Article
Growth hormone stimulates the collagen synthesis in human tendon and skeletal muscle without affecting myofibrillar protein synthesis.
Institute of Sports Medicine, Bispebjerg Hospital, Center of Healthy Aging, Faculty of Health Sciences, University of Copenhagen, Copenhagen NV, Denmark.
The Journal of Physiology (impact factor:
4.72).
11/2009;
588(Pt 2):341-51.
DOI:10.1113/jphysiol.2009.179325
pp.341-51
Source: PubMed
- Citations (3)
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Cited In (0)
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Article: Quantitative effects of position and type of single mismatch on single base primer extension.
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ABSTRACT: Single mismatch (MM) present at the region where primer binds onto the template strand can greatly affect the PCR efficacy. Earlier studies revealed that PCR or primer extension is hindered by a single MM at the primer 3' end. The MMs located at other positions within a primer also have similar performance, but to what extent they can decrease the efficiency is not clear. In this study, a modified single base extension assay was used to systematically compare the extension efficiencies between a perfect-matched (PM) primer and its single-MM primers with all possible MM types. The extension efficiencies of single-MM primers, which were generally lower or equivalent to that of the PM primer, were observed to strongly depend on the MM location and/or type. Due to the enzymatic activity, single MMs present at the last 3-4 positions from the primer 3' end exhibited zero or minimal (<3.9%) extension efficiencies. For those MMs at positions 5 onward from primer 3' end where was affected mainly by the primer-target binding stability, an increasing trend in extension efficiency with the highest (i.e., 69.3%) occurring at the primer 5' end was observed to significantly correlate in an inverse relationship with the duplex stability (i.e., difference of melting temperature) under a empirically polynomial equation, y=-0.0731 x(3) + 2.2519 x(2) - 22.617 x + 76.691 (R(2)=0.5318). It was further shown that the extension efficiencies of these MM types could be improved with a factor of 3.25 on average in relation to the decrease in the annealing temperature by 7 degrees C. On the other hand, substitution of a less selective inosine nucleotide did not convincingly improve the extension efficiency. Overall findings obtained could further improve the rational design of oligonucleotide primers in various microbiological studies that involve the use of PCR techniques.Journal of microbiological methods 04/2009; 77(3):267-75. · 2.43 Impact Factor -
Article: Growth hormone increases IGF-I, collagen I and collagen III gene expression in dwarf rat skeletal muscle.
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ABSTRACT: The effect of short-term treatment with biosynthetic growth hormone (GH) of male dwarf rats was studied in EDL and soleus muscles. In situ hybridisation revealed that in the untreated dwarf rat collagen I, collagen III and insulin-like growth factor-I (IGF-I) mRNA is mainly expressed by fibroblasts between the muscle fibre areas. Quantitative image analysis showed that, 8 h after a single GH injection, the level of mRNA for all three genes increased compared to the untreated dwarf animal. IGF-I mRNA levels were similar in normals and untreated dwarf rats but significantly increased 8 h after a single GH injection in EDL (P < 0.01) and soleus (P < 0.001). In untreated dwarf rats, collagen I and III gene expression was significantly less than in normal animals (P < 0.001). Collagen III gene expression also increased significantly 8 h after a single GH injection, in both muscles (P < 0.01). Collagen I gene expression showed significant increases 8 and 24 h after GH treatment in EDL (P < 0.01), although the increases seen in soleus did not reach significance. The effects of multiple GH injections (one, two or four) did not appear to be additive. The results of the time course studies are consistent with an intermediary role for IGF-I in the production of collagen in muscle.Molecular and Cellular Endocrinology 01/1996; 115(2):187-97. · 4.19 Impact Factor -
Article: Recombinant human insulin-like growth factor-I stimulates in vitro matrix synthesis and cell proliferation in rabbit flexor tendon.
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ABSTRACT: Flexor tendons have an intrinsic ability for repair, with a capacity to metabolize matrix components and to proliferate. To identify factors with the potential of affecting those abilities, the effects of recombinant human insulin-like growth factor (rhIGF-I), insulin and fetal calf serum (FCS) on the synthesis of proteoglycan, collagen, and non-collagen protein and cell proliferation were investigated in short-term explant cultures of the deep flexor tendon of the rabbit. Matrix synthesis and cell proliferation were stimulated dose dependently by rhIGF-I at doses between 10 and 250 and at 10-100 ng/ml, respectively, by insulin at 250-5,000 ng/ml, and by FCS at 2-15%. Estimated maximal stimulation (Emax) of up to three times the control value was observed with rhIGF-I at 250 ng/ml. Maximal stimulation was observed at 5,000 ng/ml with insulin, and FCS at 15%. rhIGF-I was more potent than insulin in stimulating protein synthesis and cell proliferation. The Emax of stimulation of proteoglycan and collagen synthesis by rhIGF-I were two times that of FCS, and the Emax of cell proliferation by FCS was twice that of rhIGF-I. Growth factors thus have the ability to stimulate matrix synthesis and cell proliferation in rabbit flexor tendon. This provides a rationale for further studies on the role of growth factors in flexor tendon healing in humans.Journal of Orthopaedic Research 08/1991; 9(4):495-502. · 2.81 Impact Factor
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Keywords
14 day administration
adult human musculotendinous tissue
extracellular matrix
GH availability stimulates matrix collagen synthesis
GH promotes matrix collagen synthesis
healthy young individuals
insulin-like growth factor-I
key importance
matrix tissue
muscle cell hypertrophy
muscle collagen protein synthesis
Musculoskeletal tissue adaptation
musculotendinous tissue
myofibrillar protein synthesis
rhGH
rhGH administration
serum GH
skeletal muscle
tendon collagen protein synthesis
tissue regeneration