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Immunocompetence in relation to a heat-processed diet (Maillard reaction) in weanling rats

Published online by Cambridge University Press:  09 March 2007

Pilar Varela ,
María Del Mar Arce ,
Ascensión Marcos  and
Ana María Castrillón
Pilar Varela
Affiliation:
Instituto de Nutrición y Bromatología (CSIC), Facultad de Farmacia, Universidad Complutense, Ciudad Universitaria, 28040 Madrid, Spain
María Del Mar Arce
Affiliation:
Instituto de Nutrición y Bromatología (CSIC), Facultad de Farmacia, Universidad Complutense, Ciudad Universitaria, 28040 Madrid, Spain
Ascensión Marcos
Affiliation:
Instituto de Nutrición y Bromatología (CSIC), Facultad de Farmacia, Universidad Complutense, Ciudad Universitaria, 28040 Madrid, Spain
Ana María Castrillón
Affiliation:
Instituto de Nutrición y Bromatología (CSIC), Facultad de Farmacia, Universidad Complutense, Ciudad Universitaria, 28040 Madrid, Spain
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Abstract

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Diets containing unheated casein (CD; control) or a casein-glucose mixture (CGD) previously heated at 140° for 2 h were fed to two groups of young rats for 21 d. Differences in body weight, feed consumption, thymus and spleen growth, protein metabolism and in vivo immune response were then determined. For this last experiment, animals were inoculated with sheep erythrocytes (SRBC) on day 15 to provide an immunological challenge. No changes were seen in body weight, feed consumption or feed conversion ratios. Neither were significant differences found in spleen weight, protein content, DNA content, DNase (EC 3.1.4.6) activity or lymphocyte count, suggesting that spleen cell growth remained similar in all the animals studied. The CGD induced marked increases in thymus DNA content whilst the protein:DNA ratio became lower. Spleen RNA content was similar in all rats, but thymus RNA content was 29% lower in the CGD group, although this difference did not reach statistical significance. This fact might be a consequence of the low RNase (EC 2.7.7.16) activity and RNase:RNA ratios in the thymus glands of CGD-fed animals. Further, the number of splenic plasma cells secreting anti-SRBC antibodies (direct plaque-forming cells) was significantly decreased in the same group. It might be concluded that both diets are adequate for rat growth and that the differences observed in the thymus of CGD-fed rats may be directed towards preserving tissue function. Nevertheless, the CGD did cause immunological disturbances affecting the humoral immune response.

Keywords

Heat-processed dietMaillard reactionImmunocompetenceThymusSpleen
Type
General Nutrition
Information
British Journal of Nutrition , Volume 77 , Issue 6 , June 1997 , pp. 947 - 956
Copyright
Copyright © The Nutrition Society 1997

References

REFERENCES

Adrian, J. (1974). Nutritional and physiological consequences of the Maillard reaction. In World Reviews of Nutrition and Dietetics, vol. 19, pp. 71–122 [Boume, G. H., editor]. Basel: S. Karger.Google Scholar
Bell, R. G., Hazell, L. A. & Price, P. (1976). Influence of dietary protein restriction on immune competence. II. Effect of lymphoid tissue. Clinical and Experimental Immunology 26, 314–319.Google ScholarPubMed
BMDP (1992). BMDP Statistical Software, release 7. Los Angeles: California University.Google Scholar
Boswell, H. S., Nerenberg, M. I., Scher, I. & Singer, A. (1980). Role of accessory cells in B cell activation. Journal of Experimental Medicine 152, 1194–1209.Google Scholar
Bounous, G. & Kongshavn, P. A. L. (1985). Differential effect of dietary protein type on the B-cell and T-cell immune responses in mice. Journal of Nutrition 115, 1403–1408.CrossRefGoogle ScholarPubMed
Burton, K. (1956). A study of the conditions and mechanism of the diphenylamine reaction for the colorimetric estimation of deoxyribonucleic acid. Biochemical Journal 62, 315–323.Google Scholar
Chandra, R. K. (1992). The fist INIG Award Lecture. Nutrition and immunology: experience of an old traveller and recent observations. In Nutrition and Immunology, pp. 9–43 [Chandra, R. K., editor]. St. John's, Newfoundland: ARTS Biomedical Publishers and Distributors.Google Scholar
Conzen, S. D. & Janeway, C. A. (1988). Defective antigen presentation in chronically protein-deprived mice. Immunology 63, 683–689.Google ScholarPubMed
Cunningham, A. J. & Szenberg, A. (1968). Further improvements in the plaque technique for detecting single antibody forming cells. Immunology 14, 599–601.Google ScholarPubMed
Finot, P. A. (1990). Metabolism and physiological effects of Maillard reaction products (MRP). In The Maillard Reaction in Food Processing, Human Nutrition and Physiology, pp. 259–272 [Finot, P. A., Aeschbacher, H. U., Hurrell, R. F. and Liardon, R., editors]. Basel: Birkhäuser Verlag.Google Scholar
Friedman, M., Gumbmann, M. R. & Masters, P. M. (1984). Protein-alkali reaction: chemistry, toxicology, and nutritional consequences. In Nutritional and Toxicological Aspects of Food Safety, pp. 367–411 [Friedman, M., editor]. New York: Plenum Press.CrossRefGoogle Scholar
Gershwin, M. E., Beach, R. S. & Hurley, L. S. (1985). Nutrition and Immunity. London: Academic Press.Google Scholar
Hudson, L. & Hay, F. C. (1989). Practical Immunology. Oxford: Blackwell Scientific Publications.Google Scholar
Hurrell, R. F. (1990). Influence of the Maillard reaction on the nutritional value of foods. In The Maillard Reaction in Food Processing, Human Nutrition and Physiology, pp. 245–258 [Finot, P. A., Aeschbacher, H. U., Hurrell, R. F. and Liardon, R., editors]. Basel: Birkhäuser Verlag.Google Scholar
Hurrell, R. F., Finot, P. A. & Ford, J. E. (1983). Storage of milk powders under adverse conditions. 1. Losses of lysine and other essential amino acids. British Journal of Nutrition 49, 343–354.Google Scholar
Kalnitsky, G., Hummel, J. P., Resnick, H., Carter, J. R., Barnett, L. B. & Dierks, C. (1959). The relation of structure to enzymatic activity in ribonuclease. Annals of the New York Academy of Sciences 81, 542–566.Google Scholar
Kenney, M. A., Roderuck, C. E., Amrich, L. & Piedad, F. (1968). Effect of protein deficiency on the spleen and antibody formation in rats. Journal of Biological Chemistry 92, 623–629.Google Scholar
Kimiagar, M., Lee, T. C. & Chichester, C. O. (1980). Long-term feeding effects of browned egg albumin to rats. Journal of Agricultural and Food Chemistry 28, 150–155.CrossRefGoogle ScholarPubMed
McDonald, M. R. (1955). Methods in Enzymology, vol. 2. New York: Academic Press.Google Scholar
Martinez, J. A., Macarulla, M. T., Marcos, R. & Larralde, J. (1992). Nutritional outcome and immunocompetence in mice fed on a diet containing raw field beans (Vicia faba, var. minor) as the source of protein. British Journal of Nutrition 68, 493–503.CrossRefGoogle Scholar
Matsuda, T., Ishiguro, H., Okubo, I., Sasaki, M. & Nakamura, R. (1990). Immunodominancy and antigenic structure of lactose-protein Maillard adduct. In The Maillard Reaction in Food Processing, Human Nutrition and Physiology, pp. 297–302 [Finot, P. A., Aeschbacher, H. U., Hurrell, R. F. and Liardon, R., editors]. Basel: Birkhäuser Verlag.Google Scholar
Metcalfe, D. D. (1985). Food allergens. Clinical Reviews of Allergy 3, 331–349.Google Scholar
Muñoz, E., Marcos, A. & Unzaga, M. T. (1981). Effect of protein on the lysosomal enzyme activities of the spleen and thymus of weanling rats. Journal of Nutrition 111, 2133–2141.Google Scholar
Munro, H. N. & Fleck, A. (1966). Recent developments in the measurement of nucleic acids in biological material. Analyst 91, 78–88.CrossRefGoogle Scholar
National Academy of Sciences (1978). Nutrient Requirements of Laboratory Animals, 3rd ed. Washington, DC: National Academy of Sciences.Google Scholar
Öste, R. E., Brandon, D. L., Bates, A. & Friedman, M. (1990). Antibody-binding to a Maillard-reacted protein. In The Maillard Reaction in Food Processing, Human Nutrition and Physiology, pp. 303–308 [Finot, P. A., Aeschbacher, H.U., Hurrell, R. F. and Liardon, R., editors]. Basel: Birkhäuser Verlag.CrossRefGoogle Scholar
Petro, T. M. & Bhattacharjee, J. K. (1981). Effect of dietary essential amino acid limitations upon the susceptibility to Salmonella typhimurium and the effect upon humoral and cellular immune responses in mice. Infection and Immunity 32, 251–257.CrossRefGoogle ScholarPubMed
Said, A. K., Hegsted, D. M. & Hayes, K. C. (1974). Response of adult rats to deficiencies of different essential amino acids. British Journal of Nutrition 31, 47–57.CrossRefGoogle ScholarPubMed
Srivastava, U., Spach, C. & Aschkenasy, A. (1975). Cyclic AMP metabolism and nucleic acid content in the lymphocytes of the thymus, spleen and lymph nodes of protein-deficient rats. Journal of Nubition 105, 924–928.Google ScholarPubMed
Statistical Analysis Systems Institute Inc. (1989). SAS/STAT User's Guide, version 6, 4th ed., vol. 1, 2. Cary, NC: SAS Institute Inc.Google Scholar
Stoltzner, G. H. & Dorsey, B. A. (1980). Life-long dietary protein restriction and immune function: responses to mitogens and sheep erythrocytes in BALB/c mice. American Journal of Clinical Nutrition 33, 1264–1271.CrossRefGoogle ScholarPubMed
Takata, K., Horiuchi, S., Araki, N., Shiga, M., Saitoh, M. & Morino, Y. (1988). Endocytic uptake of nonenzymatically glycosylated proteins is mediated by a scavenger receptor for aldehyde-modified proteins. Journal of Biological Chemistry 263, 14819–14825.Google Scholar
Vlassara, H., Brownlee, M. & Cerami, A. (1985). High-affinity-receptor-mediated uptake and degradation of glucose-modified proteins: a potential mechanism for the removal of senescent macromolecules. Proceedings of the National Academy of Sciences, USA 82, 5588–5592.CrossRefGoogle ScholarPubMed
Weichselbaum, T. E. (1946). An accurate and rapid method for the determination of proteins in small amounts of blood serum and plasma. American Journal of Clinical Pathology 16, 40–49.Google Scholar
Woodward, B. D. & Miller, R. G. (1991). Depression of thymus-dependent immunity in wasting protein-energy malnutrition does not depend on an altered ratio of helper (CD4+) to suppressor (CD8+) T cells or a disproportionately large atrophy of T-cell relative to the B-cell pool. American Journal of Clinical Nutrition 53, 1329–1335.CrossRefGoogle ScholarPubMed
Woodward, B. D., Woods, J. W. & Crouch, D. A. (1992). Direct evidence that primary acquired cell-mediated immunity is less resistant than is primary thymus-dependent humoral immunity to the depressive influence of wasting protein-energy malnutrition in weanling mice. American Journal of Clinical Nutrition 55, 1180–1185.CrossRefGoogle Scholar