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本文引用的文献

1
Localization of mitochondrial Hsp56 chaperonin during sea urchin development.海胆发育过程中线粒体Hsp56伴侣蛋白的定位
Biochem Biophys Res Commun. 2001 Oct 12;287(5):1093-8. doi: 10.1006/bbrc.2001.5503.
2
Hsp27 protects mitochondria of thermotolerant cells against apoptotic stimuli.热休克蛋白27可保护耐热细胞的线粒体免受凋亡刺激。
Cell Stress Chaperones. 2001 Jan;6(1):49-58. doi: 10.1379/1466-1268(2001)006<0049:hpmotc>2.0.co;2.
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Protein kinase inhibitors can suppress stress-induced dissociation of Hsp27.蛋白激酶抑制剂可以抑制应激诱导的Hsp27解离。
Cell Stress Chaperones. 2001 Jan;6(1):16-20. doi: 10.1379/1466-1268(2001)006<0016:pkicss>2.0.co;2.
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Stress management - heat shock protein-70 and the regulation of apoptosis.应激管理——热休克蛋白70与细胞凋亡的调控
Trends Cell Biol. 2001 Jan;11(1):6-10. doi: 10.1016/s0962-8924(00)01874-2.
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EGTA treatment causes the synthesis of heat shock proteins in sea urchin embryos.
Mol Cell Biol Res Commun. 2000 May;3(5):306-11. doi: 10.1006/mcbr.2000.0230.
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Response of Saccharomyces cerevisiae to severe osmotic stress: evidence for a novel activation mechanism of the HOG MAP kinase pathway.酿酒酵母对严重渗透胁迫的响应：HOG丝裂原活化蛋白激酶途径新激活机制的证据
Mol Microbiol. 2000 Jul;37(2):382-97. doi: 10.1046/j.1365-2958.2000.02002.x.
7
The mitogen-activated protein kinase p38 pathway is conserved in metazoans: cloning and activation of p38 of the SAPK2 subfamily from the sponge Suberites domuncula.有丝分裂原活化蛋白激酶p38信号通路在多细胞动物中是保守的：从海绵动物Suberites domuncula克隆并激活SAPK2亚家族的p38。
Biol Cell. 2000 Apr;92(2):95-104. doi: 10.1016/s0248-4900(00)89017-6.
8
p38 MAPK signalling cascades: ancient roles and new functions.p38丝裂原活化蛋白激酶信号级联反应：古老的作用与新功能
Bioessays. 2000 Jul;22(7):637-45. doi: 10.1002/1521-1878(200007)22:7<637::AID-BIES6>3.0.CO;2-E.
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p38 MAP kinases: beyond the stress response.p38丝裂原活化蛋白激酶：超越应激反应
Trends Biochem Sci. 2000 Jun;25(6):257-60. doi: 10.1016/s0968-0004(00)01595-4.
10
Heat shock proteins: regulators of stress response and apoptosis.热休克蛋白：应激反应和细胞凋亡的调节因子。
Cell Stress Chaperones. 1998 Dec;3(4):228-36. doi: 10.1379/1466-1268(1998)003<0228:hspros>2.3.co;2.

海胆去纤毛作用诱导耐热性并激活p38丝裂原活化蛋白激酶途径。

Sea urchin deciliation induces thermoresistance and activates the p38 mitogen-activated protein kinase pathway.

作者信息

Casano Caterina, Roccheri Maria Carmela, Maenza Luisa, Migliore Silvia, Gianguzza Fabrizio

机构信息

Dipartimento di Biologia Cellulare e dello Sviluppo "A. Monroy," Università di Palermo, Viale delle Scienze, Parco D'Orleans, 90128 Palermo, Italy.

出版信息

Cell Stress Chaperones. 2003 Spring;8(1):70-5. doi: 10.1379/1466-1268(2003)8<70:sudita>2.0.co;2.

DOI:10.1379/1466-1268(2003)8<70:sudita>2.0.co;2
PMID:12820656
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC514855/
Abstract

In this study, we demonstrate by a variety of approaches (ie, morphological analysis, Western blots, immunolocalization, and the use of specific antibodies) that hyperosmotic deciliation stress of sea urchin embryos induces a thermotolerant response. Deciliation is also able to activate a phosphorylation signaling cascade the effector of which might be the p38 stress-activated protein kinase because we found that the administration of the p38 inhibitor SB203580 to sea urchin deciliated gastrula embryos makes the hyperosmotic deciliation stress lethal.

摘要

在本研究中，我们通过多种方法（即形态学分析、蛋白质免疫印迹、免疫定位以及使用特异性抗体）证明，海胆胚胎的高渗去纤毛应激可诱导耐热反应。去纤毛还能够激活磷酸化信号级联反应，其效应器可能是p38应激激活蛋白激酶，因为我们发现，向海胆去纤毛原肠胚胚胎施用p38抑制剂SB203580会使高渗去纤毛应激变得致命。