不同时长冷暴露下C2C12细胞中O-GlcNAc和IL-6表达的变化

doi:10.11843/j.issn.0366-6964.2021.023

Abstract

Abstract: Under cold exposure, O-linked β-N-acetylglucosamine (O-GlcNAc) in skeletal muscle increased significantly, and O-GlcNAc, as a "stress receptor", regulated cell signal transduction and gene transcription. Skeletal muscle, as a secretory organ, produces myogenic IL-6 through contraction, which not only plays an immune role but also can regulate the metabolism of glucose and lipid in skeletal muscle. Therefore, the purpose of this study was to detect the expression of O-GlcNAc related protein and cytokine IL-6 in C2C12 under different durations of cold exposure. To explore the potential relationship between O-GlcNAc and IL-6 under of cold exposure. In this experiment, C2C12 was cultured in vitro and randomly divided into control group (37℃±0.5℃) and cold exposure (32℃±0.5℃) 3, 6, 9, and 12 hours treatment group. Western blot was used to detect the glycosylation level of O-GlcNAc and the expression level of OGT, OGA, and IL-6 under different durations of exposure. The results showed that compared with the normal temperature control group, the expression level of OGT was significantly increased (P<0.05) after 3 hours of cold exposure and the expression level of OGA was significantly increased (P<0.05) after 6 hours of cold exposure; the expression level of O-GlcNAc glycosylation and IL-6 were significantly increased (P<0.01) after 3 hours of cold exposure. The expression levels of O-GlcNAc glycosylation and IL-6 in C2C12 cells were significantly increased under different durations of cold exposure. At the same time, the trend of O-GlcNAc glycosylation and IL-6 expression under different durations of cold exposure was highly similar, suggesting that O-GlcNAc glycosylation participated in the regulation of IL-6 expression under cold exposure.

Key words: cold exposure, O-GlcNAc, IL-6, OGT, OGA

CLC Number:

S852.2

HU Yajie, LIU Yang, YAO Ruizhi, SHI Hongzhao, LIU Peng, XU Bin, LÜ Hongming, LI Shize. Variation of O-GlcNAc and IL-6 Expression in C2C12 Cells to Different Durations of Cold Exposure[J]. Acta Veterinaria et Zootechnica Sinica, 2021, 52(1): 219-225.

References 24

[1]	FEBBRAIO M A, PEDERSEN B K. Contraction-induced myokine production and release:is skeletal muscle an endocrine organ?[J]. Exerc Sport Sci Rev, 2005, 33(3):114-119.
[2]	STEENSBERG A. The role of IL-6 in exercise-induced immune changes and metabolism[J]. Exerc Immunol Rev, 2003, 9:40-47.
[3]	PEDERSEN B K, STEENSBERG A, KELLER P, et al. Muscle-derived interleukin-6:lipolytic, anti-inflammatory and immune regulatory effects[J]. Pflügers Arch, 2003, 446(1):9-16.
[4]	HART G W, HOUSLEY M P, SLAWSON C. Cycling of O-linked β-N-acetylglucosamine on nucleocytoplasmic proteins[J]. Nature, 2007, 446(7139):1017-1022.
[5]	TORRES C R, HART G W. Topography and polypeptide distribution of terminal N-acetylglucosamine residues on the surfaces of intact lymphocytes. Evidence for O-linked GlcNAc[J]. J Biol Chem, 1984, 259(5):3308-3317.
[6]	HALTIWANGER R S, HOLT G D, HART G W. Enzymatic addition of O-GlcNAc to nuclear and cytoplasmic proteins. Identification of a uridine diphospho-N-acetylglucosamine:peptide β-N-acetylgluco-saminyltransferase[J]. J Biol Chem, 1990, 265(5):2563-2568.
[7]	DONG L Y, HART G W. Purification and characterization of an O-GlcNAc selective N-acetyl-β-D-glucosaminidase from rat spleen cytosol[J]. J Biol Chem, 1994, 269(30):19321-19330.
[8]	LIU S, SHENG H X, YU Z, et al. O-linked β-N-acetylglucosamine modification of proteins is activated in post-ischemic brains of young but not aged mice:implications for impaired functional recovery from ischemic stress[J]. J Cereb Blood Flow Metab, 2016, 36(2):393-398.
[9]	HART G W. Minireview series on the thirtieth anniversary of research on O-GlcNAcylation of nuclear and cytoplasmic proteins:nutrient regulation of cellular metabolism and physiology by O-GlcNAcylation[J]. J Biol Chem, 2014, 289(50):34422-34423.
[10]	ZACHARA N E, O'DONNELL N, CHEUNG W D, et al. Dynamic O-GlcNAc modification of nucleocytoplasmic proteins in response to stress:a survival response of mammalian cells[J]. J Biol Chem, 2004, 279(29):30133-30142.
[11]	NGOH G A, HAMID T, PRABHU S D, et al. O-GlcNAc signaling attenuates ER stress-induced cardiomyocyte death[J]. Am J Physiol Heart Circ Physiol, 2009, 297(5):H1711-H1719.
[12]	YAO R Z, YANG Y Y, LIAN S, et al. Effects of acute cold stress on liver O-GlcNAcylation and glycometabolism in mice[J]. Int J Mol Sci, 2018, 19(9):2815.
[13]	LIU Y L, BI H, CHI S M, et al. The effect of compound nutrients on stress-induced changes in serum IL-2, IL-6 and TNF-α levels in rats[J]. Cytokine, 2007, 37(1):14-21.
[14]	ZHOU D, KUSNECOV A W, SHURIN M R, et al. Exposure to physical and psychological stressors elevates plasma interleukin 6:relationship to the activation of hypothalamic-pituitary-adrenal axis[J]. Endocrinology, 1993, 133(6):2523-2530.
[15]	STEPTOE A, HAMER M, CHIDA Y. The effects of acute psychological stress on circulating inflammatory factors in humans:a review and meta-analysis[J]. Brain, Behav, Immun, 2007, 21(7):901-912.
[16]	NUKINA H, SUDO N, AIBA Y, et al. Restraint stress elevates the plasma interleukin-6 levels in germ-free mice[J]. J Neuroimmunol, 2001, 115(1-2):46-52.
[17]	YILDIRIM N C, YUREKLI M. The effect of adrenomedullin and cold stress on interleukin-6 levels in some rat tissues[J]. Clin Exp Immunol, 2010, 161(1):171-175.
[18]	GIROTTI M, DONEGAN J J, MORILAK D A. Chronic intermittent cold stress sensitizes neuro-immune reactivity in the rat brain[J]. Psychoneuroendocrinology, 2011, 36(8):1164-1174.
[19]	WERNSTEDT I, EDGLEY A, BERNDTSSON A, et al. Reduced stress- and cold-induced increase in energy expenditure in interleukin-6-deficient mice[J]. Am J Physiol Regul Integr Comp Physiol, 2006, 291(3):R551-R557.
[20]	FEBBRAIO M A, HISCOCK N, SACCHETTI M, et al. Interleukin-6 is a novel factor mediating glucose homeostasis during skeletal muscle contraction[J]. Diabetes, 2004, 53(7):1643-1648.
[21]	KNUDSEN J G, BERTHOLDT L, JOENSEN E, et al. Skeletal muscle interleukin-6 regulates metabolic factors in iWAT during HFD and exercise training[J]. Obesity, 2015, 23(8):1616-1624.
[22]	GOLKS A, TRAN T T T, GOETSCHY J F, et al. Requirement for O-linked N-acetylglucosaminyltrans-ferase in lymphocytes activation[J]. EMBO J, 2007, 26(20):4368-4379.
[23]	RAMAKRISHNAN P, CLARK P M, MASON D E, et al. Activation of the transcriptional function of the NF-κB protein C-rel by O-GlcNAc glycosylation[J]. Sci Signal, 2013, 27(290):ra75.
[24]	YANG W H, PARK S Y, NAM H W, et al. NFκB activation is associated with its O-GlcNAcylation state under hyperglycemic conditions[J]. Procee Natl Acad Sci U S A, 2008, 105(45):17345-17350.

Variation of O-GlcNAc and IL-6 Expression in C2C12 Cells to Different Durations of Cold Exposure

PDF (PC)

Knowledge

Abstract

Cite this article

share this article

References 24

Related Articles 11

Recommended Articles

Metrics

Comments

[1]	WANG Tengfei, FENG Zhiqiang, SUN Yawen, ZHAO Shanjiang, HAO Haisheng, ZOU Huiying, DU Weihua, ZHAO Xueming, ZHU Huabin, PANG Yunwei. Effect of Altered O-GlcNAc Modification on in vitro Maturation of Bovine Oocytes [J]. Acta Veterinaria et Zootechnica Sinica, 2022, 53(11): 3856-3865.
[2]	LIN Chunfa, LUO Yichen, WANG Zhongqing, FENG Jingbo, LIU Juan. The Clinical Efficacy of BQJGHJ (a Traditional Chinese Medicine Compound Pharmaceutics) in the Treatment of Chickens Artificially Infected with Infectious Bronchitis Virus [J]. Acta Veterinaria et Zootechnica Sinica, 2020, 51(2): 382-391.
[3]	SHI Yi-nan, SUN Na, SUN Yao-gui, LI Hong-quan. Codonopsis pilosula Polysaccharide-induced Activation and Proliferation of Macrophage RAW264.7 cell [J]. ACTA VETERINARIA ET ZOOTECHNICA SINICA, 2017, 48(4): 777-784.
[4]	TIAN Fang-yuan, WANG Tai-an, LI Yan-min, LI Cui-cui, MA Zheng, KANG Xiang-tao, TIAN Ya-dong, LIU Xiao-jun. Cloning and Expression Characteristics of MOGAT and DGAT Genes in Chicken (Gallus gallus) [J]. ACTA VETERINARIA ET ZOOTECHNICA SINICA, 2017, 48(2): 214-224.
[5]	CHEN Xiang-xing，ZHANG Chong-yu，HUANG Li-bo，LIU Fa-xiao，YANG Wei-ren，JIANG Shu-zhen. Effects of Fusarium Toxins on IL-1β and IL-6 in Post-weaning Piglets [J]. ACTA VETERINARIA ET ZOOTECHNICA SINICA, 2016, 47(10): 2126-2135.
[6]	ZHANG Mei-hua，ZHANG Qian，MENG Le，LI Jia，ZHOU Shuang-hai,JIANG Dai-xun，CHEN Wu. Variety of Phosphodiesterase4 and IL-6，TNF-α in Lung of Clinical Porcine Respiratory Disease under the Treatment of Chinese Herbal Medicine [J]. ACTA VETERINARIA ET ZOOTECHNICA SINICA, 2014, 45(7): 1189-1195.
[7]	MA Xue-lian，JIANG Ling-ling，WANG Jin-quan，ZHANG Xiao-hong，YAO Gang. The Study on the Type and Distribution of Aerobic Bacteria in the Gastrointestinal Tract of Teraogallus himalayensis in Xinjiang [J]. ACTA VETERINARIA ET ZOOTECHNICA SINICA, 2014, 45(6): 1024-1028.
[8]	LIN Jing-jing, TAO Hui, HOU Ying-qian, CHANG Guang-jun, SHEN Xiang-zhen. Effect of Lipoteichoic Acid on Functional Receptor TLR2 Expression in Endometrial Tissue and Cell of Mice [J]. ACTA VETERINARIA ET ZOOTECHNICA SINICA, 2013, 44(5): 811-816.
[9]	CHEN Yi-jie, HUANG Zhi-jian, JIANG He-ji. Effects of Hoya Saponins on Immune Function and Antioxidation Activity of Mouse Peritoneal Macrophages [J]. ACTA VETERINARIA ET ZOOTECHNICA SINICA, 2013, 44(11): 1838-1843.
[10]	XIE Hui-mei;HU Ge;SUO Zhan-wei;LIU Yi-tong;YIN Long;YU Tong-quan;LU Ping;MU Xiang;HUANG Hui-ling. Effect of Ginsenoside Rb1 and Astragalus Polysaccharide on the Excretion of NO,IL-6 and TNF-α in Micro-vascular Endothelial Cells [J]. ACTA VETERINARIA ET ZOOTECHNICA SINICA, 2006, 37(9): 903-907.
[11]	ZHU Xiao-tong;CUI Zhi-ying;GAO Ping;JIANG Qing-yan;SHU Gang;XU Ping-wen;FU Wei-long. Effect of Glycyl-glutamine on Immune Functions of Yuehuang Chicken [J]. ACTA VETERINARIA ET ZOOTECHNICA SINICA, 2005, 36(9): 956-959.