title: The relationship between Src-suppressed C kinase substrate and β-1,4 galactosyltransferase-I in the process of lipopolysaccharide-induced TNF-α secretion in rat primary astrocytes.
abstract: Src-suppressed C kinase substrate (SSeCKS), a protein kinase C substrate, is a major lipopolysaccharide (LPS) response protein. In addition, β-1,4 Galactosyltransferase-I (β-1,4-GalT-I) also plays an important role in the inflammation reactions of nervous system. It was reported that both SSeCKS and β-1,4-GalT-I were involved in the LPS-induced tumor necrosis factor-alpha (TNF-α) expression in rat primary astrocytes. However, the functional interaction between SSeCKS and β-1,4-GalT-I in the LPS-induced TNF-α secretion remains unclear. Therefore, in this study, using the inflammation model of astrocytes treated by LPS in vitro, we found that the changed expressions of SSeCKS and β-1,4-GalT-I participated in LPS-induced TNF-α secretion through p38, JNK, and ERK signal transduction pathways in rat primary astrocytes. Knockdown by small-interfering RNAs (siRNAs) or overexpression of SSeCKS and β-1,4-GalT-I could influence Mitogen-activated protein kinases (MAPKs) signaling pathways activation and TNF-α secretion. Besides, we confirmed that knockdown of SSeCKS could prevent the induction of β-1,4-GalT-I in this process. Inversely, β-1,4-GalT-I had no significant effect on SSeCKS expression in the same way. In summary, our data indicated that SSeCKS could regulate LPS-induced TNF-α secretion through β-1,4-GalT-I in rat primary astrocytes.
authors.affiliation: Department of Neurosurgery, Affiliated Dongtai Hospital of Nantong University, Medical College, Nantong University, Yancheng, 224200 Jiangsu, People's Republic of China.
authors.forename: Bai
authors.initials: B
authors.lastname: Shao
authors.forename: Chunmiao
authors.initials: C
authors.lastname: Li
authors.forename: Huiguang
authors.initials: H
authors.lastname: Yang
authors.forename: Aiguo
authors.initials: A
authors.lastname: Shen
authors.forename: Xiaohong
authors.initials: X
authors.lastname: Wu
authors.forename: Qin
authors.initials: Q
authors.lastname: Yuan
authors.forename: Xiujie
authors.initials: X
authors.lastname: Wu
authors.forename: Lihua
authors.initials: L
authors.lastname: Kang
authors.forename: Zhiqiang
authors.initials: Z
authors.lastname: Liu
authors.forename: Guowei
authors.initials: G
authors.lastname: Zhang
authors.forename: Xiang
authors.initials: X
authors.lastname: Lu
authors.forename: Chun
authors.initials: C
authors.lastname: Cheng
mesh_terms: D054758:A Kinase Anchor Proteins / Q000235:genetics / Q000378:metabolism*; D000818:Animals; D001253:Astrocytes / Q000166:cytology / Q000187:drug effects* / Q000378:metabolism*; D018797:Cell Cycle Proteins / Q000235:genetics / Q000378:metabolism*; D002478:Cells, Cultured; D005700:Galactosyltransferases / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D008070:Lipopolysaccharides / Q000494:pharmacology*; D020935:MAP Kinase Signaling System / Q000502:physiology; D020928:Mitogen-Activated Protein Kinases / Q000378:metabolism; D034741:RNA, Small Interfering / Q000235:genetics / Q000378:metabolism; D051381:Rats; D014409:Tumor Necrosis Factor-alpha / Q000378:metabolism*
chemical_list: D054758:A Kinase Anchor Proteins; C102361:Akap12 protein, rat; D018797:Cell Cycle Proteins; D008070:Lipopolysaccharides; D034741:RNA, Small Interfering; D014409:Tumor Necrosis Factor-alpha; D005700:Galactosyltransferases; C119701:beta-1,4-galactosyltransferase I; D020928:Mitogen-Activated Protein Kinases