Molecular characterization of a tandem-repeat galectin-9 (RuGlec9) from Korean rose bitterling (Rhodeus uyekii)

Kong, Hee Jeong; Kim, Woo Jin; Kim, Hyung Soo; Lee, Ye Ji; Kim, Chi Hong; Nam, Bo‐Hye; Kim, Young‐Ok; Kim, Dong-Gyun; Lee, Sang-Jun; Lim, Sang‐Gu; Kim, Bong-Seok

doi:10.1016/j.fsi.2012.02.003

Cited by 24 publications

(5 citation statements)

References 34 publications

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“…We detected OnGal-8 expression in most tissue types of Nile tilapia (e.g., skin, intestine, spleen, and liver), consistent with observations in other species (Hadari et al 1995). In fish, several tandem-repeat galectins are expressed in a range of tissues, including the head kidney, gills, heart, and spleen (Inagawa et al 2001;Kong et al 2012). This is the first report demonstrating that expression of OnGal-8 is highest in the skin of healthy fish.…”

Section: Discussionmentioning

confidence: 75%

Molecular characterization of Galectin-8 from Nile tilapia (Oreochromis niloticus Linn.) and its response to bacterial infection

Unajak

Pholmanee

Songtawee

et al. 2015

Molecular Immunology

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Galectins belong to the family of galactoside-binding proteins and play a major role in the immune and inflammatory responses of vertebrates and invertebrates. The galectin family is divided into three subtypes based on molecular structure; prototypes, chimera types, and tandem-repeated types. We isolated and characterized the cDNA of galectin-8 (OnGal-8) in Nile tilapia (Oreochromis niloticus). OnGal-8 consisted of a 966 bp open reading frame (ORF) that encoded a 321 amino acid protein (43.47 kDa). Homology and phylogenetic tree analysis suggested the protein was clustered with galectin-8s from other animal species and shared at least 56.8% identity with salmon galectin-8. Structurally, the amino acid sequence included two distinct N- and C- terminus carbohydrate recognition domains (CRDs) of 135 and 133 amino acids, respectively, that were connected by a 39 amino acid polypeptide linker. The N- and C-CRDs contained two conserved WG-E-I and WG-E-T motifs, suggesting they have an important role in mediating the specific interactions between OnGal-8 and saccharide moieties such as β-galactoside. The structure of OnGal-8 was characterized by a two-fold symmetric pattern of 10-and 12-stranded antiparallel ß-sheets of both N- and C-CRDs, and the peptide linker presumably formed a random coil similar to the characteristic tandem-repeat type galectin. The expression of OnGal-8 in healthy fish was highest in the skin, intestine, and brain. Experimental challenge of Nile tilapia with S. agalactiae resulted in significant up-regulation of OnGal-8in the spleen after 5 d. Our results suggest that OnGal-8 is involved in the immune response to bacterial infection.

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Section: Discussionmentioning

confidence: 75%

Molecular characterization of Galectin-8 from Nile tilapia (Oreochromis niloticus Linn.) and its response to bacterial infection

Unajak

Pholmanee

Songtawee

et al. 2015

Molecular Immunology

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“…Notwithstanding, G4 and G4W did not manifest any hemolytic and cytotoxicity toward peripheral blood [ 9 ]. A 1486 bp long cDNA tandem-repeat galectin-9 (RuGlec9) isolated from Korean rose bitterling ( Rhodeus uyekii ) reportedly triggered innate immunity in R. uyekii [ 59 ].…”

Section: Marine Organism-derived Lectinsmentioning

confidence: 99%

An Update of Lectins from Marine Organisms: Characterization, Extraction Methodology, and Potential Biofunctional Applications

et al. 2022

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Lectins are a unique group of nonimmune carbohydrate-binding proteins or glycoproteins that exhibit specific and reversible carbohydrate-binding activity in a non-catalytic manner. Lectins have diverse sources and are classified according to their origins, such as plant lectins, animal lectins, and fish lectins. Marine organisms including fish, crustaceans, and mollusks produce a myriad of lectins, including rhamnose binding lectins (RBL), fucose-binding lectins (FTL), mannose-binding lectin, galectins, galactose binding lectins, and C-type lectins. The widely used method of extracting lectins from marine samples is a simple two-step process employing a polar salt solution and purification by column chromatography. Lectins exert several immunomodulatory functions, including pathogen recognition, inflammatory reactions, participating in various hemocyte functions (e.g., agglutination), phagocytic reactions, among others. Lectins can also control cell proliferation, protein folding, RNA splicing, and trafficking of molecules. Due to their reported biological and pharmaceutical activities, lectins have attracted the attention of scientists and industries (i.e., food, biomedical, and pharmaceutical industries). Therefore, this review aims to update current information on lectins from marine organisms, their characterization, extraction, and biofunctionalities.

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“…It is a common freshwater fish endemic to Korea found in rivers that empty into the Western and Southern Sea of Korea (Kong et al, 2012). This species has been proposed as a candidate for developing ornamental fish because of its small size and beautiful body color (Kang et al, 2005).…”

Section: Chrysemys Picta Bellii (Xp_005294482) and Zebrafishmentioning

confidence: 99%

Fish Myogenic Regulatory Protein LUC7L: Characterization and Expression Analysis in Korean Rose Bitterling (Rhodeus uyekii)

Kim¹,

Kong²,

Kim³

et al. 2014

Development &Amp; Reproduciton

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Molecular characterization of a tandem-repeat galectin-9 (RuGlec9) from Korean rose bitterling (Rhodeus uyekii)

Cited by 24 publications

References 34 publications

Molecular characterization of Galectin-8 from Nile tilapia (Oreochromis niloticus Linn.) and its response to bacterial infection

Molecular characterization of Galectin-8 from Nile tilapia (Oreochromis niloticus Linn.) and its response to bacterial infection

An Update of Lectins from Marine Organisms: Characterization, Extraction Methodology, and Potential Biofunctional Applications

Fish Myogenic Regulatory Protein LUC7L: Characterization and Expression Analysis in Korean Rose Bitterling (Rhodeus uyekii)

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