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Current IssueEditorial BoardOnline First ArticlesArchive

Research Article

volume 52 issue 6 (june 2018) : 799-804,   Doi: 10.18805/ijar.B-805

Evaluation of b-casein variants in Egyptian goat, sheep and cattle by allele specific PCR and relevance to b- casomorphin

A
Ahmed M. Darwish
G
Ghada H. El Nady
N
Neama I. Ali
A
Aly Z. E. Abdelsalam
1Department of Cell Biology, Genetic Engineering and Biotechnology Division, National Research Centre, 12622, 33 El Bohouth St., Dokki, Giza, Egypt.
Cite article:- Darwish M. Ahmed, Nady El H. Ghada, Ali I. Neama, Abdelsalam E. Z. Aly (2018). Evaluation of b-casein variants in Egyptian goat, sheep and cattle by allele specific PCR and relevance to b- casomorphin. Indian Journal of Animal Research. 52(6): 799-804. doi: 10.18805/ijar.B-805.

ABSTRACT

The beta casein gene (CSNS2) has 12 genetic variants divided into two groups: the first group (A1, B, and G) which differ from the second group (A2, A3 C, D, E, F, H, H2 and I) where A base replaces C base, this leads to potential liberation of a bioactive peptide, b-casomorphin, upon digestion where a histidine replaces a proline at position 67. The allele specific polymerase chain reaction (AS-PCR) was evaluated to distinguish between the beta casomorphin releasing variants (A1 and B) and the non-releasing variants. The sequence analysis was used to determine these variants and confirm it in goat, sheep and cattle. The results showed that cattle carrying allele A1 either homozygous or heterozygous more than sheep and goats. The allele frequency of A1 and A2 is 0.44, 0.56 in goats, 0.43, 0.57 in sheep and 0.54, 0.46 in cattle, respectively. The sequence results reported changing of C base to A base in goat, sheep and cattle. Therefore, this study reported that goat and sheep milk was more safe than cattle milk.    

REFERENCES

  1. Angel, B., Susana, D. and Javier, B. (1999). Technical Note: Use of PCR-Single-Strand Conformation Polymorphism Analysis for Detection of Bovine â-Casein Variants A1, A2, A3, and B. J ANIM SCI, 77:2629-2632. 
  2. Anna, M.C., Salvatore, S., Omar, B. and Eugenio, M. (2016). Detecting beta-casein variation in bovine milk, Molecules, 21: 141, 1-7.
  3. Bell, S.J., Grochoski, G.T. and Clarke, A.J. (2006). Health implications of milk containing beta-casein with the A2 genetic variant. Crit Rev Food Sci Nutr.,46(1):93-100.
  4. Bonsing, J., Ring, J.M., Stewart, A.F. and MacKinlay, A.G. (1988). Complete nucleotide sequence of the bovine â-casein gene. Australian Journal of Biological Sciences,41: 527–537.
  5. Caroli, A.M., Chessa, S. and Erhardt, G.J. (2009). Milk protein polymorphisms in cattle: Effect on animal breeding and human nutrition. J. Dairy Sci., 92: 5335–5352.
  6. Chatchatee, P., Jarvinen, K.M., Bardina, L., Vila, L., Beyer, K. and Sampson H.A. (2001). Identification of IgE and IgG binding epitopes on beta- and kappa-casein on cow’s milk allergic patients. Clin Exp Allergy,31: 1256–1265.
  7. Cieœliñska, A., Kostyra, E., Kostyra, H., Oleñski, K., Fiedorowicz, E. and Kamiñski S. (2012). Milk from cows of different â-casein genotypes as a source of â-casomorphin-7. Int. J. Food Sci. Nutr., 4:426–430.
  8. De Noni, I. and Cattaneo S. (2010). Occurrence of [beta]-casomorphins 5 and 7 in commercial dairy products and in their digests following in vitro simulated gastro-intestinal digestion. Food Chem.,2:560–566.
  9. Elliott, R.B., Wasmuth, H.E., Bibby, N.J. and Hill, J.P. (1997). The role of â-casein variants in the induction of insulin-dependent diabetes in the non-obese diabetic mouse and humans. International Dairy Federation, Brussels, 445-453. 
  10. Gobbetti, M., Stepaniak, L., De Angelis, M., Corsetti, A. and Di Cagno, R. (2002). Latent bioactive peptides in milk proteins: proteolytic activation and significance in dairy processing. Crit Rev Food Sci Nutr, 42: 223–239.
  11. Kamiñski, S., Ciesliñska, A. andKostyra E. (2007). Polymorphism of bovine beta-casein and its potential effect on human health. J Appl Genet., 48(3):189-98.
  12. Kuèerová, J., Matìjíèek, A., Jandurová, O.M., Sørensen, P. Nìmcová, E., Štípková, M., Kott, T., Bouška, J. and Frelich, J. (2006). Milk protein genes CSN1S1,CSN2,CSN3,LGB and their relation to genetic values of milk production parameters in Czech Fleckvieh. Czech J. Anim. Sci., 51(6): 241–247.
  13. Laugesen, M. and Elliott, R. (2003). Ischaemic heart disease, Type 1 diabetes, and cow milk A1 beta-casein.N Z Med J., 116(1168):U295.
  14. Martin, P., Szymanowska, M., Zwierzchowski, L. and Leroux, C. (2002). The impact of genetic polymorphisms on the protein composition of ruminant milks. Reprod Nutr Dev., 42:433-459.
  15. Matthew, P.G., Barnett, W.C., McNabb, N.C., Roy, K.B., Woodford, and Andrew, J.C.(2014). Dietary A1 â-casein affects gastrointestinal transit time, dipeptidyl peptidase-4 activity, and inflammatory status relative to A2 â-casein in Wistar rats. International Journal of Food Sciences and Nutrition, 65(6): 720-727.
  16. McLachlan, C.N. (2001). â-casein A1, ischaemic heart disease mortality, and other illnesses.Med Hypoth., 56: 262-272.
  17. Merriman, T.R. (2009). Type 1 diabetes, the A1 milk hypothesis and vitamin D deficiency. Diabetes Res. Clin. Practice, 2:149–156.
  18. Niebuhr, D.W., Li, Y., Cowan, D.N., Weber, N.S., Fisher, J.A., Ford, G.M.and Yolken, R. (2011). Association between bovine casein antibody and new onset schizophrenia among US military personnel. Schizophr Res.,128:51–55.
  19. Rijnkels, M. (2002). Multispecies comparison of the casein gene loci and evolution of casein gene family. J Mammary Gland Biol Neoplasia,7: 327–345.
  20. Sodhi, M., Mukesh, M., Mishra, B.P., Kishore, A., Prakash, B., Kapila, R. and Mclachlan, C. (2012). CNS. â-casein A1, ischaemic heart disease mortality, and other illnesses. Medical Hypoth.,56: 262–272.
  21. Sun, Z., Zhang, Z., Wang, X., Cade, R., Elmer, Z. andFregly, M. (2003). Relation of beta-casomorphin to apnea in sudden infant death syndrome. Peptides,24: 937–943.
  22. Tailford, K.A., Berry, C.L., Thomas, A.C. andCampbell J.H. (2003). A casein variant in cow’s milk is atherogenic. Atherosclerosis,170: 13–19.
  23. Thorsdottir, I., Birgisdottir, B.E., Johannsdottir, I.M. and Harris P. (2000). Different (beta-casein) fractions in Ice-landic versus Scandinavian cow’s milk may influence diabetogenicity of cow’s milk in infancy and explain low incidence of insulin-    dependent dia- betes mellitus in Iceland. Pediatrics,106: 719–724. 
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Indian Journal of Animal Research
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    Research Article

    volume 52 issue 6 (june 2018) : 799-804,   Doi: 10.18805/ijar.B-805

    Evaluation of b-casein variants in Egyptian goat, sheep and cattle by allele specific PCR and relevance to b- casomorphin

    A
    Ahmed M. Darwish
    G
    Ghada H. El Nady
    N
    Neama I. Ali
    A
    Aly Z. E. Abdelsalam
    1Department of Cell Biology, Genetic Engineering and Biotechnology Division, National Research Centre, 12622, 33 El Bohouth St., Dokki, Giza, Egypt.
    Cite article:- Darwish M. Ahmed, Nady El H. Ghada, Ali I. Neama, Abdelsalam E. Z. Aly (2018). Evaluation of b-casein variants in Egyptian goat, sheep and cattle by allele specific PCR and relevance to b- casomorphin. Indian Journal of Animal Research. 52(6): 799-804. doi: 10.18805/ijar.B-805.

    ABSTRACT

    The beta casein gene (CSNS2) has 12 genetic variants divided into two groups: the first group (A1, B, and G) which differ from the second group (A2, A3 C, D, E, F, H, H2 and I) where A base replaces C base, this leads to potential liberation of a bioactive peptide, b-casomorphin, upon digestion where a histidine replaces a proline at position 67. The allele specific polymerase chain reaction (AS-PCR) was evaluated to distinguish between the beta casomorphin releasing variants (A1 and B) and the non-releasing variants. The sequence analysis was used to determine these variants and confirm it in goat, sheep and cattle. The results showed that cattle carrying allele A1 either homozygous or heterozygous more than sheep and goats. The allele frequency of A1 and A2 is 0.44, 0.56 in goats, 0.43, 0.57 in sheep and 0.54, 0.46 in cattle, respectively. The sequence results reported changing of C base to A base in goat, sheep and cattle. Therefore, this study reported that goat and sheep milk was more safe than cattle milk.    

    REFERENCES

    1. Angel, B., Susana, D. and Javier, B. (1999). Technical Note: Use of PCR-Single-Strand Conformation Polymorphism Analysis for Detection of Bovine â-Casein Variants A1, A2, A3, and B. J ANIM SCI, 77:2629-2632. 
    2. Anna, M.C., Salvatore, S., Omar, B. and Eugenio, M. (2016). Detecting beta-casein variation in bovine milk, Molecules, 21: 141, 1-7.
    3. Bell, S.J., Grochoski, G.T. and Clarke, A.J. (2006). Health implications of milk containing beta-casein with the A2 genetic variant. Crit Rev Food Sci Nutr.,46(1):93-100.
    4. Bonsing, J., Ring, J.M., Stewart, A.F. and MacKinlay, A.G. (1988). Complete nucleotide sequence of the bovine â-casein gene. Australian Journal of Biological Sciences,41: 527–537.
    5. Caroli, A.M., Chessa, S. and Erhardt, G.J. (2009). Milk protein polymorphisms in cattle: Effect on animal breeding and human nutrition. J. Dairy Sci., 92: 5335–5352.
    6. Chatchatee, P., Jarvinen, K.M., Bardina, L., Vila, L., Beyer, K. and Sampson H.A. (2001). Identification of IgE and IgG binding epitopes on beta- and kappa-casein on cow’s milk allergic patients. Clin Exp Allergy,31: 1256–1265.
    7. Cieœliñska, A., Kostyra, E., Kostyra, H., Oleñski, K., Fiedorowicz, E. and Kamiñski S. (2012). Milk from cows of different â-casein genotypes as a source of â-casomorphin-7. Int. J. Food Sci. Nutr., 4:426–430.
    8. De Noni, I. and Cattaneo S. (2010). Occurrence of [beta]-casomorphins 5 and 7 in commercial dairy products and in their digests following in vitro simulated gastro-intestinal digestion. Food Chem.,2:560–566.
    9. Elliott, R.B., Wasmuth, H.E., Bibby, N.J. and Hill, J.P. (1997). The role of â-casein variants in the induction of insulin-dependent diabetes in the non-obese diabetic mouse and humans. International Dairy Federation, Brussels, 445-453. 
    10. Gobbetti, M., Stepaniak, L., De Angelis, M., Corsetti, A. and Di Cagno, R. (2002). Latent bioactive peptides in milk proteins: proteolytic activation and significance in dairy processing. Crit Rev Food Sci Nutr, 42: 223–239.
    11. Kamiñski, S., Ciesliñska, A. andKostyra E. (2007). Polymorphism of bovine beta-casein and its potential effect on human health. J Appl Genet., 48(3):189-98.
    12. Kuèerová, J., Matìjíèek, A., Jandurová, O.M., Sørensen, P. Nìmcová, E., Štípková, M., Kott, T., Bouška, J. and Frelich, J. (2006). Milk protein genes CSN1S1,CSN2,CSN3,LGB and their relation to genetic values of milk production parameters in Czech Fleckvieh. Czech J. Anim. Sci., 51(6): 241–247.
    13. Laugesen, M. and Elliott, R. (2003). Ischaemic heart disease, Type 1 diabetes, and cow milk A1 beta-casein.N Z Med J., 116(1168):U295.
    14. Martin, P., Szymanowska, M., Zwierzchowski, L. and Leroux, C. (2002). The impact of genetic polymorphisms on the protein composition of ruminant milks. Reprod Nutr Dev., 42:433-459.
    15. Matthew, P.G., Barnett, W.C., McNabb, N.C., Roy, K.B., Woodford, and Andrew, J.C.(2014). Dietary A1 â-casein affects gastrointestinal transit time, dipeptidyl peptidase-4 activity, and inflammatory status relative to A2 â-casein in Wistar rats. International Journal of Food Sciences and Nutrition, 65(6): 720-727.
    16. McLachlan, C.N. (2001). â-casein A1, ischaemic heart disease mortality, and other illnesses.Med Hypoth., 56: 262-272.
    17. Merriman, T.R. (2009). Type 1 diabetes, the A1 milk hypothesis and vitamin D deficiency. Diabetes Res. Clin. Practice, 2:149–156.
    18. Niebuhr, D.W., Li, Y., Cowan, D.N., Weber, N.S., Fisher, J.A., Ford, G.M.and Yolken, R. (2011). Association between bovine casein antibody and new onset schizophrenia among US military personnel. Schizophr Res.,128:51–55.
    19. Rijnkels, M. (2002). Multispecies comparison of the casein gene loci and evolution of casein gene family. J Mammary Gland Biol Neoplasia,7: 327–345.
    20. Sodhi, M., Mukesh, M., Mishra, B.P., Kishore, A., Prakash, B., Kapila, R. and Mclachlan, C. (2012). CNS. â-casein A1, ischaemic heart disease mortality, and other illnesses. Medical Hypoth.,56: 262–272.
    21. Sun, Z., Zhang, Z., Wang, X., Cade, R., Elmer, Z. andFregly, M. (2003). Relation of beta-casomorphin to apnea in sudden infant death syndrome. Peptides,24: 937–943.
    22. Tailford, K.A., Berry, C.L., Thomas, A.C. andCampbell J.H. (2003). A casein variant in cow’s milk is atherogenic. Atherosclerosis,170: 13–19.
    23. Thorsdottir, I., Birgisdottir, B.E., Johannsdottir, I.M. and Harris P. (2000). Different (beta-casein) fractions in Ice-landic versus Scandinavian cow’s milk may influence diabetogenicity of cow’s milk in infancy and explain low incidence of insulin-    dependent dia- betes mellitus in Iceland. Pediatrics,106: 719–724. 
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