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2012 | 30 | 3 |

Tytuł artykułu

cDNA cloning and expression analysis of ATGL gene in four avian species*

Warianty tytułu

Języki publikacji

EN

Abstrakty

EN
Adipose triglyceride lipase (ATGL) is a new key triglyceride-specific lipase that participates in the lipolysis in adipose tissue. The full cDNA of ATGL gene in Chinese francolin, pigeon, bengalessfinch and house sparrow was cloned to reveal its tissue-specific expression by mRNA real time analysis. The obtained cDNA of chinese francolin ATGL gene (cfATGL) was 1465 bp long, and contained 13 bp 5’-untranslated region (5’UTR) and 1452 bp open reading frame (ORF) encoding a 483-amino acid peptide. All the obtained cDNA of pigeon ATGL gene (pATGL), as well as that of bengaless-finch (bfATGL) and house sparrow (hsATGL) was 1459 bp long, including 13 bp 5’UTR and 1446 bp ORF encoding 481 amino acids. The identities of ATGL gene among these birds occurred no less than 88.4% by homology analysis. As indicated by mRNA real time analysis In Chinese francolin tissues, ATGL gene was predominantly expressed in leg muscle, heart and breast muscles of birds of both sexes. In pigeons, ATGL gene was shown to be predominantly expressed In abdominal fat, subcutaneous fat and breast muscle in males, and in subcutaneous fat, leg muscle,heart and abdominal fat in females. In bengaless-finch, very high ATGL mRNA level was found In subcutaneous, heart, breast muscle,abdominal and leg muscle fat in males, and in breast muscle,leg muscle, abdominal and subcutaneous fat in females. In house sparrow, higher ATGL mRNA level was detected in subcutaneous, breast muscle, leg muscle and abdominal fat in males, and in breast muscle, heart and leg muscle fat in females. In conclusion, the ATGL cDNA of Chinese francolin,pigeon, bengaless-finch and house sparrow was obtained and predominantly expressed in adipose,muscle and heart tissues.

Słowa kluczowe

Wydawca

-

Rocznik

Tom

30

Numer

3

Opis fizyczny

p.271-284,fig.,ref.

Twórcy

autor
  • Department of Animal Genetics, Breeding and Reproduction, College of Animal Science, South China Agricultural University, Guangzhou 510642, Guangdong, China
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Bibliografia

  • AKIYAMA M., SAKAI K., OGAWA M., MCMILLAN J.R., SAWAMURA D., SHIMIZU H., 2007 –Novel duplication mutation in the patatin domain of adipose triglyceride lipase (PNPLA2) in neutral lipid storage disease with severe myopathy. Muscle & Nerve 36, 856-885.
  • BRASAEMLE D.L., 2010 – Lipolysis Control: The Plot Thickens. Cell Metabolism 11, 173-174.
  • CUI H., ZAN L., WANG H., LIU H., 2010 – cDNA cloning, sequence analysis and tissue expression of bovine ATGL gene. Acta Veterinaria et Zootechnica Sinica 41, 141-146.
  • DAI L.H., XIONG Y.Z., JIANG S.W., CHEN J.F., 2010 – Molecular characterization and association analysis of porcine adipose triglyceride lipase (PNPLA2) gene. Molecular Biology Reports 2010 May 18. [Epub ahead of print]
  • DEIULIIS J.A., SHIN J., BAE D., AZAIN M.J., BARB R., LEE K., 2008 – Developmental, hormonal, and nutritional regulation of porcine adipose triglyceride lipase (ATGL). Lipids 43, 215-225.
  • DEIULIIS J.A., SHIN J., MURPHY E., KRONBERG S.L., EASTRIDGE M.L., SUH Y., YOON J.T., LEE K., 2010 – Bovine adipose triglyceride lipase is not altered and adipocyte fatty acid-binding protein is increased by dietary flaxseed. Lipids 45, 963-973.
  • FISCHER J., LEFČVRE C., MORAVA E., MUSSINI J. M., LAFORĘT P., NEGRE-SALVAYRE A.,LATHROP M., SALVAYRE, R., 2007 –The gene encoding adipose triglyceride lipase (PNPLA2) is mutated in neutral lipid storage disease with myopathy. Nature Genetics 39, 28-30.
  • HAEMMERLE G., LASS A., ZIMMERMANN R., GORKIEWICZ G., MEYER C., ROZMAN J., HELDMAIER G., MAIER R., THEUSSL C., EDER S., 2006 – Defective lipolysis and altered energy metabolism in mice lacking adipose triglyceride lipase. Science 312, 734-737.
  • HAEMMERLE G., ZIMMERMANN R., HAYN M., THEUSSL C., WAEG G., WAGNER E., SATTLER W., MAGIN T.M., WAGNER E.F., ZECHNER R., 2002 – Hormone-sensitive lipase deficiency in mice causes diglyceride accumulation in adipose tissue, muscle, and testis. Journal of Biological Chemistry 277, 4806-4815.
  • JENKINS C.M., MANCUSO D.J., YAN W., SIMS H.F., GIBSON B., GROSS R.W., 2004 – Identification, cloning, expression, and purification of three novel human calcium-independent phospholipase A2 family members possessing triacylglycerol lipase and acylglycerol transacylase activities. Journal of Bioloical Chemistry 279, 48968-48975.
  • LAKE A.C., SUN Y., LI J.L., KIM J.E., JOHNSON J.W., LI D., REVETT T., SHIH H.H., LIU W.,PAULSEN J.E., GIMENO R.E., 2005 – Expression, regulation, and triglyceride hydrolase activity of Adiponutrin family members. Journal of Lipid Research 46, 2477-2487.
  • LASS A., ZIMMERMANN R., HAEMMERLE G., RIEDERER M., SCHOISWOHL G.,SCHWEIGER M., KIENESBERGER P., STRAUSS J.G., GORKIEWICZ G., ZECHNER R., 2006 – Adipose triglyceride lipase-mediated lipolysisof cellular fat stores is activated by CGI-58 and defective in Chanarin-Dorfman Syndrome. Cell Metabolism 3, 309-319.
  • LEE K., SHIN J., LATSHAW J.D., SUH Y., SERR J., 2009 – Cloning of adipose triglyceride lipase complementary deoxyribonucleic acid in poultry and expression of adipose triglyceride lipase during development of adipose in chickens. Poultry Science 88, 620-630.
  • LI Y.C., ZHENG X.L., LIU B.T., YANG G.S., 2010 – Regulation of ATGL expression mediated by leptin in vitro in porcine adipocyte lipolysis. Molecular Cellular Biochemistry 333, 121-128.
  • LU X., YANG X., LIU J., 2010 – Differential control of ATGL-mediated lipid droplet degradation by CGI-58 and G0S2. Cell Cycle 9, 2719-2725.
  • NIE Q., FANG M., XIE L., SHI J., ZHANG X., 2009 – cDNA cloning, characterization, and variation analysis of chicken adipose triglyceride lipase (ATGL) gene. Molecular Cellular Biochemistry 320,67-74.
  • NIE Q., HU Y., XIE L., ZHANG C., SHEN X., ZHANG X., 2010 – Identification and characterization of adipose triglyceride lipase (ATGL) gene in birds. Molecular Biology Reports 37, 3487-3493.
  • RABEN D.M., BALDASSARE J.J., 2005 – A new lipase in regulating lipid mobilization: hormonesensitive lipase is not alone. Trends in Endocrinology and Metabolism 16, 35-36.
  • SAARELA J., JUNG G., HERMANN M., NIMPF J., SCHNEIDER W.J., 2008 – The patatin-like lipase family in Gallus gallus. BMC Genomics 9, 281.
  • SCHWEIGER M., LASS A., ZIMMERMANN R., EICHMANN T.O., ZECHNER R., 2009 – Neutral lipid storage disease: genetic disorders caused by mutations in adipose triglyceride lipase/PNPLA2 or CGI-58/ABHD5. American Journal of Physiology-Endocrinology and Metabolism 297, E289-E296.
  • SERR J., SUH Y., LEE K., 2009 – Regulation of adipose triglyceride lipase by fasting and refeeding in avian species. Poultry Science 88, 2585-2591.
  • SHAN T., WANG Y., WU T., GUO J., LIU J., FENG J., XU Z., 2008 -Porcine adipose triglyceride lipase gene clone, expression pattern and regulation by resveratrol. Journal of Animal Science 86,1781-1788.
  • VILLENA J.A., ROY S., SARKADI-NAGY E., KIM K.H., SUL H.S., 2004 –-Desnutrin, an adipocyte gene encoding a novel patatin domain-containing protein, is induced by fasting and glucocorticoids:ectopic expression of desnutrin increases triglyceride hydrolysis. Journal of Biological Chemistry 279, 47066-47075.
  • YAMAGUCHI T., 2010 – Crucial Role of CGI-58/ α/β Hydrolase Domain-Containing Protein 5 in Lipid Metabolism. Biological & Pharmaceutical Bulletin 33, 342-345.
  • YANG X., LU X., LOMBČS M., RHA G.B., CHI Y. I., GUERIN T. M., SMART E. J., LIU J., 2010 –The G0 /G1 Switch Gene 2 regulates adipose lipolysis through association with Adipose Triglyceride Lipase. Cell Metabolism 11, 194-205.
  • ZECHNER R., KIENESBERGER P.C., HAEMMERLE G., ZIMMERMANN R., LASS A., 2009 – Adipose triglyceride lipase and the lipolytic catabolism of cellular fat stores. Journal of Lipid Research 50, 3-21.
  • ZIMMERMANN R., STRAUSS J.G., HAEMMERLE G., SCHOISWOHL G., BIRNERGRUENBERGER R., RIEDERER M., LASS A., NEUBERGER G., EISENHABER F, HERMETTER A., ZECHNER R., 2004 – Fat mobilization in adipose tissue is promoted by adipose triglyceride.

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Bibliografia

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