Ryuhei Hayashi, Kenichi Kamata, Marco Gerdol, Yuki Fujii, Takashi Hayashi, Yuto Onoda, Nanae Kobayashi, Satoshi Furushima, Ryuya Ishiwata, Mayuka Ohkawa, Naoko Masuda, Yuka Niimi, Masao Yamada, Daisuke Adachi, Sarkar M. A. Kawsar, Sultana Rajia, Imtiaj Hasan, Somrita Padma, Bishnu Pada Chatterjee, Yuji Ise, Riku Chida, Kayo Hasehira, Nobumitsu Miyanishi, Tatsuya Kawasaki, Yukiko Ogawa, Hideaki Fujita, Alberto Pallavicini, Yasuhiro Ozeki
{"title":"从澳大利亚海绵中纯化的新型凝胶酶:由 TF 抗原结合介导的独特结构特征和对结直肠癌细胞的细胞毒性作用","authors":"Ryuhei Hayashi, Kenichi Kamata, Marco Gerdol, Yuki Fujii, Takashi Hayashi, Yuto Onoda, Nanae Kobayashi, Satoshi Furushima, Ryuya Ishiwata, Mayuka Ohkawa, Naoko Masuda, Yuka Niimi, Masao Yamada, Daisuke Adachi, Sarkar M. A. Kawsar, Sultana Rajia, Imtiaj Hasan, Somrita Padma, Bishnu Pada Chatterjee, Yuji Ise, Riku Chida, Kayo Hasehira, Nobumitsu Miyanishi, Tatsuya Kawasaki, Yukiko Ogawa, Hideaki Fujita, Alberto Pallavicini, Yasuhiro Ozeki","doi":"10.3390/md22090400","DOIUrl":null,"url":null,"abstract":"We here report the purification of a novel member of the galectin family, the β-galactoside-binding lectin hRTL, from the marine sponge Chondrilla australiensis. The hRTL lectin is a tetrameric proto-type galectin with a subunit molecular weight of 15.5 kDa, consisting of 141 amino acids and sharing 92% primary sequence identity with the galectin CCL from the congeneric species C. caribensis. Transcriptome analysis allowed for the identification of additional sequences belonging to the same family, bringing the total number of hRTLs to six. Unlike most other galectins, hRTLs display a 23 amino acid-long signal peptide that, according to Erdman degradation, is post-translationally cleaved, leaving an N-terminal end devoid of acetylated modifications, unlike most other galectins. Moreover, two hRTLs display an internal insertion, which determines the presence of an unusual loop region that may have important functional implications. The characterization of the glycan-binding properties of hRTL revealed that it had high affinity towards TF-antigen, sialyl TF, and type-1 N-acetyl lactosamine with a Galβ1-3 structure. When administered to DLD-1 cells, a colorectal carcinoma cell line expressing mucin-associated TF-antigen, hRTL could induce glycan-dependent cytotoxicity.","PeriodicalId":18222,"journal":{"name":"Marine Drugs","volume":null,"pages":null},"PeriodicalIF":4.9000,"publicationDate":"2024-08-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Novel Galectins Purified from the Sponge Chondrilla australiensis: Unique Structural Features and Cytotoxic Effects on Colorectal Cancer Cells Mediated by TF-Antigen Binding\",\"authors\":\"Ryuhei Hayashi, Kenichi Kamata, Marco Gerdol, Yuki Fujii, Takashi Hayashi, Yuto Onoda, Nanae Kobayashi, Satoshi Furushima, Ryuya Ishiwata, Mayuka Ohkawa, Naoko Masuda, Yuka Niimi, Masao Yamada, Daisuke Adachi, Sarkar M. A. Kawsar, Sultana Rajia, Imtiaj Hasan, Somrita Padma, Bishnu Pada Chatterjee, Yuji Ise, Riku Chida, Kayo Hasehira, Nobumitsu Miyanishi, Tatsuya Kawasaki, Yukiko Ogawa, Hideaki Fujita, Alberto Pallavicini, Yasuhiro Ozeki\",\"doi\":\"10.3390/md22090400\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"We here report the purification of a novel member of the galectin family, the β-galactoside-binding lectin hRTL, from the marine sponge Chondrilla australiensis. The hRTL lectin is a tetrameric proto-type galectin with a subunit molecular weight of 15.5 kDa, consisting of 141 amino acids and sharing 92% primary sequence identity with the galectin CCL from the congeneric species C. caribensis. Transcriptome analysis allowed for the identification of additional sequences belonging to the same family, bringing the total number of hRTLs to six. Unlike most other galectins, hRTLs display a 23 amino acid-long signal peptide that, according to Erdman degradation, is post-translationally cleaved, leaving an N-terminal end devoid of acetylated modifications, unlike most other galectins. Moreover, two hRTLs display an internal insertion, which determines the presence of an unusual loop region that may have important functional implications. The characterization of the glycan-binding properties of hRTL revealed that it had high affinity towards TF-antigen, sialyl TF, and type-1 N-acetyl lactosamine with a Galβ1-3 structure. When administered to DLD-1 cells, a colorectal carcinoma cell line expressing mucin-associated TF-antigen, hRTL could induce glycan-dependent cytotoxicity.\",\"PeriodicalId\":18222,\"journal\":{\"name\":\"Marine Drugs\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":4.9000,\"publicationDate\":\"2024-08-31\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Marine Drugs\",\"FirstCategoryId\":\"3\",\"ListUrlMain\":\"https://doi.org/10.3390/md22090400\",\"RegionNum\":2,\"RegionCategory\":\"医学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"CHEMISTRY, MEDICINAL\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Marine Drugs","FirstCategoryId":"3","ListUrlMain":"https://doi.org/10.3390/md22090400","RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"CHEMISTRY, MEDICINAL","Score":null,"Total":0}
Novel Galectins Purified from the Sponge Chondrilla australiensis: Unique Structural Features and Cytotoxic Effects on Colorectal Cancer Cells Mediated by TF-Antigen Binding
We here report the purification of a novel member of the galectin family, the β-galactoside-binding lectin hRTL, from the marine sponge Chondrilla australiensis. The hRTL lectin is a tetrameric proto-type galectin with a subunit molecular weight of 15.5 kDa, consisting of 141 amino acids and sharing 92% primary sequence identity with the galectin CCL from the congeneric species C. caribensis. Transcriptome analysis allowed for the identification of additional sequences belonging to the same family, bringing the total number of hRTLs to six. Unlike most other galectins, hRTLs display a 23 amino acid-long signal peptide that, according to Erdman degradation, is post-translationally cleaved, leaving an N-terminal end devoid of acetylated modifications, unlike most other galectins. Moreover, two hRTLs display an internal insertion, which determines the presence of an unusual loop region that may have important functional implications. The characterization of the glycan-binding properties of hRTL revealed that it had high affinity towards TF-antigen, sialyl TF, and type-1 N-acetyl lactosamine with a Galβ1-3 structure. When administered to DLD-1 cells, a colorectal carcinoma cell line expressing mucin-associated TF-antigen, hRTL could induce glycan-dependent cytotoxicity.
期刊介绍:
Marine Drugs (ISSN 1660-3397) publishes reviews, regular research papers and short notes on the research, development and production of drugs from the sea. Our aim is to encourage scientists to publish their experimental and theoretical research in as much detail as possible, particularly synthetic procedures and characterization information for bioactive compounds. There is no restriction on the length of the experimental section.