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Association of a genetic marker at the bovine Janus kinase 2 locus (JAK2/RsaI) with milk production traits of four cattle breeds

Published online by Cambridge University Press:  29 June 2015

Małgorzata Szewczuk
Małgorzata Szewczuk*
Affiliation:
Department of Ruminant Science, The West Pomeranian University of Technology, Szczecin, Poland
*
*For correspondence; e-mail: [email protected]
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Abstract

In addition to the main components of the somatotrophic axis (GH/GHR/IGF-I/IGF-IR), great importance in the control of growth and development is also attached to the Janus kinase 2 (JAK2) pathway. Induced by the GH/GHR complex, JAK2 activates signal transducer and activator of transcription 5 (STAT5), and in consequence, may be involved in the regulation of expression of insulin-like growth factor I (IGF-I) in the mammary gland. Silent mutation (rs110298451) has been identified within exon 20 using polymerase chain reaction-restriction fragment length polymorphism (PCR-RFLP). A total of 904 individuals of four dairy or dual-purpose breeds (Polish Holstein-Friesian, Montbeliarde, Simmental and Jersey) were genotyped. A genotypic imbalance in the populations was observed. In the case of dual-purpose breeds (Montbeliarde and Simmental), the frequencies of both alleles were almost equal. In contrary, the JAK2G allele was predominant in the Polish Holstein-Friesian breed while JAK2A allele in Jersey. A pronounced relationship between JAK2/RsaI polymorphism and milk production traits was found where, irrespective of breed and lactation order, the GG genotype was significantly associated with higher milk, protein and fat yields, as compared to the AA genotype. Heterozygous individuals were generally characterised by intermediate values of the analysed milk traits. It can be argued that the JAK2 gene polymorphism is a potential marker for milk production traits. However, due to the fact that rs110298451 SNP does not directly affect amino acid sequence, other association studies involving missense mutation should also be performed.

Keywords

Cattle breedsJAK2SNPtyrosine kinase
Type
Research Article
Information
Journal of Dairy Research , Volume 82 , Issue 3 , August 2015 , pp. 287 - 292
Copyright
Copyright © Proprietors of Journal of Dairy Research 2015 

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References

Argetsinger, LS & Carter-Su, C 1996 Mechanism of signaling by growth hormone receptor. Physiological Reviews 76 1089–1107CrossRefGoogle ScholarPubMed
Argetsinger, LS, Kouadio, J-LK, Steen, H, Stensballe, A, Jensen, ON & Carter-Su, C 2004 Autophosphorylation of JAK2 on tyrosines 221 and 570 regulates its activity. Molecular and Cellular Biology 24 4955–4967CrossRefGoogle ScholarPubMed
Argetsinger, LS, Stuckey, JA, Robertson, SA, Koleva, RI, Cline, JM, Marto, JA, Myers, MG Jr. & Carter-Su, C 2010 Tyrosines 868, 966, and 972 in the kinase domain of JAK2 are autophosphorylated and required for maximal JAK2 kinase activity. Molecular Endocrinology 24 1062–1076CrossRefGoogle ScholarPubMed
Babon, JJ, Lucet, IS, Murphy, JM, Nicola, NA & Varghese, LN 2014 The molecular regulation of Janus kinase (JAK) activation. Biochemical Journal 462 1–13CrossRefGoogle ScholarPubMed
Blüher, S, Kratzsch, J & Kiess, W 2005 Insulin-like growth factor-I, growth hormone and insulin in white adipose tissue. Best Practice & Research Clinical Endocrinology & Metabolism 19 577–587CrossRefGoogle ScholarPubMed
Denley, A, Cosgrove, LJ, Booker, GW, Wallace, JC & Forbes, BE 2005 Molecular interactions of the IGF system. Cytokine & Growth Factor Reviews 16 421–439CrossRefGoogle ScholarPubMed
Etherton, TD & Bauman, DE 1998 Biology of somatotropin in growth and lactation of domestic animals. Physiological Reviews 78 745–761CrossRefGoogle ScholarPubMed
Feener, EP, Rosario, F, Dunn, SL, Stancheva, Z & Myers, MG Jr 2004 Tyrosine phosphorylation of Jak2 in the JH2 domain inhibits cytokine signaling. Molecular and Cellular Biology 24 4968–4978CrossRefGoogle ScholarPubMed
Feng, J, Witthuhn, BA, Matsuda, T, Kohlhuber, F, Kerr, IM & Ihle, JN 1997 Activation of Jak2 catalytic activity requires phosphorylation of Y1007 in the kinase activation loop. Molecular and Cellular Biology 17 2497–2501CrossRefGoogle ScholarPubMed
Funakoshi-Tago, M, Pelletier, S, Matsuda, T, Parganas, E & Ihle, JN 2006 Receptor specific down regulation of cytokine signaling by autophosphorylation in the FERM domain of Jak2. The EMBO Journal 25 4763–4772CrossRefGoogle Scholar
Funakoshi-Tago, M, Pelletier, S, Moritake, H, Parganas, E & Ihle, JN 2008a Jak2 FERM domain interaction with the erythropoietin receptor regulates Jak2 kinase activity. Molecular and Cellular Biology 28 1792–1801CrossRefGoogle ScholarPubMed
Funakoshi-Tago, M, Tago, K, Kasahara, T, Parganas, E & Ihle, JN 2008b Negative regulation of Jak2 by its auto-phosphorylation at tyrosine 913 via the Epo signaling pathway. Cellular Signalling 20 1995–2001CrossRefGoogle ScholarPubMed
Godeny, MD, Sayyah, J, Vonderlinden, D, Johns, M, Ostrov, DA, Caldwell-Busby, J & Sayeski, PP 2007 The N-terminal SH2 domain of the tyrosine phosphatase, SHP-2, is essential for Jak2-dependent signaling via the angiotensin II type AT1 receptor. Cellular Signalling 19 600–609CrossRefGoogle ScholarPubMed
Herrington, J & Carter-Su, DC 2001 Signaling pathways activated by the growth hormone receptor. Trends in Endocrinology & Metabolism 12 252–257CrossRefGoogle ScholarPubMed
Kurzer, JH, Argetsinger, LS, Zhou, YJ, Kouadio, J-LK, O'She, JJ & Carter-Su, C 2004 Tyrosine 813 is a site of JAK2 autophosphorylation critical for activation of JAK2 by SH2-B. Molecular and Cellular Biology 24 4557–4570CrossRefGoogle ScholarPubMed
McDoom, I, Xianyue, M, Kirabo, A, Kuang-Yung, L, Ostrov, DA & Sayeski, PP 2008 Identification of tyrosine 972 as a novel site of Jak2 tyrosine kinase phosphorylation and its role in Jak2 activation. Biochemistry 47 8326–8334CrossRefGoogle ScholarPubMed
Polish Federation of Cattle Breeders & Dairy Farmers (PFCB&DF) 2014 The Results of Milk Recording in Poland in 2013. Warszawa: Wydaw PFHBiPMGoogle Scholar
Renaville, R, Hammadi, M & Portetelle, D 2002 Role of the somatotropic axis in the mammalian metabolism. Domestic Animal Endocrinology 23 351–360CrossRefGoogle ScholarPubMed
Robertson, SA, Koleva, RI, Argetsinger, LS, Carter-Su, C, Marto, JA, Feener, EP & Myers, MG Jr 2009 Regulation of Jak2 function by phosphorylation of Tyr317 and Tyr637 during cytokine signaling. Molecular and Cellular Biology 29 3367–3378CrossRefGoogle ScholarPubMed
Silvennoinen, O, Ungureanu, D, Niranjan, Y, Hammaren, H, Bandaranayake, R & Hubbard, SR 2013 New insights into the structure and function of the pseudokinase domain in JAK2. Biochemical Society Transactions 41 1002–1007CrossRefGoogle ScholarPubMed
Sun, Z, Shushanov, S, LeRoith, D & Wood, TL 2011 Decreased IGF type 1 receptor signaling in mammary epithelium during pregnancy leads to reduced proliferation, alveolar differentiation, and expression of Insulin Receptor Substrate (IRS)-1 and IRS-2. Endocrinology 152 3233–3245CrossRefGoogle ScholarPubMed
Walden, PD, Ruan, W, Feldman, M & Kleinberg, DL 1998 Evidence that the mammary fat pad mediates the action of growth hormone in mammary gland development. Endocrinology 139 659–662CrossRefGoogle ScholarPubMed
Wolf, A, Eulenfeld, R, Gäbler, K, Rolvering, C, Haan, S, Behrmann, I, Denecke, B, Haan, C & Schaper, F 2013 JAK2-V617F-induced MAPK activity is regulated by PI3 K and acts synergistically with PI3 K on the proliferation of JAK2 V617F-positive cells. JAK-STAT 2 e24574-1–13CrossRefGoogle Scholar