Cloning of Japanese Quail (Coturnix japonica) Follistatin and Production of Bioactive Quail Follistatin288 in Escherichia coli
DOI:
https://doi.org/10.3923/ijps.2018.8.21Keywords:
Cloning of quail, meat-animal, muscle growth, Quail follistatin, myostatinAbstract
Background and Objective: Follistatin (FST) is a cysteine-rich autocrine glycoprotein and plays an important role in mammalian prenatal and postnatal development. The FST binds to and inhibits myostatin (MSTN), a potent negative regulator of skeletal muscle growth, thus FST abundance enhances muscle growth in animals. The objective of this study was to determine cDNA sequence of quail FST and to produce biologically active quail FST288 (qFST288) in an Escherichia coli (E. coli) expression system. Materials and Methods: Total RNA isolated from quail ovary tissue was used in performing 3'-and 5'-RACE to determine the full-length mRNA sequence of quail FST. The full-length quail FST cDNA consisted of 1118 bp with an open reading frame (ORF) of 1032 bp. The qFST amino acid sequence deduced from qFST cDNA was identical to chicken FST except the sequence at 28 position. To produce recombinant qFST288 protein, Gibson assembly cloning method was used to insert the DNA fragments of qFST288 into pMALc5x vector downstream of the maltose-binding protein (MBP) gene and the plasmids containing the inserts were eventually transformed into shuffle E. coli strain for protein expression. Results: Soluble expression of the qFST288 protein was achieved through the experiments and the protein could be easily purified by the combination of amylose and heparin resin affinity chromatography. In an in vitro reporter gene assay, MBP-qFST288 demonstrated its capacity to suppress the activities of MSTN or activin A. Conclusion: Through cloning of quail FST cDNA, it was discovered that amino acid sequence of quail FST is identical to that of chicken FST. In addition, it was demonstrated that bioactive qFST288 could be produced in E. coli.
References
Webster, A.J.F., 1977. Selection for leanness and the energetic efficiency of growth in meat animals. Proc. Nutr. Soc., 36: 53-59.
Lee, S.J., 2004. Regulation of muscle mass by myostatin. Annu. Rev. Cell Dev. Biol., 20: 61-86.
McPherron, A.C., A.M. Lawler and S.J. Lee, 1997. Regulation of skeletal muscle mass in mice by a new TGF-β superfamily member. Nature, 387: 83-90.
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.
Grobet, L., D. Pirottin, F. Farnir, D. Poncelet and L.J. Royo et al., 2003. Modulating skeletal muscle mass by postnatal, muscle‐specific inactivation of the myostatin gene. Genesis, 35: 227-238.
Lee, S.J. and A.C. McPherron, 2001. Regulation of myostatin activity and muscle growth. Proc. Natl. Acad. Sci. USA., 98: 9306-9311.
Morine, K.J., L.T. Bish, K. Pendrak, M.M. Sleeper, E.R. Barton and H.L Sweeney, 2010. Systemic myostatin inhibition via liver-targeted gene transfer in normal and dystrophic mice. Plos One, Vol. 5.
Tang, L., Z. Yan, Y. Wan, W. Han and Y. Zhang, 2007. Myostatin DNA vaccine increases skeletal muscle mass and endurance in mice. Muscle Nerve, 36: 342-348.
Kim, Y.S., N.K. Bobbili, K.S. Paek and H.J. Jin, 2006. Production of a monoclonal anti-myostatin antibody and the effects of in ovo administration of the antibody on posthatch broiler growth and muscle mass. Poult. Sci., 85: 1062-1071.
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. Qiu, R.M. Hewick and N.M. Wolfman, 2003. Regulation of myostatin in vivo by growth and differentiation factor-associated serum protein-1: A novel protein with protease inhibitor and follistatin domains. Mol. Endocrinol., 17: 1144-1154.
Gilson, H., O. Schakman, S. Kalista, P. Lause, K. Tsuchida and J.P. Thissen, 2009. Follistatin induces muscle hypertrophy through satellite cell proliferation and inhibition of both myostatin and activin. Am. J. Physiol. Endocrinol. Metabolism, 297: E157-E164.
Haidet, A.M., L. Rizo, C. Handy, P. Umapathi and A. Eagle et al., 2008. Long-term enhancement of skeletal muscle mass and strength by single gene administration of myostatin inhibitors. Proc. Nat. Acad. Sci., 105: 4318-4322.
Kota, J., C.R. Handy, A.M. Haidet, C.L. Montgomery and A. Eagle et al., 2009. Follistatin gene delivery enhances muscle growth and strength in nonhuman primates. Sci. Translational Med., Vol. 1.
Nakatani, M., Y. Takehara, H. Sugino, M. Matsumoto and O. Hashimoto et al., 2008. Transgenic expression of a myostatin inhibitor derived from follistatin increases skeletal muscle mass and ameliorates dystrophic pathology in mdx mice. FASEB J., 22: 477-487.
Medeiros, E.F., M.P. Phelps, F.D. Fuentes and T.M. Bradley, 2009. Overexpression of follistatin in trout stimulates increased muscling. Am. J. Physiol.-Regul. Integr. Comparat. Physiol., 297: R235-R242.
Connolly, D.J., K. Patel, E.A.P. Seleiro, D.G. Wilkinson and J. Cooke, 1995. Cloning, sequencing and expressional analysis of the chick homologue of follistatin Genesis, 17: 65-77.
Altschul, S.F., T.L. Madden, A.A. Schäffer, J. Zhang, Z. Zhang, W. Miller and D.J. Lipman, 1997. Gapped BLAST and PSI-BLAST: A new generation of protein database search programs. Nucl. Acids Res., 25: 3389-3402.
Larkin, M.A., G. Blackshields, N.P. Brown, R. Chenna and P.A. McGettigan et al., 2007. Clustal W and clustal X version 2.0. Bioinformatics, 23: 2947-2948.
Lee, S.B., R. Choi, S.K. Park and Y.S. Kim, 2014. Production of bioactive chicken follistatin315 in Escherichia coli. Applied Microbiol. Biotechnol., 98: 10041-10051.
Gibson, D.G., L. Young, R.Y. Chuang, J.C. Venter, C.A. Hutchison III and H.O. Smith, 2009. Enzymatic assembly of DNA molecules up to several hundred kilobases. Nat. Methods, 6: 343-345.
Laemmli, U.K., 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227: 680-685.
Cash, J.N., E.B. Angerman, C. Kattamuri, K. Nolan and H. Zhao et al., 2012. Structure of Myostatin• Follistatin-like 3 N-terminal domains of follistatin-type molecules exhibit alternate modes of binding. J. Biol. Chem., 287: 1043-1053.
Shimasaki, S., M. Koga, F. Esch, K. Cooksey and M. Mercado et al., 1988. Primary structure of the human follistatin precursor and its genomic organization. Proc. Nat. Acad. Sci., 85: 4218-4222.
Schneyer, A.L., Q. Wang, Y. Sidis and P.M. Sluss, 2004. Differential distribution of follistatin isoforms: Application of a new FS315-specific immunoassay. J. Clin. Endocrinol. Metab., 89: 5068-5075.
Sugino, K., N. Kurosawa, T. Nakamura, K. Takio and S. Shimasaki et al., 1993. Molecular heterogeneity of follistatin, an activin-binding protein. Higher affinity of the carboxyl-terminal truncated forms for heparan sulfate proteoglycans on the ovarian granulosa cell. J. Biol. Chem., 268: 15579-15587.
Kimura, F., Y. Sidis, L. Bonomi, Y. Xia and A. Schneyer, 2009. The follistatin-288 isoform alone is sufficient for survival but not for normal fertility in mice. Endocrinology, 15: 1310-1319.
Inouye, S., Y. Guo, L. Depaolo, M. Shimonaka, N. Ling and S. Shimasaki, 1991. Recombinant expression of human follistatin with 315 and 288 amino acids: Chemical and biological comparison with native porcine follistatin. Endocrinology, 129: 815-822.
Hashimoto, O., N. Kawasaki, K. Tsuchida, S. Shimasaki, T. Hayakawa and H. Sugino, 2000. Difference between follistatin isoforms in the inhibition of activin signalling: Activin neutralizing activity of follistatin isoforms is dependent on their affinity for activin. Cell. Signall., 12: 565-571.
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