Identification of novel fish sialidase genes responsible for KDN-cleaving activity
- PDF / 1,001,977 Bytes
- 9 Pages / 595.276 x 790.866 pts Page_size
- 10 Downloads / 168 Views
ORIGINAL ARTICLE
Identification of novel fish sialidase genes responsible for KDN-cleaving activity Kazuhiro Shiozaki 1,2
&
Keiya Uezono 3 & Go Hirai 3 & Akinobu Honda 2 & Masaya Minoda 1 & Ryuta Wakata 1
Received: 21 June 2020 / Revised: 4 September 2020 / Accepted: 18 September 2020 # Springer Science+Business Media, LLC, part of Springer Nature 2020
Abstract 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid (KDN) is a minor component of sialic acids detected in vertebrates, such as human cancer cells, rat liver, and fish tissues. Although the enzyme activity of KDN-cleaving sialidase (KDN-sialidase) has been detected in rainbow trout, the gene responsible for its expression has not been identified in vertebrates. We evaluated sialidases in human and various fish for their KDN-cleaving activity using an artificial substrate, methylumbelliferyl-KDN (MU-KDN). Four of the human sialidases tested (NEU1, NEU2, NEU3, and NEU4) did not hydrolyze MU-KDN. Although most fish Neu1s showed negligible KDNsialidase activity, two Neu1b sialidases from Oreochromis niloticus and Astyanax mexicanus, a paralog of Neu1, exhibited a potent KDN-sialidase activity. Further, O. niloticus and Oryzias latipes Neu3a exhibited a drastically high KDN-sialidase activity, while Danio rerio Neu3.1 showed moderate activities and other Neu3 proteins exhibited little activity. All the Neu4 sialidases tested in fish cleaved KDN and Neu5Ac from MU-KDN and MU-Neu5Ac, respectively, with equivalent potential. To our knowledge, this is the first report to identify KDN-sialidase genes in vertebrates and we believe that KDN-sialidase activity could be conserved among fish Neu4s. Keywords KDN . Neu3 . Neu4 . Sialic acid . Sialidase
Abbreviations KDN 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid MU methylumbelliferone Neu5Ac N-acetylneuraminic acid Neu5Gc N-glycolylneuraminic acid
Introduction Sialic acid localizes at the non-reducing terminal of glycoconjugates and N-acetylneuraminic acid (Neu5Ac) is Electronic supplementary material The online version of this article (https://doi.org/10.1007/s10719-020-09948-6) contains supplementary material, which is available to authorized users. * Kazuhiro Shiozaki [email protected] 1
Faculty of Fisheries, Kagoshima University, 4-50-20 Shimoarata, Kagoshima 890-0056, Japan
2
The United Graduate School of Agricultural Sciences, Kagoshima University, 1-21-24 Korimoto, Kagoshima 890-0065, Japan
3
Graduate School of Pharmaceutical Sciences, Kyushu University, 3-1-1 Maidashi, Higashi-ku, Fukuoka 812-8582, Japan
one of the major sialic acids in nature. 2-keto-3-deoxy-Dglycero-D-galacto-nononic acid (KDN) is a minor component of sialic acids that is widely distributed in organisms. KDN is found in glycoproteins, glycolipids, and polysialic acids of human lung cancer [1] and prostate cancer cells [2], rat tissues [1], Iberian ribbed newt (Pleurodeles waltlii) [3], rainbow trout (Oncorhynchus mykiss) [4], and loach (Misgurnus anguillicaudatus) [5]. In zebrafish (Danio rerio), the quantity of KDN exhi
Data Loading...
