AJP - Gastrointestinal and Liver Physiology, Vol 254, Issue 3 450-G456, Copyright © 1988 by American Physiological Society

ARTICLES

Regulation of food intake and hepatic protein synthesis by recombinant-derived cytokines

L. L. Moldawer, C. Andersson, J. Gelin and K. G. Lundholm
Department of Surgery I, Sahlgren's Hospital, University of Gothenberg, Sweden.

During inflammation, activated monocytes and lymphocytes synthesize and release many soluble protein mediators, such as interleukin (IL) 1, tumor necrosis factor-alpha, and IL-2. It is presently unclear which cytokines, if any, contribute to the anorexia and hepatic protein changes frequently seen during inflammation. To evaluate their potential role, food intake and liver and plasma protein synthesis were determined in both endotoxin-sensitive C57Bl/6j mice and endotoxin-resistant C3H/HeJ mice given either crude secretory products of Staphylococcus albus-stimulated human blood monocytes or murine recombinant IL-1-alpha, human recombinant IL-1-alpha or -beta, human recombinant tumor necrosis factor-alpha, or human IL-2. When given intraperitoneally to healthy animals, 2,000 lymphocyte-activating factor U/day of secretory products of activated human blood monocytes or recombinant murine IL-1-alpha depressed spontaneous food intake by 42 and 53%, respectively. Human IL-1-alpha and -beta and human tumor necrosis factor-alpha produced smaller reductions in food intake. In contrast, human IL-2, when given in equimolar quantities, had no appreciable effect on food intake or body weight. Administration of crude secretory products of activated blood monocytes, recombinant IL-1, or tumor necrosis factor-alpha increased liver weight, protein, and RNA content. In addition, plasma protein synthesis was significantly increased, as were serum amyloid P concentrations. Administration of recombinant tumor necrosis factor-alpha resulted in IL-1 production by peritoneal adherent cells. However, IL-2 had no effect on any hepatic parameter.

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