Growth hormone stimulates the collagen synthesis in human tendon and skeletal muscle without affecting myofibrillar protein synthesis

Simon Doessing; Katja M Heinemeier; Lars Holm; Abigail Mackey; Peter Schjerling; Michael Rennie; Kenneth Smith Petersen; Søren Reitelseder; Anne-Marie Kappelgaard; Michael Højby Rasmussen; Allan Flyvbjerg; Michael Kjaer

doi:10.1113/jphysiol.2009.179325

Growth hormone stimulates the collagen synthesis in human tendon and skeletal muscle without affecting myofibrillar protein synthesis

Simon Doessing, Katja M Heinemeier, Lars Holm, Abigail Mackey, Peter Schjerling, Michael Rennie, Kenneth Smith Petersen, Søren Reitelseder, Anne-Marie Kappelgaard, Michael Højby Rasmussen, Allan Flyvbjerg, Michael Kjaer

139 Citations (Scopus)

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.

Original language	English
Journal	Journal of Physiology
Volume	588
Issue number	Pt 2
Pages (from-to)	341-51
Number of pages	11
ISSN	0022-3751
DOIs	https://doi.org/10.1113/jphysiol.2009.179325
Publication status	Published - 15 Jan 2010

Keywords

Adult
Collagen
Cross-Over Studies
Double-Blind Method
Exercise
Fluoroimmunoassay
Human Growth Hormone
Humans
Insulin-Like Growth Factor I
Male
Muscle Proteins
Muscle, Skeletal
Protein Biosynthesis
RNA, Messenger
Reverse Transcriptase Polymerase Chain Reaction
Tendons
Time Factors

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1113/jphysiol.2009.179325

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Doessing, S., Heinemeier, K. M., Holm, L., Mackey, A., Schjerling, P., Rennie, M., Petersen, K. S., Reitelseder, S., Kappelgaard, A.-M., Rasmussen, M. H., Flyvbjerg, A., & Kjaer, M. (2010). Growth hormone stimulates the collagen synthesis in human tendon and skeletal muscle without affecting myofibrillar protein synthesis. Journal of Physiology, 588(Pt 2), 341-51. https://doi.org/10.1113/jphysiol.2009.179325

Doessing, S, Heinemeier, KM, Holm, L, Mackey, A , Schjerling, P, Rennie, M, Petersen, KS, Reitelseder, S, Kappelgaard, A-M, Rasmussen, MH, Flyvbjerg, A & Kjaer, M 2010, 'Growth hormone stimulates the collagen synthesis in human tendon and skeletal muscle without affecting myofibrillar protein synthesis', Journal of Physiology, vol. 588, no. Pt 2, pp. 341-51. https://doi.org/10.1113/jphysiol.2009.179325

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title = "Growth hormone stimulates the collagen synthesis in human tendon and skeletal muscle without affecting myofibrillar protein synthesis",

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.",

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T1 - Growth hormone stimulates the collagen synthesis in human tendon and skeletal muscle without affecting myofibrillar protein synthesis

AU - Doessing, Simon

AU - Heinemeier, Katja M

AU - Holm, Lars

AU - Mackey, Abigail

AU - Schjerling, Peter

AU - Rennie, Michael

AU - Petersen, Kenneth Smith

AU - Reitelseder, Søren

AU - Kappelgaard, Anne-Marie

AU - Rasmussen, Michael Højby

AU - Flyvbjerg, Allan

AU - Kjaer, Michael

PY - 2010/1/15

Y1 - 2010/1/15

N2 - 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.

AB - 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.

KW - Adult

KW - Collagen

KW - Cross-Over Studies

KW - Double-Blind Method

KW - Exercise

KW - Fluoroimmunoassay

KW - Human Growth Hormone

KW - Humans

KW - Insulin-Like Growth Factor I

KW - Male

KW - Muscle Proteins

KW - Muscle, Skeletal

KW - Protein Biosynthesis

KW - RNA, Messenger

KW - Reverse Transcriptase Polymerase Chain Reaction

KW - Tendons

KW - Time Factors

U2 - 10.1113/jphysiol.2009.179325

DO - 10.1113/jphysiol.2009.179325

M3 - Journal article

C2 - 19933753

SN - 0022-3751

VL - 588

SP - 341

EP - 351

JO - Journal of Physiology

JF - Journal of Physiology

IS - Pt 2

ER -

Growth hormone stimulates the collagen synthesis in human tendon and skeletal muscle without affecting myofibrillar protein synthesis

Abstract

Keywords

UN SDGs

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