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The effect of phytohaemagglutinin at different dietary concentrations on the growth, body composition and plasma insulin of the rat

Published online by Cambridge University Press:  09 March 2007

S. Bardocz ,
G. Grant ,
A. Pusztai ,
M. F. Franklin  and
A. Def. F. U. Carvalho
S. Bardocz
Affiliation:
Rowett Research Institute, Bucksburn, Aberdeen AB2 9SB
G. Grant
Affiliation:
Rowett Research Institute, Bucksburn, Aberdeen AB2 9SB
A. Pusztai
Affiliation:
Rowett Research Institute, Bucksburn, Aberdeen AB2 9SB
M. F. Franklin
Affiliation:
Biomathematics and Statistics, Scotland; c/oRowett Research Institute, Bucksburn, Aberdeen AB2 9SB
A. Def. F. U. Carvalho
Affiliation:
Department of Biology, Universidade Federal do Ceara, 60,001 Fortaleza (CE), Brasil
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Abstract

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Young growing rats weighing approximately 83g were fed on diets containing kidney bean (Phaseolus vulgaris) lectin (phytohaemagglutinin, PHA) in the range of 0–0.45g/kg body weight for 10d to ascertain whether there was a minimum dose below which the lectin had no significant effect on body and skeletal muscle weights in comparison with pair-fed lectin-free controls. Averaged over all experiments, PHA doses of less than 10 mg/d (0.12 g/kg body weight) reduced body dry weight by 1.14 (SE 0.25) g when compared with controls. Between 10 and 27 mg/d (0.12−0.32 g/kg body weight) a further reduction of 0–64 (SE 0.21)g occurred, suggesting a slight but steady decline of body dry weight with increasing dose. However, above 27 mg/d the depression of growth and changes in body composition accelerated. The difference between the proportional losses of skeletal muscle and body weight was not significant at doses of PHA below 10 mg/d (0.12 g/kg body weight) but the ratio of these losses rose to 1.5–2.0 at doses above this. The proportional decrease in lipid weight exceeded that of both body and skeletal muscle weights at all lectin doses, suggesting that lipid catabolism was the first target of the PHA effect. Plasma insulin level was depressed at the PHA dose of 0.02 g/kg body weight at which growth depression and muscle atrophy were minimal but, contrary to expectations, plasma glucose levels remained stable over the whole PHA dose range. It appears that despite a PHA-induced lowering of blood insulin, glucose catabolism is elevated by an unknown, possibly hormonal, compensatory mechanism. Thus, because low insulin levels facilitate the mobilization and catabolism of lipids, it may be possible to use low doses of PHA to reduce hyperglycaemia and body fat.

Keywords

PhytohaemagglutininPlasmaInsulinMuscleBody composition
Type
General Nutrition
Information
British Journal of Nutrition , Volume 76 , Issue 4 , October 1996 , pp. 613 - 626
Copyright
Copyright © The Nutrition Society 1996

References

REFERENCES

Ashcroft, F.M. & Ashcroft, S.J.H. (1992). Insulin secretion, mechanism of insulin secretion. In Insulin, Molemlar Biology fo Pathology, pp. 97–150 [Ashcroft, F. M. and Ashcroft, S. J. H. editors]. Oxford: IRL Press at Oxford University Press.CrossRefGoogle Scholar
Bardocz, S., Brown, D. S., Grant, G., Pusztai, A., Stewart, J. C. & Palmer, R. M. (1992). Effect of the β-adrenoreceptor agonist clenbuterol and phytohaemagglutinin on growth, protein synthesis and polyamine metabolism of tissues of the rat. British Journal of Pharmcology 106, 476–482.CrossRefGoogle Scholar
Bardocz, S., Ewen, S. W. B. & Pusztai, A. (1993). Binding and endocytosis of Phaseolus vulgaris L4 lectin and insulin by 3T3 and L6 cells - effects on protein synthesis. In Lectins: Biology, Biochemistry, Clinical Biochemistry, pp. 258–264 [Van Driessche, E.Franz, H.Beeckmans, S.Pfüller, U.Kallikorm, A. and Bog-Hansen, T. C. editors]. Hellerup, Denmark: Textop.Google Scholar
Bardocz, S., Grant, G., Ewen, S.W.B., Duguid, T. J.Duguid, T., Brown, D. S., Englyst, K. & Pusztai, A. (1995). Reversible effect of phytohaemagglutinin on the growth and metabolism of rat gastrointestinal tract. Gut 37, 353–360.CrossRefGoogle ScholarPubMed
Bischoff, H. (1994). Pharmacology of α-glucosidase inhibition. European Journal of Clinical Investigation 24, Suppl 3, 3–10.Google ScholarPubMed
Carvalho, A.de, F.F.U. (1992). Dietary kidney bean lectins affect insulin levels, change gene expression and modulate metabolism PhD Thesis, University of Aberdeen.Google Scholar
Cochran, W.G. & Cox, G. M. (1958). Experimental Designs, p. 101. New York: John Wiley and Sons.Google Scholar
Cuetracasas, P. & Teller, G.P.E. (1973). Insulin-like activity of concanavalin A and wheat germ agglutinin: direct interactions with insulin receptors. Proceedings of the National Academy of Sciences, USA 70, 485–489.CrossRefGoogle Scholar
Gould, G. & Bell, G.I. (1990). Facilitative glucose transporters: an expanding family. Trends in Biochemical Science 15, 18–23.CrossRefGoogle ScholarPubMed
Grant, G., de Oliveira, J. T. A., Donvard, P. M., Annand, M. G., Waldron, M. & Pusztai, A. (1987). Metabolic and hormonal changes in rats resulting from consumption of kidney bean (Phaseolus vulgaris) or soyabean (Glycine max). Nutrition Reports International 36, 763–772.Google Scholar
Kilpatrick, D. C., Pusztai, A., Grant, G. & Ewen, S. W. B. (1985). Tomato lectin resists digestion in the mammalian alimentary canal and binds to intestinal villi without deleterious effects. FEBS Letters 185, 299–305.CrossRefGoogle ScholarPubMed
King, T. P., Pusztai, A. & Clarke, E. M. W. (1980). Immunocytochemical localization of ingested kidney bean (Phaseolus vulgaris) lectins in rat gut. Histochemical Journal 12, 201–208.CrossRefGoogle ScholarPubMed
King, T. P., Pusztai, A., Grant, G. & Slater, D. (1986). Immunogold localization of ingested kidney bean (Phaseolus vulgaris) lectins in epithelial cells of the rat small intestine. Histochemical Journal 18, 413–420.CrossRefGoogle ScholarPubMed
Knott, R. M., Grant, G., Bardocz, S., Pusztai, A., Carvalho, A.de, F. F. & Hesketh, J. E. (1992). Alterations in the level of insulin receptor and GLUT-4 mRNA in skeletal muscle from rats fed a kidney bean (Phaseolus vulgaris) diet. International Journal of Biochemistry 24, 897–902.CrossRefGoogle ScholarPubMed
Livingstone, J. N. & Purvis, B. J. (1980). Effects of wheat germ agglutinin on insulin binding and insulin sensitivity of fat cells. American Journal of Physiology 238, E267–E275.Google Scholar
Macrae, J. C., Bruce, L. A., Hovell, F. B.de, B., Hart, I. C., Inkster, J., Walker, A. & Atkinson, T. (1991). Influence of protein nutrition on the response of growing lambs to exogenous bovine growth hormone. Journal of Endocrinology 130, 53–61.CrossRefGoogle ScholarPubMed
Palmer, R. M., Pusztai, A., Bain, P. & Grant, G. (1987). Changes in rates of tissue protein synthesis in rats induced in vivo by consumption of kidney bean lectins. Comparative Biochemistry and Physiology 88C, 179–183.Google Scholar
Pusztai, A. (1989). Transport of proteins through the membranes of the adult gastrointestinal tract - a potential for drug delivery? Advances in Drug Delivery Reviews 3, 215–228.CrossRefGoogle Scholar
Pusztai, A. (1991). Planf Lectins. Cambridge: Cambridge University Press.Google Scholar
Pusztai, A., Grant, G., Duguid, T., Brown, D. S., Peumans, W. J., Van Damme, E. J. M. & Bardocz, S. (1995). Inhibition of starch digestion by α-amylase inhibitor reduces the efficiency of utilization of dietary proteins and lipids and retards the growth of rats. Journal of Nutrition 125, 1554–1562.Google ScholarPubMed
Pusztai, A., Grant, G., Spencer, R. J., Duguid, T. J., Brown, D. S., Ewen, S. W. B., Peumans, W. J., Van Damme, E. J. M. & Bardocz, S. (1993). Kidney bean lectin-induced Escherichia coli overgrowth in the small intestine is blocked by GNA, a mannose-specific lectin. Journal of Applied Bacteriology 75, 360–368.CrossRefGoogle ScholarPubMed
Pusztai, A., Greer, F. & Grant, G. (1989). Specific uptake of dietary lectins into the systemic circulation of rats. Biochemical Society Transactions 17, 481–482.CrossRefGoogle Scholar
Pusztai, A. & Palmer, R. M. (1977). Nutritional evaluation of kidney bean (Phaseolus vulgaris): the toxic principle. Journal of the Science of Food and Agriculture 28, 620–623.CrossRefGoogle Scholar
Pusztai, A. & Watt, W. B. (1974). Isolectins of Phaseolus vulgaris. A comprehensive study of fractionation. Biochimica et Biophysica Acta 365, 57–11.CrossRefGoogle ScholarPubMed
Samols, E., Bonner-Weir, S. &Weir, G. C. (1986). Intra-islet insulin-glucagon-somatostatin relationships. Clinical Endocrinology and Metabolism 15, 33–58.CrossRefGoogle ScholarPubMed
Trinder, P. (1967). Determination of glucose in blood using glucose oxidase with an alternative oxygen acceptor. Annals of Clinical Biochemistry 6, 24–27.CrossRefGoogle Scholar