Human growth hormone prevents the protein catabolic side effects of prednisone in humans.

Horber, Fritz F.; Haymond, Morey W.

doi:10.1172/jci114694

Cited by 397 publications

(186 citation statements)

References 41 publications

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“…Our current findings of the effects of ST on whole body accretion rates and amino acid oxidation are in accord with the majority of previous studies in animals and humans (4,6,17,24,25,29,37,38,45,46). However, less is known about the specific effects of ST on whole body proteolysis rates in the postabsorptive and postprandial states.…”

Section: Discussionsupporting

confidence: 90%

“…However, less is known about the specific effects of ST on whole body proteolysis rates in the postabsorptive and postprandial states. In fact, conflicting results of an increase (42), decrease (45), and/or no change (24,29) in whole body proteolysis rates have been reported with ST treatment in either postabsorptive (24,29) or postprandial states (42,45). In the current study with phenylalanine tracers, as in our previous study using a leucine tracer (45), we found that ST treatment in fed growing swine reduced whole body proteolysis.…”

Section: Discussioncontrasting

confidence: 41%

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Somatotropin-induced protein anabolism in hindquarters and portal-drained viscera of growing pigs

Bush

Burrin

Suryawan

et al. 2003

American Journal of Physiology-Endocrinology and Metabolism

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Arterial, portal venous, and vena cava whole blood samples, breath samples, and blood flow measurements were obtained for determination of tissue and whole body phenylalanine kinetics under steady-state conditions. In the fed state, ST treatment decreased whole body phenylalanine flux, oxidation, and protein degradation without altering protein synthesis, resulting in an improvement in whole body net protein balance. Blood flow to the HQ (ϩ80%), but not to the PDV, was increased with ST treatment. In the HQ and PDV, ST increased phenylalanine uptake (ϩ44 and ϩ23%, respectively) and protein synthesis (ϩ43 and ϩ41%, respectively), with no effect on protein degradation. In ST-treated and control pigs, phenylalanine was oxidized in the PDV (34-43% of enteral and arterial sources) but not the HQ. In both treatment groups, dietary (40%) rather than arterial (10%) extraction of phenylalanine predominated in gut amino acid metabolism, whereas localized blood flow influenced HQ amino acid metabolism. The results indicate that ST increases protein anabolism in young, growing swine by increasing protein synthesis in the HQ and PDV, with no effect on protein degradation. Differing results between the whole body and the HQ and PDV suggest that the effect of ST treatment on protein metabolism is tissue specific.

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Section: Discussionsupporting

confidence: 90%

Section: Discussioncontrasting

confidence: 41%

Somatotropin-induced protein anabolism in hindquarters and portal-drained viscera of growing pigs

Bush

Burrin

Suryawan

et al. 2003

American Journal of Physiology-Endocrinology and Metabolism

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“…On the other hand, the forearm release of leucine was markedly diminished during rhGH administration; this is in line with the GH-related effects of reducing leucine oxidation and increasing the use of leucine for protein synthesis (32). The diminished muscle production of BCAA was probably accompanied by a reduced utilization by other organs, in order to keep their circulating levels unchanged.…”

Section: Discussionsupporting

confidence: 64%

Effects of recombinant human growth hormone on muscle protein turnover in malnourished hemodialysis patients.

Garibotto¹,

Barreca²,

Russo³

et al. 1997

J. Clin. Invest.

106

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To assess the effect of recombinant human growth hormone (rhGH) on muscle protein metabolism in uremic patients with malnutrition, forearm [ 3 H]phenylalanine kinetics were evaluated in six chronically wasted (body weight 79% of ideal weight) hemodialysis (HD) patients in a self-controlled, crossover study. Forearm protein dynamics were evaluated before, after a 6-wk course of rhGH (5 mg thrice weekly) and after a 6-wk washout period. After rhGH: ( a ) forearm phenylalanine net balance-the difference between phenylalanine incorporation into and phenylalanine release from muscle proteins-decreased by 46% ( Ϫ 8 Ϯ 2 vs. Ϫ 15 Ϯ 2 nmol/min·100 ml at the baseline and Ϫ 11 Ϯ 2 after washout,

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“…hGH has anabolic effects, which result in an increase in lean body mass (6,10,14). In contrast to other anabolic agents, hGH also has anticatabolic actions mediated via the direct effects on cells, the release of insulin-like growth factor type 1, and the protein-sparing effects of lipid oxidation (2,5,10,19,21). Given the clinical benefits of r-hGH in patients with AIDS-related wasting, our findings that r-hGH has no effect on viral replication or on the antiretroviral activity of currently available ARVs are reassuring.…”

mentioning

confidence: 61%

Lack of Effect of Recombinant Human Growth Hormone on the In Vitro Activities of Antiretroviral Drugs against Human Immunodeficiency Virus Type 1

Wainberg

Brenner

Daar

et al. 2004

Antimicrob Agents Chemother

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We studied the effects of recombinant human growth hormone (r-hGH) on human immunodeficiency virus type 1 replication by growing both wild-type and drug-resistant variants of virus in the presence of various concentrations of eight different antiretroviral drugs. r-hGH had no significant effect on either viral replication or the 50% inhibitory concentrations of these compounds.Although highly active antiretroviral therapy (HAART) has led to declines in the rates of mortality and AIDS-related opportunistic infections in the developed world, there remains a need to prevent the loss of lean body tissue (wasting) in patients with human immunodeficiency virus (HIV) infection and AIDS (12,16). Human growth hormone (hGH) increases lean body mass and muscle nitrogen retention and thus represents a potential approach to the treatment of AIDS-related wasting (9, 13). In randomized double-blind placebo-controlled trials performed in the pre-HAART and HAART eras, recombinant hGH (r-hGH) was shown to increase total body weight and lean body mass and to decrease body fat content (9,15,17,20). These changes are associated with improvements in physical performance and quality of life (15,17,20). Although optimization of nutritional status and exercise may also provide benefits in many cases, treatment with hGH is an excellent option in patients with severe wasting.However, concern exists that r-hGH might stimulate viral replication or inhibit the activities of antiretroviral drugs (ARVs) (4), since one early study actually found that r-hGH increased the levels of p24 antigen released from peripheral blood mononuclear cells (PBMCs) in tissue culture at concentrations of 50 or 100 ng/ml, but not at concentrations of 1, 5, 10, or 250 ng/ml (7). Importantly, r-hGH did not affect the antiviral activity of zidovudine in that study. Subsequent experiments (E. Daar, unpublished data) showed that r-hGH did not increase the level of HIV replication in PBMCs at concentrations of up to 250 ng/ml and had no effect on the antiviral activities of a variety of ARVs used in the pre-HAART era (zidovudine, didanosine, zalcitabine, and stavudine). The present experiments confirm and extend these findings through the use of currently approved ARVs in each of the three major drug classes. Viral isolates. We used two wild-type (wt) and five drugresistant clinical isolates of HIV type 1 (HIV-1), the genotypes of which are shown in Table 1. The wt isolates were from patients who had not received therapy. The concentrations of all approved ARVs that inhibit viral replication by 50% (IC 50 s) for the isolates were confirmed to be the same as those for other wt isolates, and the phenotypes of the isolates were the same as those of other wt isolates. Genotyping for the detection of mutations associated with drug resistance was performed by sequencing analysis with the Tru-Gene system (Bayer Diagnostics Inc., Toronto, Ontario, Canada). The resistant isolates were from patients who had been extensively treated with antiviral agents.In vitro studies. IC 50 s ...

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Human growth hormone prevents the protein catabolic side effects of prednisone in humans.

Cited by 397 publications

References 41 publications

Somatotropin-induced protein anabolism in hindquarters and portal-drained viscera of growing pigs

Somatotropin-induced protein anabolism in hindquarters and portal-drained viscera of growing pigs

Effects of recombinant human growth hormone on muscle protein turnover in malnourished hemodialysis patients.

Lack of Effect of Recombinant Human Growth Hormone on the In Vitro Activities of Antiretroviral Drugs against Human Immunodeficiency Virus Type 1

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