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首页> 外文期刊>Harmful Algae >Caspase-like activity during aging and cell death in the toxic dinoflagellate Karenia brevis
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Caspase-like activity during aging and cell death in the toxic dinoflagellate Karenia brevis

机译：在有毒的鞭毛小孢粉Karenia brevis中衰老和细胞死亡期间的半胱天冬酶样活性

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摘要

The observation of caspase-like activity during cell death has provided a new framework for understanding the evolutionary and ecological contexts of programmed cell death in phytoplankton. However, additional roles for this caspase-like activity, the enzymes responsible, and the targets of this enzyme activity in phytoplankton remain largely undefined. In the present study, the role of caspase-like activity in aging and ROS-mediated cell death were investigated and death programs both dependent on and independent of caspase-like activity were observed in the toxic dinoflagellate, Karenia brevis. The dual use of in situ caspase 3/7 and TUNEL staining identified previously undescribed death-associated morphotypes in K. brevis. In silico motif analysis identified several enzymes with predicted caspase-like activity in the K. brevis transcriptome, although bona fide caspases are absent. Lastly, computational prediction of downstream caspase substrates, using sequence context and predicted secondary structure, identified proteins involved in a wide range of biological processes including regulation of protein turnover, cell cycle progression, lipid metabolism, coenzyme metabolism, apoptotic and autophagic death. To confirm the computational predictions, a short peptide was designed around the predicated caspase cleavage site in a predicted novel K. brevis caspase 3/7-like target, S-adenosylmethionine synthetase (KbAdoMetS). Cleavage of the peptide substrate with recombinant caspase 3 enzyme was determined by MALDI-TOF MS, confirming that KbAdoMetS is indeed a bona fide caspase substrate. These data identify the involvement of caspase-like activity in both aging and cell death in K. brevis and identify novel executioner enzymes and downstream targets that may be important for bloom termination.
机译：细胞死亡期间半胱天冬酶样活性的观察提供了一个新的框架，以了解浮游植物中程序性细胞死亡的进化和生态环境。但是，在浮游植物中，这种半胱天冬酶样活性，负责的酶以及该酶活性的靶标的其他作用在很大程度上仍未确定。在本研究中，对胱天蛋白酶样活性在衰老和ROS介导的细胞死亡中的作用进行了研究，并且在有毒的鞭毛藻（Karenia brevis）中观察到了依赖或不依赖胱天蛋白酶样活性的死亡程序。原位半胱天冬酶3/7和TUNEL染色的双重使用鉴定了短的K. brevis中以前未描述的死亡相关形态型。尽管没有真正的胱天蛋白酶，但在计算机模拟分析中鉴定出了在短小K.转录组中具有预测的胱天蛋白酶样活性的几种酶。最后，利用序列背景和预测的二级结构对下游胱天蛋白酶底物的计算预测，鉴定出了涉及广泛生物学过程的蛋白质，包括调节蛋白质更新，细胞周期进程，脂质代谢，辅酶代谢，凋亡和自噬死亡。为了证实计算预测，在预测的新型短视克鲁斯氏胱天蛋白酶3/7样靶标S-腺苷甲硫氨酸合成酶（KbAdoMetS）中，在预定的胱天蛋白酶切割位点周围设计了短肽。通过MALDI-TOF MS确定了重组caspase 3酶对肽底物的裂解，证实了KbAdoMetS确实是真正的caspase底物。这些数据确定了胱天蛋白酶样活性在短小K.Kervis的衰老和细胞死亡中的参与，并鉴定了可能对绽放终止很重要的新型执行酶和下游靶标。

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  • 来源
    《Harmful Algae》 |2014年第1期|41-53|共13页
  • 作者

    Jillian G. Johnson; Michael G. Janech; Frances M. Van Dolah;

  • 作者单位

    NOAA Center for Coastal Environmental Health and Biomolecular Research, 219 Fort Johnson Road, Charleston, SC 29412, USA;

    Marine Biomedicine and Environmental Sciences Program, Medical University of South Carolina, Charleston, SC, USA,Department of Medicine, Division of Nephrology, Medical University of South Carolina, Charleston, SC, USA;

    NOAA Center for Coastal Environmental Health and Biomolecular Research, Charleston, SC, USA,Marine Biomedicine and Environmental Sciences Program, Medical University of South Carolina, Charleston, SC, USA;

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  • 正文语种 eng
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  • 关键词

    Aging; Programmed cell death; Caspase;

    机译：老化;程序性细胞死亡;半胱天冬酶;

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