Tendon and skeletal muscle matrix gene expression and functional responses to immobilisation and rehabilitation in young males: Effect of growth hormone administration

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Standard

Tendon and skeletal muscle matrix gene expression and functional responses to immobilisation and rehabilitation in young males : Effect of growth hormone administration. / Boesen, Anders Ploug; Dideriksen, Kasper; Couppé, Christian; Magnusson, Peter; Schjerling, Peter; Boesen, Mikael; Kjær, Michael; Langberg, Henning.

I: Journal of Physiology, 30.09.2013, s. 6039-6052.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

Boesen, AP, Dideriksen, K, Couppé, C, Magnusson, P, Schjerling, P, Boesen, M, Kjær, M & Langberg, H 2013, 'Tendon and skeletal muscle matrix gene expression and functional responses to immobilisation and rehabilitation in young males: Effect of growth hormone administration', Journal of Physiology, s. 6039-6052. https://doi.org/10.1113/jphysiol.2013.261263

APA

Boesen, A. P., Dideriksen, K., Couppé, C., Magnusson, P., Schjerling, P., Boesen, M., Kjær, M., & Langberg, H. (2013). Tendon and skeletal muscle matrix gene expression and functional responses to immobilisation and rehabilitation in young males: Effect of growth hormone administration. Journal of Physiology, 6039-6052. https://doi.org/10.1113/jphysiol.2013.261263

Vancouver

Boesen AP, Dideriksen K, Couppé C, Magnusson P, Schjerling P, Boesen M o.a. Tendon and skeletal muscle matrix gene expression and functional responses to immobilisation and rehabilitation in young males: Effect of growth hormone administration. Journal of Physiology. 2013 sep. 30;6039-6052. https://doi.org/10.1113/jphysiol.2013.261263

Author

Boesen, Anders Ploug ; Dideriksen, Kasper ; Couppé, Christian ; Magnusson, Peter ; Schjerling, Peter ; Boesen, Mikael ; Kjær, Michael ; Langberg, Henning. / Tendon and skeletal muscle matrix gene expression and functional responses to immobilisation and rehabilitation in young males : Effect of growth hormone administration. I: Journal of Physiology. 2013 ; s. 6039-6052.

Bibtex

@article{1bc468e1bee644328c38809afcb219ba,
title = "Tendon and skeletal muscle matrix gene expression and functional responses to immobilisation and rehabilitation in young males: Effect of growth hormone administration",
abstract = "We examined the effect of growth hormone (GH) on connective tissue of tendon and skeletal muscle during immobilisation and re-training in humans. Young men (20-30 years; n=20) were randomly assigned to daily recombinant GH (rhGH)(33-50μg/kg/d) or placebo (Plc), and had one leg immobilised for two weeks followed by six weeks of strength training. Cross sectional area (CSA), maximal muscle strength (MVC) and biomechanical properties of m.quadriceps and patellar tendon were determined. Muscle and tendon biopsies were analysed for mRNA of collagen (COL-1A1/3A1), insulin-like growth factors (IGF-1Ea/Ec), lysyloxidase (LOX), matrix metalloproteases (MMP-2 and -9), decorin and tenascin-C. Fibril morphology was analysed by transmission electron microscope (TEM) to detect changes in fibril diameter distribution. In muscle the CSA and MVC declined with immobilisation, and recovered with rehabilitation similar in both groups. Likewise, both groups increased in IGF-1Ea/Ec and COL-1A1/3A1 expression in muscle during re-training after immobilisation compared to baseline, and the rise was more pronounced when subjects recieved GH. The tendon CSA did not change during immobilisation, but increased in both groups during six weeks of rehabilitation (~14%). A decline in tendon stiffness after immobilisation was observed only in Plc, and an increase during six weeks rehabilitation was observed only in GH. IGF-1Ea and COL-1A1/3A1 mRNA increased with immobilisation in the GH group only, and LOX mRNA was after immobilisation higher in the GH group vs Plc. Both groups increased in MMP-2 with immobilisation, whereas no changes in MMP-9, decorin and tenascin-C were observed. Tendon fibril diameter distribution remained unchanged in both groups. In conclusion, GH stimulates collagen expression in both skeletal muscle and tendon and abolishes the normal inactivity related decline in tendon stiffness and LOX, and results in an increased tendon CSA and stiffness during rehabilitation. GH has a matrix stabilising effect during periods with inactivity and rehabilitation in humans.",
author = "Boesen, {Anders Ploug} and Kasper Dideriksen and Christian Coupp{\'e} and Peter Magnusson and Peter Schjerling and Mikael Boesen and Michael Kj{\ae}r and Henning Langberg",
year = "2013",
month = sep,
day = "30",
doi = "10.1113/jphysiol.2013.261263",
language = "English",
pages = "6039--6052",
journal = "The Journal of Physiology",
issn = "0022-3751",
publisher = "Wiley-Blackwell",

}

RIS

TY - JOUR

T1 - Tendon and skeletal muscle matrix gene expression and functional responses to immobilisation and rehabilitation in young males

T2 - Effect of growth hormone administration

AU - Boesen, Anders Ploug

AU - Dideriksen, Kasper

AU - Couppé, Christian

AU - Magnusson, Peter

AU - Schjerling, Peter

AU - Boesen, Mikael

AU - Kjær, Michael

AU - Langberg, Henning

PY - 2013/9/30

Y1 - 2013/9/30

N2 - We examined the effect of growth hormone (GH) on connective tissue of tendon and skeletal muscle during immobilisation and re-training in humans. Young men (20-30 years; n=20) were randomly assigned to daily recombinant GH (rhGH)(33-50μg/kg/d) or placebo (Plc), and had one leg immobilised for two weeks followed by six weeks of strength training. Cross sectional area (CSA), maximal muscle strength (MVC) and biomechanical properties of m.quadriceps and patellar tendon were determined. Muscle and tendon biopsies were analysed for mRNA of collagen (COL-1A1/3A1), insulin-like growth factors (IGF-1Ea/Ec), lysyloxidase (LOX), matrix metalloproteases (MMP-2 and -9), decorin and tenascin-C. Fibril morphology was analysed by transmission electron microscope (TEM) to detect changes in fibril diameter distribution. In muscle the CSA and MVC declined with immobilisation, and recovered with rehabilitation similar in both groups. Likewise, both groups increased in IGF-1Ea/Ec and COL-1A1/3A1 expression in muscle during re-training after immobilisation compared to baseline, and the rise was more pronounced when subjects recieved GH. The tendon CSA did not change during immobilisation, but increased in both groups during six weeks of rehabilitation (~14%). A decline in tendon stiffness after immobilisation was observed only in Plc, and an increase during six weeks rehabilitation was observed only in GH. IGF-1Ea and COL-1A1/3A1 mRNA increased with immobilisation in the GH group only, and LOX mRNA was after immobilisation higher in the GH group vs Plc. Both groups increased in MMP-2 with immobilisation, whereas no changes in MMP-9, decorin and tenascin-C were observed. Tendon fibril diameter distribution remained unchanged in both groups. In conclusion, GH stimulates collagen expression in both skeletal muscle and tendon and abolishes the normal inactivity related decline in tendon stiffness and LOX, and results in an increased tendon CSA and stiffness during rehabilitation. GH has a matrix stabilising effect during periods with inactivity and rehabilitation in humans.

AB - We examined the effect of growth hormone (GH) on connective tissue of tendon and skeletal muscle during immobilisation and re-training in humans. Young men (20-30 years; n=20) were randomly assigned to daily recombinant GH (rhGH)(33-50μg/kg/d) or placebo (Plc), and had one leg immobilised for two weeks followed by six weeks of strength training. Cross sectional area (CSA), maximal muscle strength (MVC) and biomechanical properties of m.quadriceps and patellar tendon were determined. Muscle and tendon biopsies were analysed for mRNA of collagen (COL-1A1/3A1), insulin-like growth factors (IGF-1Ea/Ec), lysyloxidase (LOX), matrix metalloproteases (MMP-2 and -9), decorin and tenascin-C. Fibril morphology was analysed by transmission electron microscope (TEM) to detect changes in fibril diameter distribution. In muscle the CSA and MVC declined with immobilisation, and recovered with rehabilitation similar in both groups. Likewise, both groups increased in IGF-1Ea/Ec and COL-1A1/3A1 expression in muscle during re-training after immobilisation compared to baseline, and the rise was more pronounced when subjects recieved GH. The tendon CSA did not change during immobilisation, but increased in both groups during six weeks of rehabilitation (~14%). A decline in tendon stiffness after immobilisation was observed only in Plc, and an increase during six weeks rehabilitation was observed only in GH. IGF-1Ea and COL-1A1/3A1 mRNA increased with immobilisation in the GH group only, and LOX mRNA was after immobilisation higher in the GH group vs Plc. Both groups increased in MMP-2 with immobilisation, whereas no changes in MMP-9, decorin and tenascin-C were observed. Tendon fibril diameter distribution remained unchanged in both groups. In conclusion, GH stimulates collagen expression in both skeletal muscle and tendon and abolishes the normal inactivity related decline in tendon stiffness and LOX, and results in an increased tendon CSA and stiffness during rehabilitation. GH has a matrix stabilising effect during periods with inactivity and rehabilitation in humans.

U2 - 10.1113/jphysiol.2013.261263

DO - 10.1113/jphysiol.2013.261263

M3 - Journal article

C2 - 24081158

SP - 6039

EP - 6052

JO - The Journal of Physiology

JF - The Journal of Physiology

SN - 0022-3751

ER -

ID: 51582942