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

IF 4.9 2区 医学 Q1 CHEMISTRY, MEDICINAL Marine Drugs Pub Date : 2024-08-31 DOI:10.3390/md22090400
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
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引用次数: 0

摘要

我们在此报告了从海洋海绵 Chondrilla australiensis 中纯化出的一种新型半凝集素家族成员--β-半乳糖苷结合凝集素 hRTL。hRTL 凝集素是一种四聚体原型半凝集素,亚基分子量为 15.5 kDa,由 141 个氨基酸组成,与同源物种 C. caribensis 的半凝集素 CCL 有 92% 的主序列相同性。通过转录组分析,发现了属于同一家族的其他序列,从而使 hRTL 的总数达到 6 个。与大多数其他半凝集素不同,hRTLs 显示了一个 23 个氨基酸长的信号肽,根据 Erdman 降解法,该信号肽会在翻译后被裂解,留下一个没有乙酰化修饰的 N 端。此外,有两个 hRTL 显示出内部插入,这就决定了存在一个不寻常的环区,它可能具有重要的功能影响。对 hRTL 的糖结合特性进行表征后发现,它对 TF 抗原、Sialyl TF 和具有 Galβ1-3 结构的 1 型 N-乙酰乳糖胺具有很高的亲和力。当给表达粘蛋白相关 TF 抗原的结直肠癌细胞系 DLD-1 细胞施用时,hRTL 可诱导糖依赖性细胞毒性。
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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.
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来源期刊
Marine Drugs
Marine Drugs 医学-医药化学
CiteScore
9.60
自引率
14.80%
发文量
671
审稿时长
1 months
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.
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