Small heat shock proteins as relevant biomarkers for anthropogenic stressors in earthworms

被引:0
作者
Tilikj, Natasha [1 ]
de la Fuente, Mercedes [3 ]
Muniz-Gonzalez, Ana Belen [4 ]
Martinez-Guitarte, Jose-Luis [2 ]
Caballero-Carretero, Patricia [2 ]
Novo, Marta [1 ]
机构
[1] Univ Complutense Madrid, Dept Biodivers Ecol & Evolut, Dept Biodivers Ecol & Evoluc, C Jose Antonio Novais 12, Madrid 28040, Spain
[2] UNED, Fac Ciencias, Dept Fis Matemat & Fluidos, Environm Toxicol & Biol Grp, Senda Rey 9, Madrid 28040, Spain
[3] Univ Nacl Educ Distancia UNED, Dept Fis Interdisciplinar, Fac Ciencias, Ave Esparta S-N, Madrid 28232, Spain
[4] Univ Politecn Madrid UPM, Escuela Tecn Super Ingn Agron Alimentaria & Biosis, ETSIAAB, Edificio Agr,Avda Puerta Hierro 2, Madrid 28040, Spain
来源
COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY A-MOLECULAR & INTEGRATIVE PHYSIOLOGY | 2025年 / 300卷
关键词
Anthropogenic stress; Invertebrates; Biomarkers; Heat shock proteins; Adaptation; CHIRONOMUS-RIPARIUS; FUNCTIONAL-ANALYSIS; BISPHENOL-A; GENE; EXPRESSION; CHAPERONES; RESISTANCE; RESOURCES; SEQUENCE; GROWTH;
D O I
10.1016/j.cbpa.2024.111785
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Anthropogenic stressors in terrestrial ecosystems require focused research on adaptive responses in soil organisms such as Eisenia fetida, a model earthworm species. We analyzed the gene expression of five small heat shock proteins (sHSPs) in response to various stressors: heat stress (31 and 35 degrees C), desiccation (10 % and 20 % humidity), and chemical exposure (bisphenol A and endosulfan) under standard and elevated temperatures. Under moderate heat (31 degrees C), early upregulation of sHSP transcripts suggests their involvement in initial stress responses, possibly mitigating protein aggregation. At the higher temperature (35 degrees C), three sHSPs served as a defense against severe protein aggregation, a significant finding as previous studies identified only one activated heat shock protein (HSP70) in E. fetida under similar conditions. Desiccation stress at 10 % humidity activated more sHSPs than at 20 % humidity, and the expression profile at 10 % humidity closely resembled that observed under heat stress, suggesting overlapping adaptation pathways. Heat combined with chemical stress, particularly endosulfan, elevated sHSP transcription and underscored the potential of these proteins as biomarkers in multistressor environments. Monomeric sHSPs from E. fetida, which share homology with human sHSPs, showed the highest activity across all stressors, suggesting their key role in earthworm adaptation.
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页数:11
相关论文
共 68 条
[1]   Small heat shock proteins HSP27 (HspB1), αB-crystallin (HspB5) and HSP22 (HspB8) as regulators of cell death [J].
Acunzo, Julie ;
Katsogiannou, Maria ;
Rocchi, Palma .
INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY, 2012, 44 (10) :1622-1631
[2]   The major inducible small heat shock protein HSP20-3 in the tardigrade Ramazzottius varieornatus forms filament-like structures and is an active chaperone [J].
Al-Ansari, Mohammad ;
Fitzsimons, Taylor ;
Wei, Wenbin ;
Goldberg, Martin W. ;
Kunieda, Takekazu ;
Quinlan, Roy A. .
CELL STRESS & CHAPERONES, 2024, 29 (01) :51-65
[3]   Endosulfan exposure alters transcription of genes involved in the detoxification and stress responses in Physella acuta [J].
Alonso-Trujillo, Maria ;
Muniz-Gonzalez, Ana-Belen ;
Martinez-Guitarte, Jose-Luis .
SCIENTIFIC REPORTS, 2020, 10 (01)
[4]  
ALTSCHUL SF, 1990, J MOL BIOL, V215, P403, DOI 10.1006/jmbi.1990.9999
[5]  
Arrigo AP, 2007, ADV EXP MED BIOL, V594, P14
[6]   The quest to deduce protein function from sequence: the role of pattern databases [J].
Attwood, TK .
INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY, 2000, 32 (02) :139-155
[7]   Transcription Analysis of the Stress and Immune Response Genes to Temperature Stress in Ostrinia furnacalis [J].
Chen, Kangkang ;
Tang, Tai ;
Song, Qisheng ;
Wang, Zhenying ;
He, Kanglai ;
Liu, Xu ;
Song, Jiahui ;
Wang, Libao ;
Yang, Yizhong ;
Feng, Congjing .
FRONTIERS IN PHYSIOLOGY, 2019, 10
[8]   Desiccation tolerance in encysted embryos of the animal extremophile, Artemia [J].
Clegg, JS .
INTEGRATIVE AND COMPARATIVE BIOLOGY, 2005, 45 (05) :715-724
[9]   Functional analysis of a small heat shock/α-crystallin protein from Artemia franciscana -: Oligomerization and thermotolerance [J].
Crack, JA ;
Mansour, M ;
Sun, Y ;
MacRae, TH .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 2002, 269 (03) :933-942
[10]   ScanProsite: detection of PROSITE signature matches and ProRule-associated functional and structural residues in proteins [J].
de Castro, Edouard ;
Sigrist, Christian J. A. ;
Gattiker, Alexandre ;
Bulliard, Virginie ;
Langendijk-Genevaux, Petra S. ;
Gasteiger, Elisabeth ;
Bairoch, Amos ;
Hulo, Nicolas .
NUCLEIC ACIDS RESEARCH, 2006, 34 :W362-W365