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The Journal of Clinical Endocrinology & Metabolism Vol. 82, No. 1 243-246
Copyright © 1997 by The Endocrine Society

Clinical Studies

The Effect of Recombinant Human Growth Hormone on Glucose and Leucine Metabolism in Cushing’s Syndrome1

Susan B. Bowes, Margot Umpleby, Michael H. Cummings, Nicola C. Jackson, Paul V. Carroll, Clara Lowy, Peter H. Sönksen and David L. Russell-Jones

Department of Medicine, United Medical and Dental Schools of Guys and St. Thomas’s Hospitals, St. Thomas’s Hospital, London, United Kingdom

Address all correspondence and requests for reprints to: Dr. S. B. Bowes, Department of Medicine, 4th Floor North Wing, St. Thomas’s Hospital, Lambeth Palace Road, London, United Kingdom SE1 7EH.


   Abstract
Top
 Abstract
Introduction
 Subjects and Methods
 Results
 Discussion
 References
 
Cushing’s syndrome is characterized by central obesity and muscle wasting. As GH is anabolic, it may be able to counteract the loss of body protein. To evaluate the potential therapeutic use of GH preoperatively, eight patients with Cushing’s syndrome received sc injections of recombinant human GH (0.07 U/kg·day) for 7 days. Whole body leucine and glucose turnover were measured after an infusion of [1-13C]leucine and [6,6-2H2]glucose before (day 0) and after 2 and 7 days of GH treatment. Compared with the value on day 0, there was a significant increase on days 2 and 7 in insulin (P < 0.005 and P < 0.001), C peptide (P < 0.01 and P < 0.005), insulin-like growth factor I (P < 0.001), and glucose concentrations (P < 0.01 and P < 0.005) and a decrease in the leucine concentration (P < 0.005). There was no significant change in glucose production rate, glucose MCR, leucine production rate (a measure of protein degradation), or nonoxidative leucine disappearance rate (a measure of protein synthesis). The leucine MCR was increased after 7 days (P < 0.05), and the clearance of leucine into protein (nonoxidative leucine disappearance rate/leucine concentration) was increased (P < 0.05) after 2 and 7 days of GH treatment. This is consistent with GH stimulating the availability of amino acid transporters. GH may, therefore, have a therapeutic role in the preoperative treatment of Cushing’s syndrome.


   Introduction
Top
 Abstract
 Introduction
Subjects and Methods
 Results
 Discussion
 References
 
THE CHRONIC glucocorticoid excess of Cushing’s syndrome is characterized by profoundly altered body composition. Muscle weakness (1) and reduced muscle mass (2) are common features and appear to be due to a reduction in whole body protein synthesis compared with that in normal subjects (3), whereas fat mass is increased (2).

Recent studies have shown that GH has an important role in regulating protein metabolism. GH-deficient adults treated with GH had increased lean body mass, due to stimulation of protein synthesis, and decreased fat mass (4). GH has also been shown to counteract the net catabolic effects on protein metabolism of short term excess glucocorticoids in normal subjects (5) and patients receiving chronic glucocorticoid treatment (6). There is thus some rationale for the possible use of exogenous GH to counteract the net catabolic effect of excess endogenous steroids in Cushing’s syndrome. However, as GH has been shown to decrease the insulin sensitivity of glucose metabolism (7), any beneficial effect of GH on protein anabolism may be offset by an increase in insulin resistance. To examine this further, we undertook isotopic studies to investigate the effect of short term GH administration to patients with Cushing’s syndrome on protein and glucose metabolism.


   Subjects and Methods
Top
 Abstract
 Introduction
 Subjects and Methods
Results
 Discussion
 References
 
Experimental subjects

Studies were performed in eight patients (aged 30–63 yr) 1 week before surgery for Cushing’s syndrome (Table 1Go). The diagnosis was established by the measurement of 0900 and 2400 h cortisol concentrations, the 0900 h cortisol level after the administration of 1 mg oral dexamethasone at 2300 h the previous day, cortisol secretion rate, and low and high dose (2 and 6 mg) dexamethasone suppression tests. In patients with pituitary-dependent Cushing’s syndrome, all other pituitary function was normal. All patients gave informed written consent, and the studies were approved by St. Thomas’s Hospital ethics committee.


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  		Table 1. Clinical details of patients

 
Study design

Patients received sc injections of GH (0.07 U/kg·day) for 7 days and were studied at 0900 h after an overnight fast before treatment and then after 2 and 7 days of treatment. This dose of GH has previously been shown to increase protein synthesis in GH-deficient adults (4) and was chosen because Cushing’s syndrome patients were likely to be GH resistant. One patient (no. 3) received GH for only 2 days due to fluid retention and, therefore, was studied before and after 2 days of treatment. All studies were performed in the metabolic research area of the Diabetes and Endocrinology Day Center at St. Thomas’ Hospital. A primed constant infusion of [1-13C]leucine (1 mg/kg; 1 mg/kg·h) and [6,6-2H2]glucose (170 mg; 102 mg/h; Mass Trace, Somerville, NJ) was administered iv for 180 min with a priming dose of sodium [13C]bicarbonate (0.2 mg/kg; mass trace). Blood and breath samples were taken at 0, 150, 155, 160, 165, 170, and 180 min to measure the isotopic enrichment and concentration of glucose, {alpha}-ketoisocaproic acid ({alpha}KIC) enrichment, leucine concentration, and enrichment of expired CO2. Baseline blood samples were also taken for the measurement of insulin, insulin-like growth factor I (IGF-I), and C peptide concentrations.

Analytical methods

Using gas chromatography-mass spectrometry (5971A MSD, Hewlett-Packard, Palo Alto, CA) and selected ion monitoring, {alpha}KIC enrichment was measured as the quinoxalinol-trimethylsilyl derivative at m/z 232 and 233 (8), and glucose enrichment was measured as the glucose acetate boronate derivative at m/z 297 and 299 (9) [within-assay coefficient of variation (CV) for both measurements, <2%]. 13C enrichment of breath CO2 was measured on a VG SIRA series II isotope ratio mass spectrometer (VG Isotech, Cheshire, UK; within-assay CV, <1%). The CO2 production rate was measured at 0, 150, and 180 min with a Metabolic Measurement Cart (Medical Graphics Corp., Minneapolis, MN). Plasma leucine concentration was measured using an Alpha Plus II automated amino acid analyzer (within-assay CV, 4%; Pharmacia, Cambridge, UK). Insulin and C peptide were measured by double antibody RIA (within-assay CV, 6% and 9%, respectively) (10).

The C peptide assay used an anti-C peptide antiserum (GP644) kindly donated by Prof. A. Rubenstein (Department of Medicine, University of Chicago, Chicago, IL). Plasma cortisol was measured by RIA, using an iodinated label and a polyethylene glycol-assisted double antibody method, and the cortisol secretion rate was determined by isotope dilution using a modification of the method of Brooks et al. (11). The plasma glucose concentration was measured on a Clandon Scientific Glucose Analyzer (within-assay CV, 2%; Yellow Springs Instrument Co., Yellow Springs, OH), and plasma total IGF-I was determined by RIA after an ethanol-hydrochloric acid extraction (within-assay CV, 7%) (12). Lean body mass was measured by bioelectrical impedance (Holtain, UK).

Measurements of leucine and glucose metabolism were calculated using standard isotope dilution equations for steady state conditions (13). The leucine production rate (Ra; a measure of protein degradation) was calculated using {alpha}KIC enrichment rather than plasma leucine enrichment, as it has been shown to give a better estimate of the intracellular enrichment of leucine (14). Leucine and glucose MCR were calculated as: MCR = Rd/plasma concentration, where Rd (rate of disappearance) = Ra, since subjects were studied in steady state.

The nonoxidative leucine disappearance rate (NOLD; a measure of protein synthesis) was calculated as the difference between the leucine production rate and the oxidation rate. The relative proportion of leucine cleared into the oxidative pathway and the protein synthetic path was determined by dividing the relevant flux by the plasma leucine concentration.

Results are expressed as the mean ± SEM. Statistical analysis was performed using one-way ANOVA and Fisher’s least squares difference test. P < 0.05 was taken as showing a significant difference.


   Results
Top
 Abstract
 Introduction
 Subjects and Methods
 Results
Discussion
 References
 
GH treatment was tolerated by all patients except patient 3, in whom treatment was stopped due to fluid retention. Measurements of plasma IGF-I, insulin, C peptide, and glucose concentrations are shown in Fig. 1Go. Before treatment, the fasting total IGF-I concentration was within the normal range in all patients (31–40 yr old, 12.8–62.2 nmol/L; 41–60 yr old, 11.0–43.9 nmol/L; >60 yr old, 3.7–32.9 nmol/L).



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  		Figure 1. Plasma IGF-I, insulin, C peptide, and glucose concentrations in patients with Cushing’s syndrome before (0) and after 2 and 7 days of GH administration. +, P < 0.05; ++, P < 0.005; **, P < 0.001 (significantly different from day 0).

 
Insulin, C peptide, and IGF-I were significantly increased after 2 days (P < 0.005, P < 0.01, and P < 0.001) and 7 days (P < 0.001, P < 0.005, and P < 0.001, respectively) of GH treatment (Fig. 1Go). The side-effects of GH treatment in patient 3 could not be explained in terms of increased sensitivity to GH, as IGF-I levels were similar to those in the other patients after 2 days of GH treatment. Mean plasma glucose concentrations significantly increased after GH treatment for 2 days (P < 0.01) and 7 days (P < 0.005; Fig. 1Go and Table 2Go), and although the mean glucose Ra increased after 7 days of GH treatment, this failed to reach statistical significance. There was no significant change in the glucose MCR, although it fell after 7 days in five of the six patients.


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  		Table 2. Measurements of glucose and leucine metabolism in patients with Cushing’s syndrome after 0, 2, and 7 days of GH treatment

 
Measurements of leucine metabolism are shown in Table 2Go. The mean leucine concentration significantly decreased (P < 0.005) after 2 and 7 days of GH treatment by 26% and 27%, respectively. The leucine MCR increased by 30% and 38% after 2 and 7 days. There was no significant change in leucine Ra, leucine oxidation, or NOLD, but the metabolic clearance of leucine attributable to protein synthesis (NOLD/leucine) was increased by 31% and 41% (P < 0.05) after 2 and 7 days of GH treatment.


   Discussion
Top
 Abstract
 Introduction
 Subjects and Methods
 Results
 Discussion
References
 
This study demonstrated for the first time that GH may be able to counteract the catabolic action of excess endogenous glucocorticoids in patients with Cushing’s syndrome.

Before treatment of the patients with GH, IGF-I levels were within the age-matched normal range, as reported in a previous study (15). Although short term glucocorticoid administration has been shown to stimulate GH secretion, long term glucocorticoid excess has been shown to inhibit spontaneous GH secretion (16) and GH secretion in response to GHRH (17). Hepatic production of IGF-I is dependent on both GH and insulin (18, 19); thus, the diabetogenic action of glucocorticoids with concomitant increased insulin secretion may explain why IGF-I levels remain within the normal range in Cushing’s syndrome in the face of reduced GH secretion. In the present study short term GH administration increased IGF-I significantly, and after 7 days, IGF-I concentrations were just outside the normal range in three of the patients.

There was an increase in fasting glucose, insulin, and C peptide in all patients in response to GH treatment. There was a trend for an increase in glucose Ra and a reduction in glucose MCR, but these did not reach statistical significance; however, they may account for the increase in plasma glucose observed. These effects are in keeping with the known effects of GH on glucose metabolism (20).

The concentration of amino acids, in particular the branched chain amino acids, has been shown to be important in the control of protein synthesis both in vivo (21) and in vitro (22). An acute infusion of IGF-I in man (23) and dogs (24) has been shown to result in a marked decrease in amino acid concentrations due to a decrease in proteolysis, but these studies were unable to demonstrate an effect of IGF-I on protein synthesis. However, when an amino acid clamp technique was used to prevent a decrease in amino acid concentrations, IGF-I was shown to increase protein synthesis (25). In the present study the fasting leucine concentration decreased due to an increase in leucine metabolic clearance in response to GH treatment. Despite the marked fall in the leucine concentration, the rate of protein synthesis was maintained. It is possible that the decrease in the leucine concentration may be due to a change in leucine kinetics in the postprandial state. When the fraction of metabolic clearance of leucine from plasma attributable to protein synthesis was examined, this was found to markedly increase after GH administration. This rise in leucine metabolic clearance demonstrated that GH has an anabolic effect on protein metabolism in these patients mediated through increased efficiency in substrate extraction, possibly indicating an increase in amino acid transport. Inoue and co-workers (26) recently reported a stimulatory effect of GH on amino acid uptake from the human ileum and jejenum consistent with an increase in the number of functional carriers in the brush-border membrane. The increase in leucine MCR observed in the present study may be in keeping with this effect of GH stimulating the availability of amino acid transporters. This might indicate that GH has a role in regulating amino acid transporters, analogous to that of insulin with glucose transporters. These anabolic effects are probably mediated by GH rather than the concomitant rise in insulin, as previous studies have shown insulin to reduce whole body protein breakdown, with no effect on whole body protein synthesis (27, 28).

It has previously been demonstrated that GH has powerful protein anabolic effects in normal subjects and GH-deficient adults (4, 29). GH has been shown to promote positive nitrogen balance in postoperative patients (30), burn and trauma patients (31, 32), and patients with acquired immunodeficiency syndrome (33). There have been no previous studies to determine the effects of GH treatment in patients with Cushing’s syndrome. However, in patients receiving chronic glucocorticoid treatment, GH treatment for 7 days has been shown to increase nitrogen balance (34) and protein synthesis (6), whereas in normal volunteers, GH has been shown to counteract the net catabolic effects of excess glucocorticoids on protein metabolism (5).

This study demonstrated that preoperative GH treatment of patients with Cushing’s syndrome decreased amino acid concentrations and increased the MCR of leucine. The increased clearance of leucine into the protein synthetic pathway provides evidence that GH treatment warrants further investigation as a possible therapeutic agent in Cushing’s syndrome. However, GH treatment was also associated with insulin resistance, as shown by the increases in glucose, insulin, and C peptide concentrations.


   Acknowledgments
 
We thank Dr. A. Weissberger, Dr. F. Shojaee-Moradie, and Miss E. Albany for their assistance with this study. We are grateful to Kabi-Pharmacia for supplying the GH.


   Footnotes
 
1 This work was supported by grants from the Special Trustees of St. Thomas’ Hospital and the Hordern Fund. Back

Received February 29, 1996.

Revised August 23, 1996.

Accepted September 11, 1996.


   References
Top
 Abstract
 Introduction
 Subjects and Methods
 Results
 Discussion
 References
 

  1. Ross EJ, Linch DC. 1982 Cushing’s syndrome–killing disease. Discriminatory values of signs and symptoms aiding early diagnosis. Lancet 2:646–649.
  2. Lamberts SWJ, Birkenhager JC. 1976 Body composition in Cushing’s disease. J Clin Endocrinol Metab. 42:864–868.[Abstract]
  3. Bowes SB, Benn JJ, Scobie IN, Umpleby AM, Lowy C, Sönksen PH. 1993 Leucine metabolism in patients with Cushing’s syndrome before and after successful treatment. Clin Endocrinol (Oxf). 39:591–598.[Medline]
  4. Russell-Jones DL, Weissberger AJ, Bowes SB, et al. 1993 The effects of growth hormone on protein metabolism in growth hormone deficient patients. Clin Endocrinol (Oxf). 38:427–431.[Medline]
  5. Horber FF, Haymond MW. 1990 Human growth hormone prevents the protein catabolic effects of prednisone in humans. J Clin Invest. 86:265–272.
  6. Bennet WM, Haymond MW. 1992 Growth hormone and lean tissue catabolism during long-term glucocorticoid treatment. Clin Endocrinol (Oxf). 36:161–164.[Medline]
  7. Sherwin RS, Shulman GA, Hendler R, Walesky AB, Belous A, Tamborlane W. 1983 Effects of growth hormone on oral glucose tolerance and circulating metabolic fuels in man. Diabetologia. 24:155–161.[Medline]
  8. Ford GC, Cheng KN, Halliday D. 1985 Analysis of 1-13C leucine and 13C KIC in plasma by capillary gas chromatography/mass spectrometry in protein turnover studies. Biomed Mass Spectom. 128:432–436.
  9. Weicko J, Sherman WR. 1976 Boroacetylation of carbohydrates. Correlations between structure and mass spectral behaviour in monoacetylhexose cyclic boronic esters. J Am Chem Soc. 98:7631–7637.[CrossRef]
  10. Sönksen PH. 1976 Double antibody technique for the simultaneous assay of insulin and growth hormone. In: Antoniades H, ed. Hormones in human blood: detection and assay. Cambridge: Harvard University Press; 176–199.
  11. Brooks RV, Dupre J, Gogate AN, Mills IH, Prunty FTG. 1963 Appraisal of adrenocortical hyperfunction: patients with Cushing’s syndrome or non-endocrine tumours. J Clin Endocrinol Metab. 23:725–736.
  12. Teale JD, Marks V. 1990 Inappropriately elevated plasma IGF-II in relation to suppressed IGF-I in the diagnosis of non-islet cell tumour hypoglycaemia. Clin Endocrinol (Oxf). 33:87–98.[Medline]
  13. Matthews DE, Motil KJ, Rohrbaugh DK, Burke JF, Young VR, Bier DM. 1980 Measurements of leucine metabolism in man from a primed continuous infusion of 1-13C leucine. Am J Physiol 238:E473–E479.
  14. Matthews DE, Schwarz HP, Yang RD, Motil KJ, Young VR, Bier DM. 1982 Relationship of plasma leucine and {alpha}-ketoisocaproate during a L-[1-13C]leucine infusion in man: a method for measuring human intracellular leucine tracer environment. Metab Clin Exp. 31:1105–1112.
  15. Bang P, Degerblad M, Thoren M, Schwander J, Blum W, Hall K. 1993 Insulin like growth factor I II and IGF binding protein (IGFBP) 1,2 and 3 in serum from patients with Cushing’s syndrome. Acta Endocrinol (Copenh). 128:397–404.[Medline]
  16. Frantz AG, Rabkin MT. 1964 Human growth hormone, clinical measurement, response to hypoglycaemia and suppression by corticosteroids. N Engl J Med. 271:1375.
  17. Leal-Cerro A, Pumar A, Garcia-Garcia E, Dieguez C, Casanueva FF. 1994 Inhibition of growth hormone release after administration of GHRH and GHRP-6 in patients with Cushing’s syndrome. Clin Endocrinol (Oxf). 41:649–654.[Medline]
  18. Daughaday WH, Phillips LS, Mueller M. 1976 The effects of insulin and GH on the release of somatomedin by the isolated rat liver. Endocrinology. 98:1214–1220.[Abstract]
  19. Böni-Schnetzler M, Schmid C, Meier PJ, Froesch ER. 1991 Insulin regulates insulin-like growth factor I mRNA in rat hepatocytes. Am J Physiol 260:E846–E851.
  20. Sherwin RS, Schulman GA, Hendler R, Walesky M, Belous A, Tamborlane W. 1983 Effect of GH on glucose tolerance and circulating metabolic fuels in man. Diabetologia. 24:155–161.
  21. Castellino P, Luzi L, Simonson DC, Haymond MW, DeFronzo RA. 1987 Effect of insulin and plasma amino acid concentrations on leucine metabolism in man. J Clin Invest. 80:1784–1793.
  22. Loftfield RB, Harris A. 1956 Participation of free amino acids in protein synthesis. J Biol Chem. 219:151–159.[Free Full Text]
  23. Turkalji I, Keller U, Ninnis R, Vosmeer S, Stauffacher W. 1992 Effect of increasing doses of recombinant human insulin-like growth factor-I on glucose, lipid and leucine metabolism in man. J Clin Endocrinol Metab. 75:1186–1191.[Abstract]
  24. Umpleby AM, Shojaee-Moradie F, Thomason MJ, et al. 1994 Effects of insulin-like growth factor-I (IGF-I), insulin and combined IGF-I-insulin infusions on protein metabolism in dogs. J Clin Invest. 24:337–344.
  25. Russell-Jones DL, Umpleby AM, Hennessy TR, et al. 1994 Use of a leucine clamp to demonstrate that IGF-I actively stimulates protein synthesis in normal humans. Am J Physiol 267:E591–E598.
  26. Inoue Y, Copeland EM, Souba WW. 1994 Growth hormone enhances amino acid uptake by the human small intestine. Ann Surg. 219:715–722.[Medline]
  27. Umpleby AM, Boroujerdi MA, Brown PM, Carson ER, Sonksen PH. 1986 The effect of metabolic control on leucine metabolism in type 1 (insulin-dependent) diabetic patients. Diabetologia. 29:131–141.[CrossRef][Medline]
  28. Tessari P, Trevisan R, Inchiostro S, et al. 1986 Dose response curves of effects of insulin on leucine kinetics in humans. Am J Physiol 251:E334–E342.
  29. Fryburg DA, Gefland RA, Barrett EJ. 1991 Growth hormone acutely stimulates forearm muscle protein synthesis in normal humans. Am J Physiol 260:E499–E504.
  30. Lehner JH, Jauch KW, Berger G, Tacke J, Savic B. 1992 A multicentre study of the dose response effect of human recombinant GH on cumulative nitrogen balance in patients after major abdominal surgery. Ann Surg. 208:6–16.
  31. Wilmore DW, Moylan JA, Bristow BF, Mason AD, Pruitt BA. 1974 Anabolic effects of growth hormone and high caloric feedings following thermal injury. Surg Gynecol Obstet. 138:875–884.[Medline]
  32. Ziegler TR, Young LS, Ferrari-Baliviera E, Demlind RH, Wilmore DW. 1990 Use of hGH combined with nutritional support in a critical care unit J Parenter Enteral Nutr. 14:574–581.
  33. Krentz AJ, Koster FT, Crist DM, et al. 1993 Anthropometric, metabolic and immunological effects of recombinant human GH in AIDS and AIDS-related complex. J Acquired Immune Deficiency Syndrome. 6:245–251.
  34. Giustina A, Bussi AR, Jacobello C, Wehrenberg WB. 1995 Effects of recombinant human GH on bone and intermediary metabolism in patients receiving chronic glucocorticoid treatment with suppressed endogenous GH response to GH releasing hormone. J Clin Endocrinol Metab. 80:122–129.[Abstract]



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