Research Progress on SOCS3 Regulation of Dairy Cow Lactation Signal Pathway
Abstract
Suppressor of cytokine signaling 3 (SOCS3) is a cytokine-induced negative regulator of cytokine signaling. There is evidence that it inhibits the activation of signal transducers and activators of transcription 5 (STAT5), and the Janus kinase 2-signal transducer and activator of transcription 5 (JAK2-STAT5) signaling pathway plays a role in the transcriptional synthesis of milk proteins in dairy cows. And the expression of SOCS3 has an inhibitory effect o n the synthesis of SREBP-1c gene and fatty acids. Therefore, this paper reviews the effects of the structure and function of SOCS3 on the lactation signaling pathway of dairy cows, and aims to provide constructive suggestions for further increasing the milk protein content in milk through manual intervention.
Keywords
Full Text:
PDFReferences
Zhou Y, Song F, Li Y S, et al. Double-antibody based immunoassay for the detection of β-casein in bovine milk samples. Food Chemistry, 2013, 141(1):167-173.
Berit C, Rottenberg M E. SOCS3, a Major Regulator of Infection and Inflammation. Frontiers in Immunology, 2014, 5(5):58.
Tregove M C, ward A C. SOCS proteins in development and disease. Am J Clin Exp, Immunol, 2013, 2: 1- 29.
Martínez-Caselles A, Pons-Miñano J A, Vargas-Acosta Á, et al. Hepatoportal sclerosis clinical different evolutionary stages: presentation of 3 cases and literature review. Revista Espanola De Enfermedades Digestivas, 2012, 104(2):94.
Huang Y L, Zhao F, Luo C C, et al. SOCS3-mediated blockade reveals major contribution of JAK2 STAT5 signaling pathway to lactation and proliferation of dairy cow mammary epithelial cells in vitro. Molecules, 2013, 18(10):12987-13002.
Udy G B, Towers R P, Snell R G, et al. Requirement of STAT5b for sexual dimorphism of body growth rates and liver geneexpression. Proceedings of the National Academy of Sciences of the United States of America, 1997, 94(14):7239-7244.
Shi Linlin. JAK2-STAT5 and mTOR signal pathway cooperatively regulate milk protein synthesis Harbin :Northeast Agricultural University, 2013.
White C A, Nicola N A. SOCS3: An essential physiological inhibitor of signaling by interleukin-6 and G-CSF family cytokines. JAKSTAT. 2013, 2(4):e25045-e25045.
Singh K, Vetharaniam I, Dobson J M, et al. Cell survival signaling in the bovine mammary gland during the transition from lactation to involution. Journal of Dairy Science, 2016, 99(9):7523-7543.
Pujhari S, Kryworuchko M, Zakhartchouk A N. Role of phosphatidylinositol-3-kinase (PI3K) and the mammalian target of rapamycin (mTOR) signalling pathways in porcine reproductive and respiratory syndrome virus (PRRSV) replication. Virus Research, 2014, 194(1):138-144.
Proud C G. Amino acids and mTOR signalling in anabolic function. Biochemical Society Transactions, 2007, 35(5):1187-1190.
Beugnet A, Tee A R, Taylor P M, et al. Regulation of targets of mTOR (mammalian target of rapamycin) signalling by intracellular amino acid availability. Biochemical Journal, 2003, 372(Pt 2):555.
Burgos S A, Dai M, Cant J P. Nutrient availability and lactogenic hormones regulate mammary protein synthesis through the mammalian target of rapamycin signaling pathway.Journal of Dairy Science, 2010, 93(1):153-161.
Lynch C J. Role of leucine in the regulation of mTOR by amino acids: revelations from structure-activity studies. Journal of Nutrition, 2001, 131(3):861S.
Menzies K K, Macmillan K L, Nicholas K R. Insulin regulates milk protein synthesis at multiple levels in the bovine mammary gland. Functional & Integrative Genomics, 2009, 9(2):197-217.
Nishi M, Kawata M. Dynamics of glucocorticoid receptor and mineralocorticoid receptor: implications from live cell imaging studies. Neuroendocrinology, 2007, 85(3):186-192.
Jr B F, Nicholas K R, Van Wyk J J, et al. Insulin is essential for accumulation of casein mRNA in mouse mammary epithelial cells. Proceedings of the National Academy of Sciences of the United States of America, 1981, 78(9):5682.
Boutet P, Sulon J, Closset R, et al. Prolactin-Induced Activation of Nuclear Factor κ B in Bovine Mammary Epithelial Cells: Role in Chronic Mastitis. Journal of Dairy Science, 2007, 90(1):155-164.
Sachithanandan N, Fam B C, Fynch S, et al. Liver-specific suppressor of cytokine signaling-3 deletion in mice enhances hepatic insulin sensitivity and lipogenesis resulting in fatt y liver and obesity. Hepatology, 2010, 52(5):1632.
Yoshimura A, Naka T, Kubo M. SOCS proteins, cytokine signalling and immune regulation. Nature Reviews Immunology, 2007, 7(6):454-65.
Robinson G W, Pacherzavisin M, Zhu B M, et al. Socs 3 modulates the activity of the transcription factor Stat3 in mammary tissue and controls alveolar homeostasis. Developmental Dynamics, 2007, 236(3):654-661.
Babon J J, Kershaw N J, Murphy J M, et al. Suppression of Cytokine Signalling by SOCS3: Characterisation of the mode of inhibition and the basis of its specificity. Immunity, 2012, 36(2):239.
Kershaw N J, Murphy J M, Liau N P, et al. SOCS3 binds specific receptor-JAK complexes to control cytokine signaling by direct kinase inhibition. Nature Structural & Molecular Biology, 2013, 20(4):469-476.
Dif F, Saunier E, Demeneix B, et al. Cytokine-inducible SH2-containing protein suppresses PRL signaling by binding the PRL receptor. Endocrinology, 2001, 142(12):5286-5293.
Clarkson R W, Boland M P, Kritikou E A, et al. The genes induced by signal transducer and activators of transcription (STAT)3 and STAT5 in mammary epithelial cells define the roles of these STATs in mammary development. Molecular Endocrinology, 2006, 20(3):675-685.
Wall E H, Auchtungmontgomery T L, Dahl G E, et al. Short communication: Short-day photoperiod during the dry period decreases expression of suppressors of cytokine signaling in mammary gland of dairy cows. Journal of Dairy Science, 2005, 88(9):3145-3148.
Macias H, Hinck L. Mammary gland development. Wiley Interdisciplinary Reviews Developmental Biology, 2012, 1(4):533-557.
Singh K, Vetharaniam I, Dobson J M, et al. Cell survival signaling in the bovine mammary gland during the transition from lactation to involution. Journal of Dairy Science, 2016, 99(9):7523-7543.
Dang H V, Sakai T, Pham T A, et al. Nucling, a Novel Apoptosis-associated Protein, Controls Mammary Gland Involution by Regulating NF-κB and STAT3. Journal of Biological Chemistry, 2015, 290(40):24626-35.
Feng J, Witthuhn B A, Matsuda T, et al. Activation of Jak2 catalytic activity requires phosphorylation of Y1007 in the kinase activation loop. Molecular & Cellular Biology, 1997, 17(5):2497-501.
Brantley D M, Yull F E, Muraoka R S, et al. Dynamic expression and activity of NF-kappaB during post-natal mammary gland morphogenesis. Mechanisms of Development, 2000, 97(1):149-155.
Connelly L, Barham W, Pigg R, et al. Activation of nuclear factor kappa B in mammary epithelium promotes milk loss during mammary development and infection. Journal of Cellular Physiology, 2010, 222(1):73-81.
Monowar A, Asha J, Akihisa M, et al. Pre-Treatment of Recombinant Mouse MFG-E8 Downregulates LPS-Induced TNF-α Production in Macrophages via STAT3-Mediated SOCS3 Activation. Plos One, 2011, 6(11):e27685.
Günther J, Esch K, Poschadel N, et al. Comparative Kinetics of Escherichia coli- and Staphylococcus aureus-Specific Activation of Key Immune Pathways in Mammary Epithelial Cells Demonstrates That S. aureus Elicits a Delayed Response Dominated by Interleukin-6 (IL-6) but Not by IL-1A or Tumor Ne. Infection & Immunity, 2011, 79(2):695.
Liu B, Zhang N, Liu Z, et al. RP105 involved in activation of mouse macrophages via TLR2 and TLR4 signaling. Molecular & Cellular Biochemistry, 2013, 378(1-2):183-193.
Tuaillon E, Cambonie G, Viljoen J, et al. Subclinical mastitis occurs frequently in association with dramatic changes in inflammatory anti-inflammatory breast milk components. Pediatric Research, 2016, 81(4):556.
Matsunaga K, Tsugami Y, Kumai A, et al. IL-1β directly inhibits milk lipid production in lactating mammary epithelial cells concurrently with enlargement of cytoplasmic lipid droplets. experimental cell research. 2018, 370(2):365-372.
Casey T M, Plaut K. The Role of Glucocorticoids in Secretory Activation and Milk Secretion, a Historical Perspective. Journal of Mammary Gland Biology & Neoplasia, 2007, 12(4):293-304.
Dong B, Zhao F Q. Involvement of the ubiquitous Oct-1 transcription factor in hormonal induction of beta-casein gene expression. Biochemical Journal, 2007, 401(1):57-64.
Khatib H, Monson R L, Schutzkus V, et al. Mutations in the STAT5A, Gene Are Associated with Embryonic Survival and Milk Composition in Cattle. Journal of Dairy Science, 2008, 91(2):784.
Huang Yuling. SOCS3 inhibits STAT5a signal pathway regulates lactation of cow mammary epithelial cells Harbin: Northeast Agricultural University, 2014.
Barclay J L, Anderson S T, Waters M J, et al. SOCS3 as a tumor suppressor in breast cancer cells, and its regulation by PRL. International Journal of Cancer, 2009, 124(8):1756-1766.
Chueh F Y, Leong K F, Cronk R J, et al. Nuclear localization of pyruvate dehydrogenase complex-E2 (PDC-E2), a mitochondrial enzyme, and its role in signal transducer and activator of transcription 5 (STAT5)-dependent gene transcription. Cellular Signalling, 2011, 23(7):1170-1178.
Wagner K U, Schmidt J W. The two faces of Janus kinases and their respective STATs in mammary gland development and cancer. Journal of Carcinogenesis, 2011, 10(1):32.
Peterson T R, Sengupta S S, Harris T E, et al. mTOR complex 1 regulates lipin 1 localization to control the SREBP pathway. Cell, 2011, 146(3):408.
DOI: https://doi.org/10.18686/pas.v2i1.1312
Refbacks
- There are currently no refbacks.
