enormousJ. Ocean Univ. China(Oceanic and Coastal Sea Rearch)
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doi/10.1007/s11802-018-3561-3
ISSN 1672-5182, 2018 17 (5): 1189-1196
www.ouc.edu/xbywb/
E-mail:xbywb@ouc.edu
Molecular Characterization and Expression and DNA
Methylation Analys of a Galectin-Related Protein
Gene from Cynoglossus milaevis
XIU Yunji1), 3), 4), #, GAN Tian1), 2), 3), #, XU Wenteng1), 3), SHAO Changwei1), 3),
and CHEN Songlin1), 3), *imo是什么
1) Laboratory for Marine Fisheries Science and Food Production Process, Qingdao National Laboratory
四六级改革
for Marine Science and Technology, Yellow Sea Fisheries Rearch Institute, Chine Academy of Fishery
Sciences, Qingdao 266071, China
2) College of Fisheries and Life Science, Shanghai Ocean University, Shanghai 201306, China
百度翻译器在线3) Key Laboratory of Sustainable Development of Marine Fisheries, Ministry of Agriculture, Qingdao 266071, China
4) Marine Science and Engineering College, Qingdao Agricultural University, Qingdao 266109, China广元在线
(Received May 27, 2017; revid July 22, 2017; accepted May 6, 2018)
国际英文© Ocean University of China, Science Press and Springer-Verlag GmbH Germany 2018
Abstract Galectins, a family of ß-galactoside-binding proteins, participate in both innate immunity and adaptive immunity. This study identified one novel galectin-related protein from half-smooth tongue sole Cynoglossus milaevis, which was designated as CsGRP. The full-length cDNA of its e
ncoding gene was 785bp in length with a 528bp open reading frame encoding a putative pro-tein of 176 amino acids. The deduced CsGRP contained a putative 131-aa galactoside-binding lectin domain and 3 critical residues re-sponsible for carbohydrate binding (R93, W109 and R114). Genomic structural analysis revealed that CsGRP consisted of five exons and four introns. CsGRP showed 68% similarity with Poecilia latipinna GRP and 67% similarity with Stegastes partitus GRP. CsGRP showed the highest expression level in liver, although its expression was detected in all tested tissues. When challenged with Vibrio har-veyi, the expression of CsGRP was significantly down-regulated in liver (P<0.05). In addition, we found that in spleen and kidney of C. milaevis, the CpG island of CsGRP showed significantly higher (P<0.05) methylation level in dia-resistant family of C. milaevis (DR-Cs) than in dia-susceptible ones (DS-Cs). Our results suggested that CsGRP may play important roles in the immune re-spon of C. milaevis. Moreover, DNA methylation patterns provided valuable data for understanding the relationship between epigenetic regulation and immunity, which would assist the animal genetic rearch and improve the animal breeding in the future. Key words Cynoglossus milaevis; galectin-related protein;expression pattern; DNA methylation; immune respon重庆计算机培训哪好
1 Introduction
affluence
Lectins are a group of carbohydrate-binding proteins widely existing in protists, invertebrates and vertebrates. They function in, for example, innate immunity, pathogen recognition, endocytosis, complement activation, antigen processing, B and T cell clonal lection, maturation, ac-tivation and apoptosis (Vasta et al., 2004). Galectins, de-fined by their ability to recognize β-galacto and their conrved quences to lectin, were firstly described in 1970s as galactoside-binding lectins (Waard et al., 1976). They were also called galaptins and S-type lectins (Barondes et al., 1994). All galectins share conrved carbohydrate-recognition domains (CRDs) of about 130 amino acids, which are responsible for carbohydrate bind- # The authors contributed equally to this paper.
msci是什么意思* Corresponding author. Tel: 0086-532-85844606
E-mail: chensl@ysfri.ac ing. Structurally, there are three subfamilies of mammal- ian galectins: 1) proto-type galectins with a single CRD (galectin-1, -2, -5, -7, -10, -11,-13, -14, and -15), 2) chi-mera-type galectins with a single C-terminal CRD and an extended N-terminal 120-160 aa domain (galectin 3), and 3) tandem-repeat or bivalent galectins with two distinct CRDs connected by a flexible peptide linker (galectin-4, -8 and -9) (Cooper, 2002; Rabinovich and Gruppi, 2005). Galectins have been implicated in a variety of biological process, such as cell adhesion (He and Baum, 2006), innate immunity (Kohatsu et al., 2006; Pace and Baum, 2002; Sato and Nieminen, 2002), cell
differentiation and development (Pace and Baum, 2002), signal transduction (Nakahara and Raz, 2006), regulation of cell proliferation and cell death (Hernandez and Baum, 2002; Hsu et al., 2006), and pre-mRNA splicing (Liu et al., 2002).
In recent years, a number of proteins showing clo quence similarity to the galectin family have been dis-covered. However, due to lacking galactoside binding activity, they are referred to galectin-related proteins
