Advanced SearchSearch Tips
Expression Analysis of Galectin-1 from Fat in Berkshire Pigs
facebook(new window)  Pirnt(new window) E-mail(new window) Excel Download
 Title & Authors
Expression Analysis of Galectin-1 from Fat in Berkshire Pigs
Jung, Won Yong; Cho, Eun Seok; Kwon, Eun Jung; Park, Da Hye; Chung, Ki Hwa; Kim, Chul Wook;
  PDF(new window)
Galectins are a group of animal lectins consisting of galectin-type carbohydrate recognition domains (CRD) with relatively minor domains. The biological properties of galectins include the regulation of inflammation, intercellular adhesion, cell differentiation and cell death. The diverse kinds of galectin suggest variety in their biological roles. Galectin-1 is released during adipocyte differentiation and is associated with fat which is one of the important factors for meat quality. To verify expression level, a 0.5 kb clone of galectin-1 was obtained from cDNA prepared from back fat tissue of a Sancheong Berkshire pig with good quality meat, and the galectin-1 gene identified. The deduced amino acid sequence of the galectin-1 gene was compared with those obtained from other species. By using RT-PCR and Real time-PCR, an attempt was made to determine the expression level of galectin-1 and to compare with various tissues (tenderloin and back fat) taken from pigs in different groups. Grouping of pigs was based on growth-stage (weighing 60, 80, and 110 kg) and the sub-speciation (Yorkshire and Sancheong Berkshire pigs). We attempted to determine influences of pig species, growth stages and tissue variations on the expression level of the galectin-l gene and it was revealed that the expression pattern of the galectin-1 gene was significantly different (p<0.01 or p<0.05). Galectin-1 genes were expressed more highly in the back fat tissues of pigs weighing 110 kg than in those weighing 60 kg or 80 kg. However, the lowest expression was seen in the tenderloin tissues of pigs weighing 110 kg. Sancheong Berkshire pigs showed higher expression of the galectin-1 gene compared to Yorkshire pigs. Accordingly, it is considered that the expression pattern of the galectin-1 gene influences the growth of back fat tissues and the pig speciation relationship. Previous studies suggested that different expression of galectin-1 genes represents variety among the breeds and is closely related to fat tissue growth, conjugation and catabolism. Further, this study suggests that the expression of galectin-1 at a specific growth stage and tissue contributes significantly to the overall meat quality of Sancheong Berkshire pigs.
Galectin-1;Back Fat;Sancheong Berkshire;RT-PCR;Meat Quality;
 Cited by
Barondes, S. H., D. N. W. Cooper, M. A. Gitt and H. Leffler. 1994. Galectins: structure and function of a large family of animal lectins. J. Bio. Chem. 269:20807-20810.

Barondes, S. H., V. Castronovo, D. N. W. Cooper, R. D. Cummings, K. Drickamer, T. Feizi, M. A. Gitt, J. Hirabayashi, C. Hughes, K. Kasai, H. Leffler, F. Liu, R. Lotan, A. M. Mercurio, M. Monsigni, S. Pillai, F. Poirer, A. Raz, P. W. J. Rigby, J. M. Rini and J. L. Wang. 1994. Galectins: a family of animal beta-galactoside-binding lectins. Cell 76:597-598. crossref(new window)

Colnot, C., D. Fowlis, M. A. Ripoche, I. Bouchaert and F. Poirier. 1998. Embryonic implantation in galectin 1/galectin 3 double mutant mice. Dev. Dyn. 11:306-313.

Colnot, C., M. A. Ripoche, F. Scaerou, D. Foulis and F. Poirier. 1996. Galectins in mouse embryogenesis. Biochem. Soc. Trans. 24:141-146. crossref(new window)

Gitt, M. A. and S. H. Barondes. 1986. Evidence that a human soluble beta-galactoside-binding lectin is encoded by a family of genes. Proc. Nat. Acad. Sci. 3:7603-7607.

Hirabayashi, J. and K. Kasai. 1993. The family of metazoan metal-independent $\beta$-galactoside-bing lectins: structure, function and molecular evolution. Glycobiol. 3:297-304. crossref(new window)

Hughes, R. C. 2004. Galectins in kidney development. Glycoconjugate J. 19:612-629.

Kasi, K. and J. Hirabayashi. 1996. Galectins: a family of animal lectins that decipher glycocodes. J. Biochem. 119:1-8. crossref(new window)

Kim, C. W., K. T. Chang, Y. H. Hong, E. J. Kwon, W. Y. Jung, K. K. Cho, K. W. Chung, B. W. Kim, J. G. Lee, J. S. Yeo, Y. S. Kang and Y. K. Joo. 2005. Screening of specific genes expressed in the swine tissues and development of a functional cDNA chip. Asian-Aust. J. Anim. Sci. 18(7):933-941. crossref(new window)

Leffler, H., S. Carlsson, M. Hedlund, Y. Qian and F. Poirier. 1997. Introduction to galectins. Trends in Glycoscience and Glycotechnology 45:9-19.

Leffler, H., S. Carlsson, M. Hedlund, Y. Qian and F. Poirier. 2004. Introduction to galectins. Glycoconjugate J. 19:433-440.

Liu, F. T., R. J. Patterson and J. L. Wang. 2002. Intracellular functions of galectins. Biochim. Biophys. Acta. 1572:209-231. crossref(new window)

Liu, F. T. 1993. S-type mammalian lectins in allergic inflammation. Immunol. Today. Oct; 14(10):486-490. crossref(new window)

Melissa, A. W., L. R. Susna and K. E. Alan. 2005. Identification of galectin-4 isoforms in porcine small intestine. Biochimie 87:143-149. crossref(new window)

Marcon, P., M. Marsich, V. Vetere, P. Mozetic, C. Campa, I. Donati, F. Vittur, A. Gamini and S. Paoletti. 2005. The role of Galectin-1 in the interaction between chondrocytes and a lactose-modified chitosan. Biomaterials 26:4975-4984. crossref(new window)

Perillo, N. L., M. E. Marcus and L. G. Baum. 1998. Galectins: versatile modulators of cell adhesion, cell proliferation, and cell death. J. Mol. Med. 76:402-412. crossref(new window)

Poirier, F. and E. J. Robertson. 1993. Normal development of mice carrying a null mutation in the gene encoding the L14 S-type lectin. Development 119:1229-1236.

Pieters, R. J. 2006. Inhibiton and Detection of Galectins. Chem. Bio. Chem. 00:1-9. crossref(new window)

Rabinovich, G. A. 1999. Galectins: an evolutionarily conserved family of animal lectins with multifunctional properties; a trip from the gene to clinical therapy. Cell Death Differ 6:711-721. crossref(new window)

Rabinovich, G. A., C. M. Riera, C. A. Landa and C. E. Sotomayor. 1999. Galectins: a key intersection between glycobiology and immunology. Braz. J. Med. Biol. Res. 32:383-393. crossref(new window)

Tadayosi, N. 2003. Organisms in natural features; production of a native black pig. Gyeongsangnam-do pp. 11-21.

Takenaka, Y., T. Fukumori and A. Raz. 2004. Galectin-3 and metastasis. Glycoconjugate J. 19:543-549.

Truong, M. J., V. Gruart, F. T. Liu, L. Prin, A. Capron and M. Capron. 1993. IgE-binding molecules (Mac-2/epsilon BP) expressed by human eosinophils. Implication in IgE-dependent eosinophil cytotoxicity. Eur. J. Immunol. 23:3230-3235. crossref(new window)

Walls, V. and L. Mallucci. 1991. Identification of an auto-crine negative growth factor: mouse beta-galactoside-binding protein in a cytostatic factor and cell growth regulator. Cell 64:91-97. crossref(new window)

Walzel, H., J. Brock, R. Pohland, J. Vanselow, W. Tomek, F. Schneider and U. Tiemann. 2004. Effects of galectin-1 on regulation of progesterone production in granulosa cells from pig ovaries in vitro. Glycobiol. 14(10):871-881. crossref(new window)

Wang, P., E. Mariman, J. Keijer, F. Bouwman, J. P. Noben, J. Robben and J. Renes. 2004. Profiling of the secreted proteins during 3T3-L1 adipocyte differentiation leads to the identification of novel adipokines. Cell. Mol. Life. 61:2405-2417.

Watt, D., G. E. Jones and K. Goldring. 2004. The involvement of galectin-1 in skeletal muscle determination, differentiation and regeneration. Glycoconjugate J. 19:615-619.