scholarly journals External induction of heat shock stimulates the immune response and longevity of Caenorhabditis elegans towards pathogen exposure

2016 ◽  
Vol 22 (6) ◽  
pp. 466-478 ◽  
Author(s):  
Udayakumar Prithika ◽  
Veerappan Deepa ◽  
Krishnaswamy Balamurugan
Keyword(s):  
Caenorhabditis Elegans ◽  
Heat Shock ◽  
Bacterial Infections ◽  
External Heat ◽  
Supporting Evidence ◽  
Heat Induction ◽  
C Elegans ◽  
Type C ◽  
Shock Proteins

Heat shock proteins (HSPs) are highly chaperonic molecules that give immediate response during any stress, tissue damage or bacterial infections. In the present study, the role of HSPs upon bacterial encounter is studied by applying external heat induction to live Caenorhabditis elegans. Heat shock was observed to increase the life span of wild type C. elegans upon pathogenic encounter, indicating a role of HSPs in bacterial infection and immunity. Similar increase in resistance towards pathogenesis observed in long-lived C. elegans daf-2 mutants and the increase in the lifespan indicated a role for the insulin/IGF-1 signaling (IIS) pathway in HSP-mediated pathogenic resistance. The microscopic observation of C. elegans after external heat induction and sequential exposure of pathogens indicated reduction of egg viability. Results of Real-time PCR and immunoblotting analysis of candidate genes revealed that heat shock and IIS pathways collaborate in the observed pathogenic resistance and further suggested SGK-1 to be the possible factor linking both these pathways. In addition, survival assays carried out using mutants equips us with supporting evidence that HSP and HSF-1 are necessary for the accelerated lifespan of C. elegans. Our findings thus confirm that crosstalk between HSPs and SGK-1 influences C. elegans longevity.

scholarly journals The noncanonical small heat shock protein HSP-17 from Caenorhabditis elegans is a selective protein aggregase

2020 ◽  
Vol 295 (10) ◽  
pp. 3064-3079 ◽  
Author(s):  
Manuel Iburg ◽  
Dmytro Puchkov ◽  
Irving U. Rosas-Brugada ◽  
Linda Bergemann ◽  
Ulrike Rieprecht ◽  
...  
Keyword(s):  
Caenorhabditis Elegans ◽  
Heat Shock ◽  
Small Heat Shock Protein ◽  
Independent Manner ◽  
C Elegans ◽  
Higher Eukaryotes ◽  
Prolonged Heat ◽  
Shock Proteins ◽  
Excretory Organs

Small heat shock proteins (sHsps) are conserved, ubiquitous members of the proteostasis network. Canonically, they act as “holdases” and buffer unfolded or misfolded proteins against aggregation in an ATP-independent manner. Whereas bacteria and yeast each have only two sHsps in their genomes, this number is higher in metazoan genomes, suggesting a spatiotemporal and functional specialization in higher eukaryotes. Here, using recombinantly expressed and purified proteins, static light-scattering analysis, and disaggregation assays, we report that the noncanonical sHsp HSP-17 of Caenorhabditis elegans facilitates aggregation of model substrates, such as malate dehydrogenase (MDH), and inhibits disaggregation of luciferase in vitro. Experiments with fluorescently tagged HSP-17 under the control of its endogenous promoter revealed that HSP-17 is expressed in the digestive and excretory organs, where its overexpression promotes the aggregation of polyQ proteins and of the endogenous kinase KIN-19. Systemic depletion of hsp-17 shortens C. elegans lifespan and severely reduces fecundity and survival upon prolonged heat stress. HSP-17 is an abundant protein exhibiting opposing chaperone activities on different substrates, indicating that it is a selective protein aggregase with physiological roles in development, digestion, and osmoregulation.

scholarly journals Functional peroxisomes are required for heat shock-induced hormesis in Caenorhabditis elegans

2021 ◽  
Author(s):  
Marina Musa ◽  
Ira Milosevic ◽  
Nuno Raimundo ◽  
Anita Krisko
Keyword(s):  
Heat Shock ◽  
Antioxidant Response ◽  
Pentose Phosphate ◽  
Lifespan Extension ◽  
C Elegans ◽  
In The Wild ◽  
Triglyceride Content ◽  
Organelle Communication ◽  
Shock Proteins

Exact mechanisms of heat shock induced lifespan extension, while documented across species, are still not well understood. Here we put forth evidence that fully functional peroxisomes are required for the activation of the canonical heat shock response and heat-induced hormesis in C. elegans. While during heat shock the HSP-70 chaperone is strongly upregulated in the wild-type (WT) as well as in the absence of peroxisomal catalase (Δctl-2 mutant), the small heat shock proteins display modestly increased expression in the mutant. Nuclear localization of HSF-1 is reduced in the Δctl-2 mutant. In addition, heat-induced lifespan extension, observed in the WT, is absent in the Δctl-2 mutant. Activation of the antioxidant response, the pentose phosphate pathway and increased triglyceride content are the most prominent changes observed during heat shock in the WT worm, but not in the Δctl-2 mutant. Involvement of peroxisomes in the cell-wide response to transient heat shock reported here gives new insight into the role of organelle communication in the organisms stress response.

scholarly journals Characterization of Caenorhabditis elegans Homologs of the Down Syndrome Candidate Gene DYRK1A

Genetics ◽  
2003 ◽  
Vol 163 (2) ◽  
pp. 571-580 ◽  
Author(s):  
William B Raich ◽  
Celine Moorman ◽  
Clay O Lacefield ◽  
Jonah Lehrer ◽  
Dusan Bartsch ◽  
...  
Keyword(s):  
Down Syndrome ◽  
Caenorhabditis Elegans ◽  
Trisomy 21 ◽  
Gene Dosage ◽  
Inducible Promoters ◽  
C Elegans ◽  
Dual Specificity ◽  
Specificity Protein

Abstract The pathology of trisomy 21/Down syndrome includes cognitive and memory deficits. Increased expression of the dual-specificity protein kinase DYRK1A kinase (DYRK1A) appears to play a significant role in the neuropathology of Down syndrome. To shed light on the cellular role of DYRK1A and related genes we identified three DYRK/minibrain-like genes in the genome sequence of Caenorhabditis elegans, termed mbk-1, mbk-2, and hpk-1. We found these genes to be widely expressed and to localize to distinct subcellular compartments. We isolated deletion alleles in all three genes and show that loss of mbk-1, the gene most closely related to DYRK1A, causes no obvious defects, while another gene, mbk-2, is essential for viability. The overexpression of DYRK1A in Down syndrome led us to examine the effects of overexpression of its C. elegans ortholog mbk-1. We found that animals containing additional copies of the mbk-1 gene display behavioral defects in chemotaxis toward volatile chemoattractants and that the extent of these defects correlates with mbk-1 gene dosage. Using tissue-specific and inducible promoters, we show that additional copies of mbk-1 can impair olfaction cell-autonomously in mature, fully differentiated neurons and that this impairment is reversible. Our results suggest that increased gene dosage of human DYRK1A in trisomy 21 may disrupt the function of fully differentiated neurons and that this disruption is reversible.

Potential role of protein stabilizers in amelioration of Parkinson's disease and associated effects in transgenic Caenorhabditis elegans model expressing alpha-synuclein

RSC Advances ◽  
2015 ◽  
Vol 5 (95) ◽  
pp. 77706-77715 ◽  
Author(s):  
Supinder Kaur ◽  
Aamir Nazir
Keyword(s):  
Parkinson’S Disease ◽  
Parkinson's Disease ◽  
Caenorhabditis Elegans ◽  
Potential Role ◽  
Alpha Synuclein ◽  
C Elegans

Studies employing transgenicC. elegansmodel show that trehalose, a protein stabilizer, alleviates manifestations associated with Parkinson's diseaseviaits inherent activity and through induction of autophagic machinery.

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