recombinant human GH (rhGH) in healthy young individuals. rhGH administration caused an increase in serum GH, serum IGF-I, and IGF-I mRNA expression in tendon and muscle. Tendon collagen I mRNA expression and tendon collagen protein synthesis increased by 3.9-fold and 1.3-fold, respectively (P < 0.01 and P = 0.02), and muscle collagen I mRNA expression and muscle collagen protein synthesis increased by 2.3-fold and 5.8-fold, respectively (P < 0.01 and P = 0.06). Myofibrillar protein synthesis was unaffected by elevation of GH and IGF-I. Moderate exercise did not enhance the effects of GH manipulation. Thus, increased GH availability stimulates matrix collagen synthesis in skeletal muscle and tendon, but without any effect upon myofibrillar protein synthesis. The results suggest that GH is more important in strengthening the matrix tissue than for muscle cell hypertrophy in adult human musculotendinous tissue.
Footnotes
(Received 25 July 2009; accepted after revision 22 November 2009; first published online 23 November 2009)
© 2010 The Authors. Journal compilation © 2010 The Physiological Society