Pharmacokinetics and Tissue Distribution of Recombinant Bovine Somatotropin after Subcutaneous Administarion in Male and Female Rats

Recombinant Bovine Somatotropin의 피하주사 후 Male과 Female Rat에서 약물동태 및 조직분포

  • Park, Byung-kwon (College of Veterinary Medicine, Chungnam National University) ;
  • Park, Seung-chun (College of Veterinary Medicine, Kyungpook National University) ;
  • Yun, Hyo-in (College of Veterinary Medicine, Chungnam National University)
  • Accepted : 2003.05.28
  • Published : 2003.06.30

Abstract

The purpose of this study is to investigate the pharmacokinetics and tissue distribution of recombinant bovine somatotropin (rBST) after subcutaneous adminstration of $^{125}I-rBST$ in male and female rats. A solid state conjugation (Iodo-bead$^{(R)}$) method was confirmed useful for producing $^{125}I-rBST$ because the administration of the conjugated form enabled enough to determine time- concentration relationships of rBST in rats. Subcuatenous administrations showed sex differences that female ($t_{1/2,kc}$, 2.87 h) revealed rapid elimination as compared to male ($t_{1/2,ke}$, 4.81 h), with the absorption ($t_{1/2,ka}$ in male being 0.3 h and that in female 0.75 h) in the reverse order. For subcutaneous administration of rBST in male rats, the liver was the highest in amount, followed by kidney, testes, muscle, and stomach, at the slaughtering tame of 1, 6, 12 and 24 h. But the testes was the highest at the 48 h slaughtered animals, followed by liver, kidney, stomach, and muscle. In slaughtered females at 1, 6, and 12 h after the administration of rBST, the liver was the highest, followed by ovary, kidney, small intestine, and stomach. At 24 and 48 h slaughtered female rats, the ovary was the highest, the liver the second, and the kidney the third.

Keywords

References

  1. 송창우, 황화선, 한상섭. SD 랫드의 주령에 따른 기초연구: I. 체중변화, 혈액·혈액생화학적 변화 및 뇨분석. 한국실험동물학회지.1990, 6, 33-43
  2. 신종서, 김종복, 성경일, 여인서, 김기은, 박연수, 홍병주. 고품질 쇠고기 생산을 위한 한우 사육기술. 1. 소 성장호르몬과 알코을 발효사료의 처리가 증체율, 사료효율, 혈액성상, 육조성 및 도체등급에 미치는 영향. 한영사지. 1994a, 18(5), 363
  3. 신종서, 김종복, 성경일, 여인서, 김기은, 홍병주. 고품질 쇠고기 생산을 위한 한우사육기술. 2. 소 성장호르몬과 알콜발효사료의 처리가 도체품질 및 조성에 미치는 영향. 한영사지. 1994b, 18(5), 373
  4. 심태수. 서방형 Recombinant Bovine Somatotropin 투여수준이 젖소의 산유량, 유성분, 혈액성분 및 수익성에 미치는 영향. 강원대학교. 석사학위논문. 1995
  5. 이영순. 실험동물의학. 서울대학교 출판부. 1995, 408-420
  6. 홍병주, 정지원, 성경일, 여인서, 김종복, 이병건, 장병선. Recombinant Bovine Somatotropin 투여가 한우의 성장 및 도체품질에 미치는 영향. Kor. J. Anim. Sci. 1993, 35(2), 91
  7. Anthony, N. B., Vasilatos-Younken, R., Emmerson, D. A, Nestor K. E. and Bacon. W. L Rattern of growth and plasma growth hormone secretion in turkeys selected for increased egg production. Poult. Sci. 1990, 69(12), 2057-2063
  8. Annexstad, R. J., Otterby, D. E., Linn, J. G., Hansen, W. P., Soderholm, C G. and Wheaton, J. E. Somatotropin treatment for a second consecutive lactation. J. Dairy Sci. 1990, 73, 2423
  9. Baumann, D. E., Peel, C. J., Steinbour, W. D., Reynold, P. J., Tyrrell, H. F., Brown, A. C. G. and Haaland, G. L. Effect of bovine somatotropin on metabolism of lactating dairy cow: influence on ratio of irreversible loss and oxidation of glucose and nonesterified fatty acids. J. Nutr. 1988, 118(32), 1031
  10. Baxter, R. C. Measurement of growth hormone and prolactin receptor turnover in rat liver. Endocrinol 1985, 117, 650-655
  11. Bradford, M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 721, 248-254
  12. Brown-Borg, H. M., Klemcke, H. G., Borg, K. E. and Klint, J. Prolactin and growth hormone clearance in neonatal boais. J. Anim. Sci. 1993, 71, 2055-2060
  13. Carr, D. and Friesen, H. G. Growth hormone and insulin binding to human liver. J. Clin. Endocrinol Metab. 1976, 2, 484-493
  14. Colby, H. D. Regulation of hepatic drug and steroidal metabolism by androgens and estrogens. hi Advances in sex hormone research. Vol. 4, eds Thomas, J.A. and Singhai, R.L. Urban and Schwarzenberg, Baltimore-Munich. 1980, 27-29
  15. Craig, M. Z., Holly, W. S. and Peter, H. B. Rapid and sensitive ELISA method for the determiantion of bovine somatotropin in blood and milk. J. Agricul. Food Chem. 1990, 38, 1358-1362
  16. David, H. N-Chloroacetyl-[$^{125}I$]Iodotyramine: An alkylating agent with high Specific Activity. Analy Biochem. 1981, 117, 390-397
  17. Donoghue, D. J., Campbell, R. M. and Scanes, C. G. Effect of biosynthetic chicken growth hormone on egg production in White Leghorn hens. Poult. Sci. 1990, 69, 1818-1821
  18. Downer, J. V., Patterson, D. L. and Rock, D. W. Dose titration of sustained-release recombinat bovine somatotropin in lactating daily cows. J. Dairy Sci. 1993, 76, 1125-1136
  19. Early, R. J., Mcbride, B. W. and Ball, R. 0. Growth and metabolism in somatotropin-treated steer: 1. growth, serum chemistry and carcass weights. J. Anim. Sci. 1990a, 68, 4134- 4143
  20. Early, R. J., Mcbride, B. W. and Ball, R. 0. Growth and metabolism in samatatropin-treated steer: 2. Carcass and noncarcass tissue components and chemical composition. J. Anim Sci. 1990b, 68, 4144-4152
  21. George, P., Tuszynski, L. C., Knight, E. K. and Srivastava, S. Labelling of platelet surface proteins with $^{125}I$ by the iodogen method. Anal. Biochem. 1983, 130, 166-170
  22. Gilman, A. G., Rall, T. W., Nies, A. S. and Taylor, P. (ed), The Phamiacological Basis of Therapeutics, 8th edition, Pergman, New York, 1995, 1364-1368
  23. Gluckman, P. D., Butler, J. H. and Elliott, T. B. The ontogeny of somatotropic binding sites in ovine hepatic membranes. Endocrinol. 1983, 112, 1607-1612
  24. Greenwood, F. C., Hunetr, W. M. and Glouer, J. S. The preparation of $^{131}I$-labeled human growth of high specific radioactivity. Biochem. J. 1962, 89, 114
  25. Hunter, W. M. and Greenwood, F. C. Radioimmunoelectrophoretic assay for human growth hormone. Nature. 1962, 194, 495
  26. Johnson-Berling, B. M. and Ohlssen, K. Distribution and elimination of intravenously injected urinary trypsin inhibitor. Scand. J. Clin Lab. Invest. 1991, 51, 549-557
  27. Kathleen, H. S. and Willinams, R. P. Use of iodogen and $^{125}I$ to label the outer membrane proteins of whole cells of Neisseria gonorrhoeae. Anal. Biochem. 1982, 120, 254-258
  28. Kimura, T., Matsueda, R., Nakagawa, Y. and Kaiser, E. T. New reagents for the introduction of thiomethyl group at sulfhydiyl residues of proteins with concominant spectrophotometric titration of the sulfhydryls: methyl 3-nitro-2-pyridy1 disulfide and methyl 2-pyridy1 disulfide. Anal. Biochem. 1982, 122, 274-282
  29. Kornecki, E, Davis, T. B. and Ehrlich, Y. H. lodination of membrane surface proteins of neuroblastoma $\times$ glioma cell. Abstract presented of the American Society of Neurochemistry, The llth Annual Meeting, March. 12-16, 1984
  30. Lotan, E, Sturman, H, and Weller, J. I. Effects of recombination bovine somatotropin under conditions of high production and heat stress. J. Dairy Sci. 1993, 76, 1394-1402
  31. Marchalonis, J. J. Enzymic method for the trace iodination of immunoglobulins and other proteins. Biochem. J. 1969, 113, 299
  32. Markwell, M. A. K. A new solid-state reagent to iodinate proteins: conditions for the efficient labelling of antiserm. Anal. Biochem. 1982, 125, 427-432
  33. McLaughlin, C. L., Byatt, J. C., Hedrick, H. B., Veenhuizen, J. J., Curran, D. F., Hintz, R. L., Hartnell, G. F., Kasser, T. R., Collier, R. J. and Baile, C A. Performance, clinical chemistry, and carcass responses of finishing lambs to recombinant bovine somatotropin and bovine placental and bovine placental lactogen. J. Dairy Sci. 1993, 71, 3307-3318
  34. Munson, P. L. Principles of Pharmacology. Chapman & Hall Co., 1995, 897-905
  35. Pell, A. N., Tsang, D. S., Howlett, B. A., Huyler, M. T., Meserole, V. K., Samuels, W. A., Hartnell, G. F. and Hintz, R. L. Effects of a prolonged-release formulation of sometribove (n-methionyl bovine somatotropin) on Jersey cows. J. Dairy Sci. 1992, 75, 3416-3431
  36. Purchas, R. W., Macmillan, K. L. and Hafs, H. D. Pitutary and plasma growth hormone levels in bulls from birth to one year of age. J. Anim. Sci. 1970, 31, 358-363
  37. Richrdson, K. and Parker, C. D. Identification and characterization of Vibrio cholerae surface proteins by radioiodination. Infect. Imuun. 1985, 48(1), 87-93
  38. Salacinski, P. R., McLean, C., Sykes, J. E., Clement-Jones, V. V. and Lowry, P. J. lodination of proteins, glycoproteins, and peptides using a solid-phase oxidizing agents, 1,3,4,6- tetrach1oro-3a,6a-dipheny1 glycoluril (lodogen). Anal. Biochem. 1991, 117, 136-146
  39. Shan, S. W. Chemistry of Protein Conjugation and Crosslinking. CRC press, 1993, 49-70
  40. Sinha, Y. N., Baxter, S. R. and Vanderlaan, W. P. Metabolic clearance rate of growth hormone in mice during various physiological states. Endocrinol. 1979, 105, 685-689
  41. Skett, P. Biochemical basis of sex differences in drug metabolism, Pharmacology and Therapeutics. 1988, 38, 269-304
  42. Stegman, J. J. and Chevion, M. Sex differences in cytochrome P-450 and mixed function oxygenase activity in gonadally mature trout. Biochem. Pharmacol. 1980, 29, 553-558
  43. Thean, E. T. Comparison of specific radioactivities of human a-lactalbumin iodinated by three different methods. Anal. Biochem. 1990, 188, 330-334
  44. Toutain, P. L., Schams, D., Laurentie, M. P. and Thomson, T. D. Pharmacokinetics of a recombinant bovine growth hormone and pituitary bovine growth hormone in lactating dairy cows. J. Anim. Sci. 1993, 71, 1219-1225
  45. Trenkle, A. Growth hormone secretion rates in cattle. J. Anim. Sci. 1971, 32, 115-118
  46. Verson, R. D. Relationship of milk yield, clinical mastitis and associated antibiotic use in control and sometribove-treated cows. J. Dairy Sci. 1993, 76, 237