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Inhibition of proliferative responses of mouse spleen lymphocytes and rabbit Peyer's patch cells by bovine milk caseins and their digests

Published online by Cambridge University Press:  01 June 2009

Hajime Otani  and
Isao Hata
Hajime Otani
Affiliation:
Laboratory of Applied Biochemistry of Animal Products, Faculty of Agriculture, Shinshu University, Minamiminowa-mura 399–45, Japan
Isao Hata
Affiliation:
Laboratory of Applied Biochemistry of Animal Products, Faculty of Agriculture, Shinshu University, Minamiminowa-mura 399–45, Japan
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Summary

The modulating effect of bovine milk casein components and their digests on the proliferative responses of mouse spleen lymphocytes and rabbit Peyer's patch cells induced or not induced by mitogens has been studied with a colorimetric assay using 3-(4, 5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide. All the casein components and their digests tested had little mitogenic effect on the proliferative responses of mouse spleen lymphocytes and rabbit Peyer's patch cells. Intact κ-casein significantly inhibited the proliferative responses of mouse spleen lymphocytes and Peyer's patch cells induced by mitogens such as lipopolysaccharide from Salmonella typhimurium, concanavalin A, phytohaemagglutinin and pokeweed mitogen. In contrast, intact αsl-casein and β-casein had little effect. κ-Casein had an inhibitory effect after digesti on by pancreatin or trypsin, but not after pepsin or chymotrypsin digestion. Both pancreatin and trypsin digests of αsl-casein and -casein significantly inhibited the proliferative responses of mouse spleen lymphocytes and rabbit Peyer's patch cells induced by mitogens, whereas pepsin and chymotrypsin digests of both caseins were without effect. Moreover, the trypsin digest of each casein component had an inhibitory effect on mouse spleen lymphocyte proliferation in the absence of mitogen. Since trypsin is a major proteinase in pancreatin, the substrate specificity of trypsin seems to be important for the formation of the inhibitory peptides from casein components. These observations suggest that intact κ-casein and some peptides formed from milk casein components by the action of trypsin may suppress the immune responsiveness of neonates.

Type
Original Articles
Information
Journal of Dairy Research , Volume 62 , Issue 2 , May 1995 , pp. 339 - 348
Copyright
Copyright © Proprietors of Journal of Dairy Research 1995

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References

REFERENCES

Agunod, M., Yamaguchi, N., Lopez, R., Luhby, A. L. & Glass, G. B. J. 1969 Correlative study of hydrochloric acid, pepsin, and intrinsic factor secretion in newborns and infants. American Journal of Digestive Diseases 14 400–414.CrossRefGoogle ScholarPubMed
Aschaffenburg, R. 1963 Preparation of β-casein by a modified urea fractionation method. Journal of Dairy Research 30 259–260CrossRefGoogle Scholar
Barrett, A. J. 1986 An introduction to the proteinases. In Proteinase Inhibitors, p. 15 (Eds Dingle, J. T. and Gordon, J. L.). Oxford: Elsevier Science Publishers (Research Monographs in Cell and Tissue Physiology 12)Google Scholar
Bbrkenstam, R., Jagenburg, R. & Mellander, O. 1955 Protein hydrolysis in the stomachs of premature and full-term infants. Acta Paediatrica 44 348–354Google Scholar
Brantl, V. & Teschemacher, H. 1979 A material with opioid activity in bovine milk and milk products. Naunyn-Schmiedeberg's Archives of Pharmacology 306 301–304CrossRefGoogle ScholarPubMed
Coste, M., Rochet, V., LÉOnil, J., MollÉ, D., Bouhallab, S. & Tome, D. 1992 Identification of C-terminal peptides of bovine -casein that enhance proliferation of rat lymphocytes. Immunology Letters 33 41–46CrossRefGoogle ScholarPubMed
Fiat, A. -M. & JollÉs, P. 1989 Caseins of various origins and biologically active casein peptides and oligosaccharides. Structural and physiological aspects. Molecular and Cellular Biochemistry 87 5–30CrossRefGoogle ScholarPubMed
Franoakis, M. V., Koopman, W. J., Kiyono, H., Michalek, S. M. & Mcghee, J. R. 1982 An enzymatic method for preparation of dissociated murine Peyer's patch cells enriched for macrophages. Journal of Immunological Methods 48 33–44CrossRefGoogle Scholar
Johnson, H. M., Smith, E. M., Torres, B. A. & Blalock, J. E. 1982 Regulation of the in vitro antibody response by neuroendocrine hormones. Proceedings of the National Academy of Sciences, USA 79 4171–4174CrossRefGoogle ScholarPubMed
JollÉs, P., LÉVy-Toledano, S., Fiat, A. -M., Soria, C., Gillessen, D., Thomaidis, A., Dunn, F. W. & Caen, J. P. 1986 Analogy between fibrinogen and casein. Effect of an undecapeptide isolated from κ-easein on platelet function. European Journal of Biochemistry 158 379–382CrossRefGoogle ScholarPubMed
JollÉs, P., Parker, F., Floc'h, F., Migliore, D., Alliel, P., Zerial, A. & Werner, G. H. 1981–1982 Immunostimulating substances from human casein. Journal of Immunopharmacology 3 363–369CrossRefGoogle ScholarPubMed
Kawasaki, Y., Isoda, H., Tanimoto, M., Dosako, S., Idota, T. & Ahiko, K. 1992 Inhibition by lactoferrin and κ-easein glycomacropeptide of binding of cholera toxin to its receptor. Bioscience, Biotechnology, and Biochemistry 56 195–198CrossRefGoogle ScholarPubMed
Lowry, O. H., Rosebrough, N. J., Farr, A. L. & Randall, R. J. 1951 Protein measurement with the Folin phenol reagent. Journal of Biological Chemistry 193 265–275CrossRefGoogle ScholarPubMed
Mccain, H. W., Lamster, I. B., Bozzone, J. M. & Grbic, J. T. 1982 β-Endorphin modulates human immune activity via non-opiate receptor mechanisms. Life Sciences 31 1619–1624CrossRefGoogle ScholarPubMed
Maruyama, S., Nakagomi, K., Tomizuka, N. & Suzuki, H. 1985 Angiotensin I-converting enzyme inhibitor derived from an enzymatic hydrolysate of casein. II. Isolation and bradykinin-potentiating activity on the uterus and the ileum of rats. Agricultural and Biological Chemistry 49 1405–1409Google Scholar
Maruyama, S. & Suzuki, H. 1982 A peptide inhibitor of angiotensin I converting enzyme in the tryptic hydrolysate of casein. Agricultural and Biological Chemistry 46 1393–1394Google Scholar
Mathews, P. M., Froelich, C J., Sibbitt, W. L. & Bankhurst, A. D. 1983 Enhancement of natural cytotoxicity by β-endorphin. Journal of Immunology 130 1658–1662CrossRefGoogle ScholarPubMed
Mepham, B. 1975 The Secretion of Milk. London: Edward Arnold (Studies in Biology 60)Google Scholar
Migliore-Samour, D. & JollÉS, P. 1988 Casein, a prohormone with an immunomodulating role for the newborn? Experientia 44 188–193CrossRefGoogle ScholarPubMed
Mosmann, T. 1983 Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays. Journal of Immunological Methods 65 55–63CrossRefGoogle ScholarPubMed
Nakamura, A., Nagai, K., Suzuki, S., Ando, K. & Tamura, G. 1986 A novel method of screening for immunomodulating substances, establishment of an assay system and its application to culture broths of microorganisms. Journal of Antibiotics 39 1148–1154CrossRefGoogle ScholarPubMed
Neeser, J. -R., Chambaz, A., Del Vedovo, S., Prigent, M. -J. & Guggenheim, B. 1988 Specific and nonspecific inhibition of adhesion of oral actinomyces and streptococci to erythrocytes and polystyrene by caseinoglycopeptide derivatives. Infection and Immunity 56 3201–3208CrossRefGoogle ScholarPubMed
Otani, H. 1981 Antigenicities of β-lactoglobulin treated with proteolytic enzymes. Japanese Journal of Zootechnical Science 52 47–52Google Scholar
Otani, H., Higashiyama, S. & Tokita, F. 1984 Studies on the antigenic structure of bovine β-casein II. Antigenic reactivity of γ2-casein with antiserum to β-casein. Milchwissenschaft 39 291–293Google Scholar
Otani, H., Kitoh, M. & Hosono, A. 1990 Preparation and properties of rabbit antisera against cow κ-casein prepared by 3 different procedures. Milchwissenschaft 45 689–693Google Scholar
Otani, H. & Monnai, M. 1993 Inhibition of proliferative responses of mouse spleen lymphocytes by bovine milk κ-casein digests. Food and Agricultural Immunology 5 219–229CrossRefGoogle Scholar
Otani, H., Monnai, M. & Hosono, A. 1992 Bovine κ-casein as inhibitor of the proliferation of mouse splenocytes induced by lipopolysaccharide stimulation. Milchwissenschaft 47 512–515Google Scholar
Otani, H., Takayama, K. & Tokita, F. 1985 Antigenic identity of bovine αs1- and αs1-I caseins. Milchwissenschaft 40 24–26Google Scholar
Parker, F., Migliore-Samour, D., Floc'h, F., Zerial, A., Werner, G. H., JollÉS, J., Casaretto, M., Zahn, H. & JollÉS, P. 1984 Immunostimulating hexapeptide from human casein: amino acid sequence, synthesis and biological properties. European Journal of Biochemistry 145 677–682CrossRefGoogle ScholarPubMed
Shammet, K. M., Brown, R. J. & Mcmahon, D. J. 1992 Proteolytic activity of proteinases on macropeptide isolated from κ-casein. Journal of Dairy Science 75 1380–1388CrossRefGoogle ScholarPubMed
Walsh, K. A. 1970 Trypsinogens and trypsins of various species. Methods in Enzymology 19 4–63Google Scholar
Wilcox, P. E. 1970 Chymotrypsinogens-chymotrypsins. Methods in Enzymology 19 64–108CrossRefGoogle Scholar
Zioudrou, C., Streaty, R. A. & Klee, W. A. 1979 Opioid peptides derived from food proteins. The exorphins. Journal of Biological Chemistry 254 2446–2449CrossRefGoogle ScholarPubMed
Zittle, C. A. & Custer, J. H. 1963 Purification and some of the properties of αs-casein and κ-easein. Journal of Dairy Science 46 1183–1188CrossRefGoogle Scholar