Expression of contractile protein-encoding genes TPM2 and TNNT3 during ontogenesis in pigs raised in Poland

• Autorzy: Rozycki M. , Piorkowska K. , Oczkowicz M.
• Języki publikacji: EN

Abstrakty

EN

Troponin is a regulatory proteins complex composed of subunits TnC, TnI, and TnT encoded by separate genes – TNNT1, TNNT2 and TNNT3. It is a component of thin filaments (along with actin and tropomyosin), to which calcium binds to accomplish this regulation. The TPM2 gene encodes beta-tropomyosin. An imprinted QTL for muscle mass deposition has been detected near the TNNT3 gene and several significant linkages between TPM2 and QTLs on chromosome 1 have been identified. However, no significant correlation was found between polymorphism in both genes and economically important pig traits. The study aimed at analysing the level of expression of TNNT3 and TPM2 in the developing muscle (day 60-210 of life) and determining the expression differences among Polish Large White, Polish Landrace, Pulawska, Duroc and Pietrain pigs. Within the mentioned period the expression level of both genes in question did not change significantly. No developmental pattern characteristic for all breeds was revealed. In PL gilts a highly significant correlation was found among the level of expression in both white muscles (longissimus dorsi and semimembranosus) and the animals’ maternal origin. The above results suggest that an unknown polymorphism, probably located in regulatory part of the gene has an effect on the level of TNNT3 expression. Expression of the TPM2 did not change during ontogenesis and was not correlated with maternal origin. However, significant differences among gilts of different breeds were identified.

Słowa kluczowe

EN

gene expression; protein-encoding gene; TPM2 gene; TNNT3 gene; ontogenesis; pig; muscle development; animal breed; Poland

• Wydawca: -
• Czasopismo: Animal Science Papers and Reports
• Rocznik: 2011
• Tom: 29
• Numer: 1
• Opis fizyczny: p.65-74,fig.,ref.

Twórcy

autor

Rozycki M.

• Department of Genetics and Animal Breeding, National Research Institute of Animal Production, Krakowska 1, 32-083 Balice, Poland

autor

Piorkowska K.

autor

Oczkowicz M.

Bibliografia

• BRYM P., KAMIŃSKI S., 2006 – Database of SNPs in candidate genes potentially associated with yield and quality of pork. Animal Science Papers and Reports 24 (3), 239-257.
• CHAUDHURI T., MUKHERJEA M., SACHDEV S., RANDALL J.D., SARKAR S., 2005 – Role of the fetal and α/β exons in the function of fast skeletal troponin T isoforms: correlation with altered Ca2+ regulation associated with development. Journal of Molecular Biology 325. 58-71.
• CHOMCZYŃSKI P., 1993 – A reagent for the single-step simultaneous isolation of RNA, DNA and protein from cell and tissue sample. Bio Techniques 15, 532-537
• CHRISTENSEN M., HENCKEL P., PURSLOW P.P., 2004 – Effect of muscle type on the rate of post-mortem proteolysis in pigs. Meat Science 66 (3), 595-601.
• DAVOLI R., FONTANESI L., ZAMBONELLI P., BIGI D., GELLIN J., YERLE M., MILC J.,BRAGLIA S., CENCI V., CAGNAZZO M., RUSSO V., 2002 – Isolation of porcine expressed sequence tags for the construction of the first genomic transcript map of the skeletal muscle in pig.Animal Genetics 33, 3-18.
• DAVOLI R., FONTANESI L., BRAGLIA S., RUSSO V., 2003 – The porcine fast skeletal muscle troponin T3 (TNNT3) gene: identification of mutations and linkage mapping to chromosome 2.Animal Genetics 34, 391-392.
• FARAH C.S. REINACH F.C. 1995 – The troponin complex and regulation of muscle contraction FASEB Journal 9, 755-767.
• FIRULLI A.B., OLSON E.N., 1997 – Modular regulation of muscle gene transcription: a mechanism for muscle cell diversity. Trends in Genetics 13, 364-369.
• GONG H., HATCH V., LECHMAN W., GRAIG R. TOBACMAN L.S., 2005 – Mini-thin filaments regulated by troponin-tropomyosin. Proceedings of the National Academy of Sciences of the USA 102 (3), 656-661.
• GORDON A.M., HOMSHER E., REGNIER M., 2000 – Regulation of contraction in striated muscle.Physiological Reviews 80(2), 853-924.
• GRABAREK Z. 2001 – Mechanizmy regulacji skurczu mięśni prążkowanych, „Mechanisms of regulation of striated muscle contraction”. Kosmos 4, 349-358.
• JIN J.P., BROTTO M.A., HOSSAIN M.M., HUANG Q.Q., BROTTO L.S., NOSEK T.M., MORTON D.H., CRAWFORD T.O. 2003 – Truncation by Glu180 nonsense mutation results in complete loss of slow skeletal muscle troponin T in a lethal nemaline myopathy. Journal of Biological Chemistry 278(28), 26159-26165.
• Kim K.S., Sherwood J., Ciobanu D.C., Zhang Y.D. and Rothschild M.F. 2001 – Mapping and investigation of two novel candidate genes for growth and meat quality traits in the pig. Swine Research Report, Iowa State University (AS-644).
• KITAMURA S., MUROYA S., TANABE S., OKUMURA T., CHIKUNI K., NISHIMURA T., 2005 – Mechanism of production of troponin T fragments during postmortem aging of porcine muscle. Journal of Agricultural and Food Chemistry 53, 4178- 4181.
• LIU G. 2005 – Detection and characterization of QTL in a porcine Duroc-Pietrain resource population,Cuvillier Verlag, , ISBN 3865376576, 9783865376572, 134
• MAO C., BAUMGARTNER A.P., JHA P.K., HUANG T.H.-M. SARKAR S. 1996 – Assignment of the human fast skeletal troponin T gene (TNNT3) to chromosome 11p15.5: evidence for the presence of 11pter in a monochromosome 9 somatic cell hybrid in NIGMS Mapping Panel 2. Genomics 31,385-388.
• MILEWSKA W., 2006 – Production traits of Polish Large White sows kept in breeding herds in the Warmia and Mazury region in the years 1998-2002. Animal Science Papers and Reports 24,Supplement 1, 103-112.
• PERRY S.V., 1998 – Troponin T: genetics, properties and function. Journal of Muscle Research and Cell Motility 19, 575-602.
• SHERWOOD J., CIOBANU D., ROTHSCHILD M.F., 2002 – Rapid communication: mapping of the beta Tropomyosin (TPM2) gene to pig chromosome 1. Journal of Animal Science 80, 1379-1380.
• STEFANCSIK R., RANDALL J.D., MAO CH. SARKAR S. 2003 – Structure and sequence of human fast skeletal troponin T (TNNT3) gene: insight into the evolution of the gene and the origin of the developmentally regulated isoforms. Comparative and Functional Genomics , 4, 609-625.
• STRYER L., 1997 – Biochemia (Biochemistry). In Polish. Wydawnictwo Naukowe PWN,Warszawa.
• SZYNDLER-NĘDZA M., BLICHARSKI T., BAJDA Z., 2008 – Świnie puławskie – uwarunkowania kształtujące wielkość populacji w latach 1932–2007. Wiadomości Zootechniczne XLVI, 4, 37-40.
• Tang Z., Li Y., Wan P., Li X., Zhao S., Liu B., Fan B., Zhu M., Yu M., Li K., 2007 – LongSAGE analysis of skeletal muscle at three prenatal stages in Tongcheng and Landrace pigs. Genome Biology; 8(6), R115.
• VAN LAERE A.S, NGUYEN M., BRAUNSCHWEIG M,, NEZER C., COLLETTE C., MOREAU L., ARCHIBALD A.L., HALEY C.S., BUYS N., TALLY M., ANDERSSON G., GEORGES M.,ANDERSSON L., 2003 – A regulatory mutation in IGF2 causes a major QTL effect on muscle growth in the pig. Nature 425, 832-836.
• WU Q.L., JHA P.K., RAYCHOWDHURY M.K., YAN D.U., LEAVIS P.C., SARKAR S., 1994 – Isolation and characterization of human fast skeletal β-troponin T cDNA: comparative sequence analysis of isoforms and insight into the evolution of members of multigene family. DNA and Cell Biology, 13, 217-233.
• YUAN L., QIAN N., TYCKO B., 1996 – An extended region of biallelic gene expression and rodenthuman synteny downstream of the imprinted H19 gene on chromosome 11p.15.5. Human Molecular Genetics 12, 1931-1937.