Please use this identifier to cite or link to this item: http://hdl.handle.net/11455/22798
標題: 重組酵母菌產製功能性蛋白質作為豬隻飼料添加物之功能評估
Recombinant Yeast Produced Functional Proteins as the Porcine Feed Additives and their Performance Evaluations
作者: 劉芳爵
Liu, Fang-Chueh
關鍵字: Recombinant Yeast;重組酵母菌;Functional Proteins;Feed Additives;功能性蛋白質;飼料添加物
出版社: 生命科學系所
引用: 臺灣地區養豬飼養標準編輯委員會。1990。臺灣地區飼養標準-豬。臺灣地區養豬飼養標準編輯委員會編印。台北。台灣。 廖宗文、蔡金生、劉建甫、蘇天明。2001。增加畜試黑豬一號母豬懷孕期之飼料餵量對其繁殖性能以及仔豬生長性能之影響。未發表文獻。 蔡金生、劉建甫、李茂盛、陳添福、蘇天明、顏念慈、廖宗文、黃鈺嘉、張秀鑾、 陳義雄、王政騰。2003。畜試黑豬繁殖性能及生長性能之探討。畜產研究 36(4):317–325。 劉芳爵、徐阿里。2000。熱能與離胺酸對台灣黑豬與三品種雜交肉豬生長性能及 屠體性狀之影響。畜產研究 33(2): 165-174。 劉芳爵、徐阿里、嚴世俊、許晉賓。2003。脂肪來源與含量對離乳仔豬生長性能和胰脂肪酶以及胰輔脂肪活性發展之效應。畜產研究36(3): 231- 223。 劉芳爵、李恆夫、許晉賓、嚴世俊、徐阿里。2004。蛋白質與脂肪含量對離乳仔豬生長性能和胰脂肪酶以及胰輔脂肪酶活性發展之效應。畜產研究37(1): 1- 13。 劉芳爵、陳全木。2007。畜試黑豬肌肉生長抑制素互補DNA選殖及其mRNA表現量對新生仔豬出生體重相關性分析。畜產研究40(2):119-128。 劉芳爵、陳全木。2007。添加重組胰輔脂肪酶改善畜試黑豬離乳仔豬之生長性狀與脂肪利用率。畜產研究 40(3):169-175。 Acton, T., K. Gunsalus, R. Xiao, L. Ma, J. Aramini, M. Baran, Y. Chiang, T. Climent, B. Cooper, N. Denissova, S. Douglas, J. Everett, C. Ho, D. Macapagal, P. Rajan, R. Shastry, L. Shih, G. Swapna, M. Wilson, M. Wu, M. Gerstein, M. Inouye, J. Hunt, and G. Montelione. 2005. Robotic cloning and protein production platform of the Northeast Structural Genomics Consortium. Methods Enzymol. 394:210-243. Adamczak,M., A. Wiecek, T. Funahashi, J. Chudek, F. Kokot, and Y. Matsuzawa. 2003. Decreased plasma adiponectin concentration in patients with essential hypertension. Am. J. Hypertens. 16:72–75. Albinsson, A. R., and G. K. Andersson. 1990. Subclinical characteristics of the wasting pig syndrome. Res. Veteri. Sci. 49(1):71-76. Arita, Y., S. Kihara, N. Ouchi, M. Takahashi, K. Maeda, J. Miyagawa, K. Hotta, I. Shimomura, T. Nakamura, K. Miyaoka, H. Kuriyama, M. Nishida, S. Yamashita, K. Okubo, K. Matsubara, M. Muraguchi, Y. Ohmoto, T. Funahashi, and Y. Matsuzawa. 1999. Paradoxical decrease of an adipose-specific protein, adiponectin, in obesity, Biochem. Biophys. Res. Commun. 257:79–83. Armand, M., P. Borel, P. H. Rolland, M. Senft, M. Andre, H. Lafant, and D. Lairon. 1992. Adaptation of gastric lipase in mini-pigs fed a high-fat diet. Nutr. Res. 12:489-499. Attisano, L., and J. L. Wrana. 2002. Signal transduction by the TGF-βsuperfamily. Science 296:1646–1647. Baumann, A., P. C. Ibebunjo, W. A. Grasser, and V. M. Paralkar. 2003. Myostatin expression in age and denervation-induced skeletal muscle atrophy. J. Musculoskelet. Neuronal Interact. 3:8–16. Berg, A. H., T. P. Combs, X. Du, M. Brownlee, and P. E. Scherer. 2002. The adipocyte- secreted protein Acrp30 enhances hepatic insulin action. Nat. Med. 7: 947–953. Bertrand, S., G. A. Anik. O. Malika, and V. Dominioue.1982. Response of the exocrine pancreas to quantitative and qualitative variation s in dietary lipids. Am. Physol. 242:G10-G15. Boettner, M., B. Prinz, C. Holz, U. Stahl, and C. Lang. 2002. High-throughput screening for expression of heterologous proteins in the yeast Pichia pastoris. J. Biotechnol. 99: 51-62. Bogdanovich, S., T. O. Krag, E. R. Barton, L. D. Morris, L. A. Whittemore, R. S. Ahima, and T. S. Khurana. 2002. Functional improvement of dystrophic muscle by myostatin blockade. Nature 420:418–421. Bogdanovich, S., K. J. Perkins, T. O. Krag, L. A. Whittemore, and T. S. Khurana. 2005. Myostatin propeptide-mediated amelioration of dystrophic pathophysiology. FASEB J. 19:543–549. Borgstrom, B. 1975. On the interactions between pancreatic lipase and colipase and the substrate, and the importance of bile salts. J. Lipid Res. 16(6):411-417. Borgstrom, B., T. Wieloch, and C. Erlanson-Albertsson. 1979. Evidence for a pancreatic procolipase and its activation by trypsin. FEBS Lett. 108(2):407- 410. Borgstrom, B. and H. Hildebrand. 1975. Lipase and co-lipase activities of human small intestinal contents after a liquid test meal. Scand. J. Gastro. 10:585 - 591. Bottner, M. and C. Lang. 2004. High-throughput expression in microplate format in pichia pastoris. Methods Mol. Biol. 267: 277-286. Boucher, J. 2005. Adipokine expression profile in adipocytes of different mouse models of obesity, Horm. Metab. Res. 37:761–767. Bowie, J. U., R. Luthy, and D. Eisenberg. 1991. A method to identify protein sequences that fold into a known three-dimensional structure. Science 253:164-170. Brand-Saberi, B. and B. Christ. 1999. Genetic and epigenetic control of muscle development in vertebrates. Cell Tissue Res. 296: 199–212. Brannon, P. M. 1990. Primary cultures of pancreatic acinar cells. In: Thompson, J. C., ed. Gastrointestinal endocrinology: receptors and post-receptor mechanisms. SanDiego, CA: Academic Press pp. 199–209. Braun, T., M. Rudnicki, A. H. H. Arnold, and R. Jaenisch. 1992. Targeted inactivation of the muscle regulatory gene Myf-5 results in abnormal rib development and perinatal death. Cell 71:369–382. Cera, K. R., D. C. Mahan, and G. A. Reinhart. 1988. Weekly digestibilities of diets supplemented with corn oil, lard or tallow by weanling swine. J. Anim. Sci. 66(6):1430-1437. Cera, K. R., D. C. Mahan, and G. A.Reinhart. 1990. Evaluation of various extracted vegetable oils, roasted soybeans, medium-chain triglyceride and an animal-vegetable fat blend for postweaning swine. J. Anim. Sci. 68(9):2756-2765. Cereghino, J. and J. Cregg. 2000. Heterologous protein expression in the methylotrophic yeast Pichia pastoris. FEMS Microbiol. Rev. 24:45-66. Chandran, M., S. A. Phillips, T. Ciaraldi, and R. R. Henry. 2003. Adiponectin: more than just another fat cell hormone? Diabetes Care 26:2442–2450. Chapus, C., M. Rovery, L. Sarda, and R. Verger. 1988. Minireview on pancreatic lipase and colipase. Biochimie. 70(9):1223-1234. Chiang, S.H., J. E. Pettigrew, S. D. Clarke, and S. G.Cornelius. 1989. Digestion and absorption of fish oil by neonatal piglets. J. Nutri. 119(11):1741-1743. Cieslak, D., T. Blicharski, W. Kapelanski, and M. Pierzchala. 2003. Investigation of polymorphisms in the porcine Myostatin (GDF8; MSTN) gene. Czech J. Anim. Sci. 48:69–75. Clement, K., C. Vaisse, N. Lahlou, S. Cabrol, V. Pelloux, D. Cassuto, M. Gourmelen, C. Dina, J. Chambaz, J. M. Lacorte, A. Basdevant, P. Bougneres, Y. Lebouc, P. Froguel, and B. Guy-Grand. 1998. A mutation in the human leptin receptor gene causes obesity and pituitary dysfunction. Nature 392:398–401. Cnop, M., P. J. Havel, K. M. Utzschneider, D. B. Carr, M. K. Sinha, E. J. Boyko, B. M. Retzlaff, R. H. Knopp, J. D. Brunzell, and S. E. Kahn. 2003. Relationship of adiponectin to body fat distribution, insulin sensitivity and plasma lipoproteins: evidence for independent roles of age and sex. Diabetologia. 46:459–469. Coerver, K. A. 1996. Activin signaling through activin receptor type II causes the cachexia-like symptoms in inhibin-deficient mice. Mol. Endocrinol. 10:534–543. Cole, D. J. A., G. M. Sparkers, D. Lewis, and H. Y. Yen. 1983. Proceeding, 5th World Conference on Animal Production. 2:417. Combs, T. P., A. H. Berg, S. Obici, P. E. Scherer, and L. Rossetti. 2001. Endogenous glucose production is inhibited by the adipose-derived protein Acrp30. J. Clin. Invest. 108:1875–1881. Constan, D. B., and E. J. Robertson. 1999. Regulation of bone morphogenetic protein deficient mice. J. Clin. Invest. 109:595–601. Cregg, J., T. Vedvick, and W. Raschke. 1993. Recent advances in the expression of foreign genes in Pichia pastoris. Biotechnology (NY) 11: 905-910. Dagorn, J. C. 1978. Non-parallel enzyme secretion from rat pancreas: in vivo studies. J. Physiol. 280:435–448. de Caestecker, M. 2004. The transforming growth factor-beta superfamily of receptors. Cytokine Growth Factor Rev. 15(1):1-11. DeCaro, J., M. Boudouard, J. Bonicel, A. Guidoni, P. Desnuelle, and M. Rovery. 1981. Porcine pancreatic lipase completion of the primary structure. Biochim. Biophys. Acta. 671(2):129-238. Delbaere, A., Y. Sidis, and A. Schneyer. 1999. Differential response to exogenous andendogenous activin in a human ovarian teratocarcinoma-derived cell line(PA-1): regulation by cell surface follistatin. Endocrinology 140:2463–2470. Diaz-Candamio, M. J., F. Dominguez, L. S. Haro, N. Ling, and J. Devesa. 1993. A 12-kilodalton N-glycosylated growth hormone-related peptide is present in humanpituitary extracts. J. Clin. Endocrinol. Metab. 77:134–138. Dubois, C. M., M. H. Laprise, F. Blanchette, L. E. Gentry, and R. Leduc. 1995. Processing of transforming growth factorβ1 precursor by human furine convertase. J. Biol. Chem. 270:10618–10624. Erlanson-Albertsson, C., A. Larsson, and R. Duan. 1987. Secretion of pancreatic lipase and colipase from rat pancreas. Pancreas 2:531–535. Faber, K., W. Harder, G. Ab, and M. Veenhuis. 1995. Review: Methylotrophic yeasts as factories for the production of foreign proteins. Yeast 11: 1331-1344. Fernandez, S., R. Rios, V. Arce, J. A. Diaz, N. Alonso, M. Perez, J. L. Bello, and J. Devesa. 2002. GDF-8 (myostatin) is expressed in human myeloid leukemic cells. Proc 7th Annual Meeting of the European Haematology Association, Monduzzi Editor, pp 323–326. Ferre, F. 2004. The biology of peroxisome proliferator-activated receptors: relationship with lipid metabolism and insulin sensitivity. Diabetes 53 (Suppl. 1):S43–S50. Field, C. J., E. A. Ryan, A. B. Thomson, and M. T. Clandinin. 1990. Diet fat composition alters membrane phospholipid composition, insulin binding, and glucose metabolism in adipocytes from control and diabetic animals. J. Biol. Chem. 265:11143–11150. Fisher, F. M., P. G. McTernan, G. Valsamakis, R. Chetty, A. L. Harte, A. J. Anwar, J. Starcynski, J. Crocker, A. H. Barnett, C. L. McTernan, and S. Kumar. 2002. Differences in adiponectin protein expression: effect of fat depots and type 2 diabetic status. Horm. Metab. Res. 34:650–654. Flores, C. A., P. M. Brannon, S. A. Bustamante, J. Bezerra, K. T. Butler, T. Goda, and O. Koldovsky. 1988. Effect of diet on intestinal and pancreatic enzyme activities in the pig. J. P. Gastro. Nutr. 7(6):914-921. Fujita, Y., I. Mori, and S. Kitano. 1983. Color reaction between pyrogallol red-molybdenum (VI) complex and protein. Bunsei Kagaku 32:379–386. Gamer, L. W., K. A. Cox, C. Small, and V. Rosen. 2001. GDF-11 is a negative regulator of chondrogenesis and myogenesis in the developing chick limb. Dev. Biol. 229: 407–420. Gamer. L., N. Wolfman, A. Celeste, G. Hattersley, R. Hewick, and V. Rosen. 1999. A novel BMP expressed in developing mouse limb, spinal cord, and tail bud is a potent mesoderm inducer in Xenopus embryos. Dev. Biol. 208:222–232. Gargouri, Y., G. Pieroni, J. F. Riviere, P. A. Lowe, L. Sarda, and R. Verger. 1986. Kinetic assay of human gastric lipase on short- and long-chain triacylglycerol emulsions. Gastrology. 91:919-925. Gaskin, K. J., P. R. Durie, R. E. Hill, L. M. Lee, and G. G. Forstner. 1982. Colipase and maximally activated pancreatic lipase in normal subjects and patients with steatorrhea. J. Clin. Invest. 69(2):427-34. Gil-Campos, M., R. R. Canete, and A. Gil. 2004. Adiponectin the missing link in insulin resistance and obesity. Clin. Nutr. 23:963–974. Girgenrath, S., K. Song, and L. A. Whittemore. 2005. Loss of myostatin expression alters fiber-type distribution and expression of myosin heavy chain isoforms in slow- and fast-type skeletal muscle. Muscle Nerve 31:34–40. Gleizes, P. E., J. S. Munger, I. Nunes, J. G. Harper, R. Mazzieri, I. Noguera, and D. B. Rifkin. 1997. TGF-βlatency: biological significance and mechanisms of activation. Stem Cells 15:190–197. Goldstein, B. J., and R. Scalia. 2004. Adiponectin: a novel adipokine linking adipocytes and vascular function, J. Clin. Endocrinol. Metab. 89:2563–2568. Goransson, L. 1990. The effect of late pregnancy feed allowance on the milk composition of the sow’s colostrum and milk. Acta. Vet. Scandi. 31(1):109-115. Granon, S. and M. Semeriva. 1980. Effect of taurodeoxycholate, colipase and temperature on the interfacial inactivation of porcine pancreatic lipase. Eur. J. Biochem. 111(1):117-124. Grobet, L., D. Pirottin, F. Farnir, D. Poncelet, L. J. Royo, B. Brouwers, E. Christians, D. Desmecht, F. Coignoul, R. Kahn, and M. Georges. 2003.Modulating skeletal muscle mass by postnatal, muscle-specific inactivation of the myostatin gene. Genesis 35: 227–238. Grobet, L., L. J. Royo, D. Poncelet, D. Pirottin, B. Brouwers, J. Riquet, A. Schoeberlein, S. Dunner, F. Menissier, J. Massabanda, R. Fries, R. Hanset, and M. Georges. 1997. A deletion in the bovine myostatin gene causes the double-muscled phenotype in cattle. Nat. Genet. 17:71–74. Grobet, L., Poncelet, D., Royo, L.J., Brouwers, B., Pirottin, D., Michaux, C., Menissier, F., Zanotti, M., Dunner, S., and M.Georges. 1998. Molecular definition of an allelic series of mutations disrupting the Myostatin function and causing double-muscling in cattle. Mamm. Genome. 9:210–213. Grundy, S. M. 2007. Metabolic syndrome: a multiplex cardiovascular risk factor. J. Clin. Endocrinol. Metab. 92:399–404. Guo, K.Y., P. Halo, R. L. Leibel, and Y. Zhang. 2004. Effects of obesity on the relationship of leptin mRNA expression and adipocyte size in anatomically distinct fat depots in mice. Am. J. Physiol. Regul. Integr. Comp. Physiol. 287:R112–R119. Guo, K., and K.Walsh. 1997. Inhibition of Myogenesis by Multiple Cyclin-Cdk Complexes. J. Biol. Chem. 272:791–797. Hartman, P. A., V. W. Hays, R. O. Baker, L. H. Neagle, and D.V. Catron. 1961. Digestive enzyme development in the young pig. J. Anim. Sic. 20:114-123. Hasty, P., A. Bradley, J. H. Morris, D. G. Edmondson, J. M.Venuti, E. N. Olson, and W. H. Klein.1993. Muscle deficiency and neonatal death in mice with a targeted mutation in the myogenin gene. Nature 364:501–506. Havel, P. J. 2004. Update on adipocyte hormones: regulation of energy balance and carbohydrate/lipid metabolism. Diabetes 53 (Suppl. 1):S143–S151. Hayashi, S., and A. P. McMahon. 2002. Efficient recombination in diverse tissues by a tamoxifen-inducible form of Cre: a tool for temporally regulated gene activation/inactivation in the mouse. Dev. Biol. 244:305–318. Hedemann, M. S., A. R. Pedersen, and R. M. Engberg. 2001. Exocrine pancreatic secretion is stimulated in piglets fed fish oil compared with those fed coconut oil or lard. J. Nutri. 131(12) :3222-3226 Hedley, A. A., C. L. Ogden, C. L. Johnson, M. D. Carroll, L. R. Curtin, and K. M. Flegal. 2004. Prevalence of overweight and obesity among US children, adolescents, and adults, 1999–2002, J. Amer. Med. Assoc. 291:2847–2850. Hermoso, J., D. Pignol, S. Penel, M. Roth, C. Chapus, and J. C. Fontecilla-Camps. 1997. Neutron crystallographic evidence of lipase-colipase complex activation by a micelle. EMBO J. 16(18):5531-5536. Hidaka, K., I. Yamamoto, Y. Arai, and T. Mukai. 1993. The MEF-3 motif is required for MEF-2 mediated skeletal muscle-specific induction of the rat aldolase A gene. Mol. Cell Biol. 13:6469–6478. Hill, J. J., M. V. Davies, A. A. Pearson, J. H. Wang, R. M. Hewick, N. M. Wolfman, and Y. Qiu. 2002. The myostatin propeptide and the follistatin-related gene are inhibitory binding proteins of myostatin in normal serum. J. Biol. Chem. 277:40735–40741. Hill, J. J., Y. Quiu, R. N. Hewick, and N. M. Wolfman. 2003. Regulation of myostatin in vivo by GASP-1: a novel protein with protease inhibitor and follistatin domains. Mol. Endocrinol. 17:1144–1154. Holm, L., and J. Park. 2000. DaliLite workbench for protein structure comparison. Bioinformatics 16: 566-567. Holz, C., O. Hesse, N. Bolotina, U. Stahl, and C. Lang. 2002. A micro-scale process for high-throughput expression of cDNAs in the yeast Saccharomyces cerevisiae. Protein Exp. Purif. 25: 372-378. Huguet, A., G. Savary, E. Bobillier, Y. Lebreton, and I. Le Huerou-Luron. 2006. Effects of level of feed intake on pancreatic expcrine secretions during the early postweaning period in piglet. J. Anim. Sci. 84:2965-2972. Hunt, I. 2005. From gene to protein: A review of new and enabling technologies for multi-parallel protein expression. Protein Exp. Purif. 40:1-22. International Human Genome Sequencing Consortium. 2001. Initial sequencing and analysis of the human genome. Nature 409:860-921. Iwaki, M., M. Matsuda, N. Maeda, T. Funahashi, Y. Matsuzawa, M. Makishima, and I. Shimomura. 2003. Induction of adiponectin, a fat-derived antidiabetic and antiatherogenic factor, by nuclear receptors. Diabetes 52:655–663. Jennifer, J. H., M. V. Davies, A. A. Pearson, J. H. Wang, R. M. Hewick, N. M. Wolfman, and Y. Qiu. 2002. Themyostatin propeptide and follistatin-related gene are inhibitory binding proteins of myostatin in normal serum. J. Bio. Chem. 277(43):40735-40741. Jensen, M. S., S. K. Jensen, and K. Jakobsen. 1997. Development of digestive enzymes in pigs with emphasis on lipolytic activity in the stomach and pancreas. J. Anim. Sci. 75:437-445. Ji, S., L. R. Losinski, C. S.Gornelius, G. R. Frank, W. G. Millis, G. D. Eerrard, F. F. Depreux, and M. E. Spurlock. 1998. Myostatin expression in porcine tissues: tissue specificity and developmental and postnatal regulation. Am. J. Physiol. 275:R1265–R1273. Ji, S., R. L.Losinski, S. G. Cornelius, G. R. Frank, G. M.Willis, D. E. Gerrard, F. F. Depreux, and M. E. Spurlock. 1998. Misstating expression in porcine tissues: tissue specificity and developmental and postnatal regulation. Am. J. Physiol. 275: R1265–R1273. Jiang, Y. L., N. Li, G. Plastow, Z. L.Liu, X. X. Hu, and C. X.Wu. 2002. Identification of three SNPs in the porcine Myostatin gene (MSTN). Anim. Biotechnol. 13:173–178. Joulia, D., H. Bernardi, V. Garandel, F. Rabenoelina, B. Vernus, and G. Cabello. 2003. Mechanisms involved in the inhibition of myoblast proliferation and differentiation by myostatin. Exp. Cell Res. 286:263–275. Kadowaki, T., K. Hara, T. Yamauchi, Y. Terauchi, K. Tobe, and R. Nagai. 2003. Molecular mechanism of insulin resistance and obesity. Exp. Biol. Med. (Maywood) 228:1111–1117. Kambadur, R., M. Sharma, T. P. L. Smith, and J. J. Bass 1997. Mutations in myostatin (GDF8) in double-muscled Belgiam Blue and Piedmontese cattle. Genome Res. 7:910–915. Karim, L., W. Coppieters, L. Grobet, A. Valentini, and M. Georges. 2000. Convenient genotyping of six myostatin mutations causing double-muscling in cattle using a multiplex oligonucleotide ligation assay. Anim. Genet. 31:396–399. Katagiri, T., A. Yamaguchi, M. Komaki, E. Abe, N. Takahashi, T. Ideda, V. Rosen, J. M. Wozney, A. Fujisawa-Sehara, and T. Suda. 1994. Bone morphogenetic protein-2 converts the differentiation pathway of C2C12 myoblasts into the osteoblast lineage. J. Cell Biol. 127:1755–1766. Kaufman, F. 2002. Type 2 diabetes mellitus in children and youth: a new epidemic. J. Pediatr. Endocrinol. Metab. 15:737–744. Kawai, S., C. Faucheu, S. Gallea, S. Spinella-Jaegle, A. Atfi, R. Baron, and S. Roman. 2000. Mouse Smad8 phosphorylation downstream of BMP receptors ALK-2, ALK-3, and ALK-6 induces its association with Smad4 and transcriptional activity. Biochem. Biophys. Res. Commun. 271:682–687. Kelly, D., J. A. Smyth, and K. J.McCracken. 1991. Digestive development of the early-weaned pig. 2.Effect of level of food intake on digestive enzyme activity during the immediate postweaning period. Br. J. Nutri. 65(2):181-188. Kershaw, E. E., and J. S. Flier. 2004. Adipose tissue as an endocrine organ. J. Clin. Endocrinol. Metab. 89:2548–2556. Kim, H. S., L. Liang, R. G. Dean, D. B. Hausman, D. L. Hartzell, and C. A. Baile. 2001. Inhibition of preadipocyte differentiation by myostatin treatment in 3T3-L1 cultures. Biochem. Biophys. Res. Commun. 281:902–906. Kinkel, M. D., and W. E. H. Jr. 2003. Coordinate down-regulation of cartilage matrix gene expression in Bcl-2 deficient chondrocytes is associated with decreased SOX9 expression and decreased mRNA stability. J. Cell Biochem. 88:941–953. Knowler, W., C. E. Barrett-Connor, S. E. Fowler, R. F. Hamman, J. M. Lachin, E. A. Walker, and D. M. Nathan. 2003. Diabetes Prevention Program Research Group Reduction in the incidence of type 2 diabetes with lifestyle intervention or metformin. N. Engl. J. Med. 346:393–403. Kocamis, H., D. C. McFarland, and J. Killefer. 2001. Temporal expression of growth factor genes during myogenesis of satellite cells derived from the biceps femoris and pectoralis major muscles of the chicken. J. Cell. Physiol. 186: 146–152. Kopelman, P. G. 2003. Obesity as a medical problem. Nature 404:635–643. Kumar, A., V. Novoselov, A. J. Celeste, N. M. Wolfman, P. ten Dijke, and M. R. Kuehn. 2001. Nodal signaling uses activin and transforming growth factor-βreceptor regulated Smads. J. Biol. Chem. 276:656–661. Langley, B., M. Thomas, A. Bishop, M. Sharma, S. Gilmour, and R. Kambadur. 2002. Myostatin inhibits myoblast differentiation by down-regulating MyoD expression. J. Biol. Chem. 277:49831–49840. Langlois, B. E., G. L. Cromwell, and V. W. Hays. 1978a. Influence of chlortetracycline in swine feed on reproductive performance and on incidence and persistence of antibiotic resistant bacteria. J. Anim. Sci. 46:1369-1382. Langlois, B. E., G. L. Cromwell, and V. W. Hays. 1978b. Influence of type of antibiotic and length of antibiotic feeding period on performance and persistence of antibiotic resistant enteric bacteria in growing-finishing swine. J. Anim. Sci. 46:1383-1396. Larsson, A. and C. Erlanson-Albertsson. 1986. Effect of phosphatidylcholine and free fatty acid on the activity of pancreatic lipase-colipase. Biochim. Biophys. Acta. 876(3):543-550. Larsson, A. and C. Erlanson-Albertsson. 1991. The effect of pancreatic procolipase and colipase on pancreatic lipase activation. Biochim. et Biophys. Acta. 1083(3):283 -288. Lee, C., T. Williams, D. Wong, and G. Robertson. 2005. An episomal vector for screening mutant gene libraries in Pichia pastoris. Plasmid. 54: 80-85. Lee, J.L., S.N. Yang, C.S. Park, D. Jeoung, and H.Y. Kim. 2004. Purification and glycosylation pattern of human L-ferritin in Pichia pastoris. J. Microbiol. Biotechnol. 14:68-73. Lee, S. J., and A. C. McPherron. 2001. Regulation of myostatin activity and muscle growth. Proc. Natl. Acad. Sci. 98:9306–9311. Lee, S. J., L. A. Reed, M. V. Davies, S. Girgenrath, M. E. Goad, K. N. Tomkinson, J. F. Wright, C. Barker, G. Ehrmantraut, J. Holmstrom, B. Trowell, B. Gertz, M. S. Jiang, S. M. Sebald, M. Matzuk, E. Li, L. F. Liang, E. Quattlebaum, R. L. Stotish, and N. M. Wolfman. 2005. Regulation of muscle growth by multiple ligands signaling through activin type II receptors. Proc. Natl. Acad. Sci. 102:18117–18122. Lee, S. J., and A. C. McPherron. 2001. Regulation of myostatin activity and muscle growth. Proc. Natl. Acad. Sci. 98:9306–9311. Lee, S. J. 2004. Regulation of muscle mass by myostatin. Annu. Rev. Cell Dev. Biol. 20:61–86. Lee, S. J. 2008. Genetic analysis of the role of proteolysis in the activation of latent myostatin. Pub. Lib. Sci. 3(2):1-7. Liang, E., P. Hu, and B. M. Spiegelman. 1996. AdipoQ is a novel adipose-specific gene dysregulated in obesity. J. Biol. Chem. 271:10697–10703. Lin, J., A H. B. rnold, M. A. Della-Ferra, M. J. Azain, D. L. Hartzell, and C. A. Baile. 2002. Myostatin knockout in mice increases myogenesis and decreases adipogenesis. Biochem. Biophys. Res. Commun. 291:701–706. Lindemann, D., S. G. Gornelius, and S. M. Kandellegy. 1986. Effect of age, weaning, and diet on digestive enzyme levels in the piglet. J. Anim. Sci. 62:1298-1307. Link, B. A., and R. Nishi. 1997. Opposing effects of activin A and follistatin on developing skeletal muscle cells. Exp. Cell Res. 233:350–362. Liu, S., V. E. Baracos, H. A. Quinney, T. Le Bricon, and M. T. Clandinin. 1995. Parallel insulin-like growth factor I and insulin resistance in muscles of rats fed a high fat diet. Endocrinology 136:3318–3324. Livak, K. J., and T. D. Schmittgen. 2001. Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)). Methods 25:402–408. Lowe, M. E. 1994. Pancreatic triglyceride lipase and colipase: insights into dietary fat digestion. Gastrolgy. 107(5):1524-1536. Lueking, A., C. Holz, C. Gotthold, H. Lehrach, and D. Cahill. 2000. A system for dual protein expression in Pichia pastoris. Protein Exp. Purif. 20:373-378. Lueking, A., S. Horn, H. Lehrach, and D. Cahill. 2003. A dual expression vector allowing expression in E. coli and P. pastoris, including new modifications. Methods Mol. Biol. 205:31-42. Luthy, R., J. U. Bowie, and D. Eisenberg. 1992. Assessment of protein models with three-dimensional profiles. Nature 356:83-85. Macauley-Patrick, S., M. L. Fazenda, R. McNeil, and L. M. Harvey. 2005. Heterologous protein expression using the Pichia pastoris expression system. Yeast 22:249-270. Mahe-Gouhier, N., and C. L. Leger. 1988. Immobilized colipase affinities for lipases B, A, C and their terminal peptide (336-449): the lipase recognition site lysine residues are located in the C-terminal region. Biochim. Biophys. Acta. 962(1): 91-97. Malika, O., S. Bertrand , G. G. Anikn, and A. Genevieve.1980. Differential regulation of lipase and colipase in the pancreas by dietary fat and protein. J. Nutr.110:2302-2309. Massague, J. 1998. TGF-βsignal transduction. Annu. Rev. Biochem. 67:753–791. Massague, J., S. Cheifetz, T. Endo, and B. N. Ginard. 1986.Type beta transforming growth factor is an inhibitor of myogenic differentiation. Proc. Natl. Acad. Sci. 83: 8206–8210. Mateescu, R. G., and M. L. Thonney. 2005. Effect of testosterone on insulin-like growth factor-I, androgen receptor, and myostatin gene expression in splenius and semitendinosus muscles in sheep. J. Anim. Sci. 83:803–809. Matzuk, M. M., N. Lu, H. Vogel, K. Sellheyer, D. R Roop, and A. Bradley. 1995. Multiple defects and perinatal death in mice deficient in follistatin. Nature 374:360–363. McClung, J. P., C. A. Roneker, W. Mu, D. J. Lisk, P. Langlais, F. Liu, and X. G. Lei. 2004. Development of insulin resistance and obesity in mice overexpressing cellular glutathione peroxidase. Proc. Natl. Acad. Sci. 101:8852–8857. McConnell, J. C., K. M. Barth, and S. A. Griffin. 1971. Nutrient digestibility and nitrogen metabolism studies at different stages of growth with fat and lean type swine fed two levels of protein. J. Anim. Sci. 32(4): 654-657. McPherron, A. C. and S. J. Lee. 1997. Double muscling in cattle due to mutations in the myostatin gene. Proc. Natl. Acad. Sci. 94:12457-12461. McPherron, A. C., and S. J. Lee.1996. The transforming growth factor-beta superfamily. In Growth Factors and Cytokines in Health and Disease. Pressed Greenwich, C.T. Vol. 1B pp. 357-393. McPherron, A. C., A. M. Lawler, and S. J. Lee. 1997. Regulation of skeletal muscle mass in mice by a new TGF-beta superfamily member. Nature 387:83–90. McPherron, A. C., A. M. Lawler, and S. J. Lee. 1999. Regulation of anterior/ posterior patterning of the axial skeleton by growth/differentiation factor 11. Nat. Genet. 22: 260–264. McPherron, A. C., and S. J. Lee. 2002. Suppression of body fat accumulation inmyostatin- deficient mice. J. Clin. Invest. 109:595–601. Mendler, L., E. Zador, M. Ver Heyen, L. Dux, and F. Wuytack. 2000. Myostatin levels in regenerating rat muscles and in myogenic cell cultures. J. Muscle Res. Cell Moti. 21:551–563. Menendez, J., L. Hernandez, A. Banguela, and J. Pais. 2004. Functional production and secretion of the Gluconoacetobacter diazatrophicus fructose-releasing exo-levanase (LsdB) in Pichia pastoris. Enz. Microb. Technol. 34:446-452. Meyer, J. H., R. S. Jones. 1975. Canine pancreatic responses to intestinally perfused fat and products of fat digestion. Am. J. Physiol. 226:1178-1187. Molkentin, J. D., and E. N. Olson. 1996. Defining the regulatory networks for muscle development. Curr. Opin. Genet. Dev. 6:445–453. Momsen, W. E., M. M. Momsen, and H. L. Brockman.1995. Lipid structural reorganization induced by the pancreatic lipase cofactor, procolipase. Biochem. 34(21):7271-7281. Montague, C. T., I. S. Farooqi, J. P. Whitehead, M. A. Soos, H. Rau, N. J. Wareham, C. P. Sewter, J. E. Digby, S. N. Mohammed, J. A. Hurst, C. H. Cheetham, A. R. Earley, A. H. Barnett, J. B. Prins, and S. O. Rahilly. 1997. Congenital leptin deficiency is associated with severe earlyonset obesity in humans. Nature 387:903–908. Morissette, M. R., S. A. Cook, S. Foo, G. McKoy, N. Ashida, M. Novikov, M. Scherrer-Crosbie, L. Li, T. Matsui, G. Brooks, and A. Rosenzweig. 2006. Myostatin regulates cardiomyocyte growth through modulation of Akt signaling. Circ. Res. 99: 15–24. Muoio, D. M., J. M. Way, C. J. Tanner, D. A. Winegar, S. A. Kliewer, J. A. Houmard, W. E. Kraus, and G. L. Dohm. 2002. Peroxisome proliferatoractivated receptor-alpha regulates fatty acid utilization in primary human skeletal muscle cells. Diabetes 51:901–909. Nabeshima, Y., K. Hanaoka, M. Hayasaka, E. Esumi, S. Li, I. Nonaka, and Y. Nabeshima. 1993. Myogenin gene disruption results in perinatal lethality because of severe muscle defect. Nature 364:532–535. Nadal-Ginard, B. 1978. Commitment, fusion and biochemical differentiation of a myogenic cell line in the absence of DNA synthesis. Cell 15:855–864. National Center for Chronic Disease Prevention and Health Promotion, Behavioral Risk Factor Surveillance System. http://www.cdc. gov/brfss/index.htm 2007. Neville, C., D. Gonzales, L. Houghton, M. J. McGrew, and N. Rosenthal. 1996. Modular elements of the MLC 1f/3f locus confer fiber-specific transcription regulation in transgenic mice, Dev. Genet. 19:157–162. Newfeld, S. J., R. G. Wisotzkey, and S. Kumar. 1999. Molecular evolution of a developmental pathway: phylogenetic analyses of transforming growth factor-beta family ligands, receptors and Smad signal transducers. Genetics 152:783–795. Nishitoh, H., H. Ichijo, M. Kimura, T. Matsumoto, F. Makishima, A. Yamaguchi, H. Yamashhita, S. Enomoto, and K. Miyazono. 1996. Identification of type I and type II serine/threonine kinase receptors for growth/differentiation factor-5. J. Biol. Chem.271:21345–21352. Ogden, C., K. Flegal, M. Carroll, and C. Johnson. 2002. Prevalence and trends in overweight among US children and adolescents, 1999–2000. J. Amer. Med. Asso. 288:1728–1732. Olson, E. N. 1992. Interplay between proliferation and differentiation within the myogenic lineage. Dev. Biol. 154:261–272. Okuno, A., H. Tamemoto, K. Tobe, K. Ueki, Y. Mori, K. Iwamoto, K. Umesono, Y. Akanuma, T. Fujiwara, H. Horikoshi, Y. Yazaki, and T. Kadowaki. 1998. Troglitazone increases the number of small adipocytes without the change of white adipose tissue mass in obese Zucker rats. J. Clin. Invest.101:1354–1361. Oldham, J. M., J. A. K. Martyn, M. Sharma, R. Jeanplong, R. Kambadur, and J. J. Bass. 2001. Molecular expression of myostatin and MyoD is greater in double-muscled than normal-muscled cattle fetuses. Am. J. Physiol. Reg. Int. Comp. Physiol. 280: R1488–R1493. Oliver, I. T. 1955. A spectrophotometric method for the determination of creatine phosphokinase and myokinase. J. Biochem. 61:116. Palade, G. 1975. Intracellular aspects of the process of protein synthesis.Science 189 (4200):347-358. Patton, J. S., P. A. Albertsson, C. Erlanson, and B. Borgstrom. 1978. Binding of porcine pancreatic lipase and colipase in the absence of substrate studies by two phase partition and affinity chromatography. J. Biol. Chem. 253(12):4195-4202. Piek, E., C. H. Heldin, and P. ten. Dijke. 1999. Specificity, diversity, and regulation in pituitary extracts. J. Clin. Endocrinol. Metab. 77:134–138. Pierzynowski, S. G., B. R. Westrom, C. Erlanson-Albertsson, B. Ahre''n, J. Svendsen, and B. W. Karlsson. 1993. Induction of exocrine pancreas maturation at weaning in young developing pigs. J. Pedi. Gastro. Nutr. 16(3):287-293. Potts, J. K., S. E. Echternkamp, T. P. Smith, and J. M. Reecy. 2003. Characterization of gene expression in double-muscled and normal-muscled bovine embryos. Anim. Genet. 34:438–444. Rausch, U., P. Vasiloudes, K. Rudiger, and H. F. Kern.1985. In-vivo stimulation of rat pancreatic acinar cells by infusion of secretin. II. Changes in individual rates of enzyme and isoenzyme biosynthesis. Cell Tissue Res. 242(3):641-644. Rawls, D., and E. N. Olson. 1997. MyoD meets its maker. Cell 89:5–8. Rawls, A., M. R. Valdez, W. Zhang, J. Richardson, W. H. Klein, and E. N. Olson.1998. Overlapping functions of the myogenic bHLH genes MRF4 and MyoD revealed in double mutant mice. Development 125:2349–2358. Rebbapragada, A., H. Benchabane, J. L. Wrana, A. J. Celeste, and L. Attisano. 2003. Myostatin signals through a transforming growth factorβ-like signaling pathway to block adipogenesis. Mol. Cell. Biol. 23:7230–7242. Reisz-Porszasz. S., S. Bhasin, A. J. Nrtaza, R. Shen, I. Sinha-Hikim, A. Hogue, T. J. Fielder, and N. F. Gonzalez-Cadaviz. 2003. Lower skeletal muscle mass in male transgenic mice with muscle-specific overexpression of myostatin. Am. J. Physiol. 285:E876–E878. Reshef, R., M. Maroto, and A. B. Lassar. 1998. Regulation of dorsal somitic cell fates: BMPs and noggin control the timing and pattern of myogenic regulat
摘要: 
近5年來在台灣地區每頭母豬年生產離乳仔豬頭數約為13-15頭,顯著低於歐美養豬先進國家之23頭仔豬,而且仔豬於保育期間之死亡率更高達15-40%,造成養豬業者為提高仔豬育成率常添加含藥物之飼料添加物。雖然抗生素可預防疫病及促進豬隻的生長,不過有藥物殘留之疑慮,歐盟在2006年全面禁止將抗生素做為畜禽之生長促進劑。另外在豬養殖過程中,為提高瘦肉率迎合消費者需求,在飼料添加腎上腺素β-受體激動劑(β-adrenergic agonist)或培林 (Ractopamine)等,但其副作用為導致噁心、頭暈、肌肉顫抖、心悸、血壓上升等中毒癥狀,因此國內至今未開放其作為豬之飼料添加物。為因應上述國內養豬需求,本試驗計畫將運用基因重組方法與酵母細胞,表現提高仔豬生長性能與育成率之脂肪水解酵素與改善肉豬屠體品質之功能蛋白質等飼料添加物,建立無抗生素物質之養豬飼養模式,確保國人食肉之安全與符合世界潮流之趨勢。
豬飼糧中大部分 (超過90%) 脂肪的消化與吸收,需經胰脂肪酶之水解作用,但在胰脂肪酶水解過程受胰輔脂肪酶 (colipase) 的調控,即是將經膽鹽乳化後之脂肪小滴 (droplet) 穩定於胰脂肪酶氮端功能區塊,進行脂肪水解作用形成甘油與脂肪酸。不過仔豬在離乳後最初 2 週期間會發生胰脂肪酶和胰輔脂肪酶活性與分泌量不足之現象,嚴重減低離乳仔豬脂肪之吸收與利用。因此,藉由選殖豬胰脂肪酶與胰輔脂肪酶cDNA,將其構築於酵母菌之Pichia pastoris表現載體,再以電穿孔方法轉形至酵母菌宿主細胞,經發酵培養酵母菌轉形株後,分離與乾燥上清液,產生表現量高且具有高生物活性之重組胰脂肪酶與胰輔脂肪酶蛋白質。在添加重組胰輔脂肪酶與胰脂肪酶之動物生長試驗方面,結果顯示,在保育期飼糧中添加 5,000 U/kg 之重組胰脂肪酶或胰輔脂肪酶,可以提升離乳仔豬之增重(P<0.05),而添加 5,000 U/kg 之重組胰脂肪酶或 10,000 U/kg 胰輔脂肪酶,則具有改善離乳仔豬脂肪利用率之效果(P<0.05)。
探討畜試黑豬仔豬之出生體重與肌肉生長抑制素mRNA量之相關性,試驗結果顯示,出生體重較輕仔豬組 (1.0 ± 0.1 kg) 之肌肉生長抑制素 mRNA表現量顯著高於體重較重仔豬組 (1.5 ± 0.2 kg) 約1.97倍,顯示肌肉生長抑制素基因表現量高可能具有抑制畜試黑豬仔豬出生體重之作用。在運用重組肌肉生長抑制素前胜肽改善畜試黑豬肉豬之生長性能與屠體性狀,試驗利用巢式聚合酶連鎖反應 (Nest PCR) 選殖,合成828-bp之肌肉生長抑制素前胜肽PCR產物,將肌肉生長抑制素前胜肽cDNA序列接合於pGAPZαA中,完成表現載體 (pGAPZαA Myostatin-propeptide) 之建構,再將此構築完成之表現載體轉形至酵母細胞,經發酵培養後分離與乾燥上清液,供進行蛋白質特性與動物效果試驗。動物效果試驗顯示,添加1.0 mg/kg重組肌肉生長抑制素前胜肽具有改善畜試黑豬增重與採食量之效果(P<0.05)。雖然添加0.5與1.0 mg/kg重組肌肉生長抑制素前胜肽對畜試黑豬屠體性狀沒有顯著效應,不過在瘦肉量與骨骼百分比隨重組肌肉生長抑制素前胜肽添加量增加而增加,而脂肪百分比則隨添加量之增加而降低。由此結果顯示,應用添加1.0 mg/kg重組肌肉生長抑制素前胜肽,具有改善畜試黑豬肉豬增重與採食量之效果,以及提升瘦肉率與骨骼百分率以及降低脂肪百分率之趨勢,但不影響背最長肌、小里肌與腹脇等部位之肉質化學組成。

For the latest 5 years in Taiwan, each sow per year can yield 13-15 hd post-weaning piglets, which is less than those of pig industry of advanced countries including Europe and America. Cope with this situation our pig farmers usually like to complement several drug additives. Although antibiotics can prevent piglets from disease impacts and enhance their growth performance, we can be regardless of drug remainder in pork. Europe Union had prohibited antibiotics to be growth enhancer from livestock since 2006. Most of consumers prefer higher lean meat products, so several pig farmers add β-adrenergic agonist or Ractopamine to increase lean meat. Owing to there are some serious side effects such as nausea, giddiness, muscular shiver, palpitations, hypertension and so on, thus our government still forbids them to be feed additives. To confront this situation, we have applied gene engineering yeast cells to generate fatty hydrolysis enzymes in order to improve growth performance and survival rate, and to generate functional protein as feed additive to improve carcass quality. We hope that can apply those of feed additives to establish antibiotic-free of pig feeding model, and assure consumers' safety of Taiwanese pork products at the same time to conform the world trend.
Lipase plays an important role in fat digestion and absorption, owing to the use of fat in most animal diets (over 90%). The activity of the lipase will be regulated by colipase, which anchors the emulsification of fat droplet by bile salt to the N-terminal domain of lipase. Therefore, fat can hydrolyze into glycerol and fatty acid. The activity and secretion of lipase and colipase deficient is often for pig during the first 2 wks after weaning. We performed gene cloning for porcine pancreatic lipase and colipase, and constructed both of cDNA into the Pichia pastoris expression vector, and transformed them into yeast host cells through electroportion process and raised the yeast transformants. Following the fermentation of yeast transformants, the supernatant was harvested and freeze dried, and then provided to analyze protein characters and animal tests, respectively. In animal trial, we found that for adding 5,000 U/kg of recombinant lipase or colipase can increase the weight gain(P<0.05), as well as, added 5,000 U/kg of recombinant colipase or 10,000 U/kg of recombinant lipase also show a positive effect in fat digestion for post-weaning piglets(P<0.05).
To survey the relation between myostatin mRNA amounts and birth-weight of neonatal TLRI No.1 Black pigs. The result showed the myostatin mRNA amounts of the piglets with lower birth-weight was 1.97 times higher than those with heavier birth-weight. The results hint that myostatin gene may possess unique impact on neonatal TLRI No.1 Black Pig. We also cloned myostatin propeptide cDNA, and to construct porcine myostatin propeptide expression vector, and to transfer expression vector into yeast cells to generate recombinant myostatin propeptide, and to apply it to improve growth performance and carcass characters of TLRI No. 1 black pigs. In animal test, we formulated the corn-soybean basal diet blended with 0.5 or 1.0 mg/kg of recombinant myostatin propeptide. The blended recombinant misstating protein (1.0mg/kg) could increase gain weight and feed intake, but there were not a significant difference on carcass characters of TLRI black pigs. Therefore, we may conclude that addition of 1.0mg/kg recombinant myostatin propeptide could improve gain weight and feed intake of TLRI black pigs. In the meanwhile the lean and bone percentage showed a trend while the amount of recombinant myostatin propeptide increased from 0.5 to 1.0mg/kg, but there were no effect on chemical assessment of longissimus dorsi and small tenderloin, and belly muscle.
URI: http://hdl.handle.net/11455/22798
其他識別: U0005-2910200822303200
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