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Original Studies |
Departments of Surgery (M.A.M., P.J.G., C.H.L.) and Medicine (R.A.F., K.A.D., R.T.S., J.F., M.G.) at the State University of New York at Stony Brook, Stony Brook, New York 11794
Address all correspondence and requests for reprints to: Margaret McNurlan, Department of Surgery, Health Science Center T19, State University of New York at Stony Brook, Stony Brook, New York 11794-8191. E-mail: mcnurlan{at}surg.som.sunysb.edu
Loss of lean tissue often accompanies human immunodeficiency virus (HIV) infection. Exogenous human recombinant GH (hrGH) has been shown to be beneficial in reversing this wasting. However, catabolic effects of hrGH on muscle protein metabolism have also been reported. Therefore, the responsiveness of other GH-sensitive tissues, including bone formation and albumin synthesis, has been examined.
Anabolic activity in bone, from serum levels of carboxy-terminal propeptide of type I collagen, was stimulated by 2 weeks of hrGH in controls (56 ± 15%, P = 0.002), patients with asymptomatic HIV (24 ± 10%, not significant), patients with AIDS (47 ± 7%, P < 0.001), and patients with AIDS and >10% weight loss (21 ± 12%, P = 0.02). Albumin synthesis, determined from the incorporation of L-[2H5]phenylalanine, was increased in response to hrGH in controls (23 ± 7%, P < 0.05), HIV+ subjects (39 ± 16%, P < 0.05), and patients with AIDS (25 ± 7%, P < 0.01). Patients with AIDS and weight loss, however, did not increase albumin synthesis (-0.6 ± 12%) in response to hrGH.
The results indicate variable anabolic responses to hrGH. Bone collagen synthesis remained sensitive to hrGH, whereas, the anabolic action of hrGH on the synthesis of albumin diminished with severity of disease. However unlike muscle protein synthesis, albumin synthesis was not depressed below basal levels by hrGH.
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