Latent alterations in swimming behavior by developmental methylmercury exposure are modulated by the homolog of tyrosine hydroxylase in Caenorhabditis elegans

2021 ◽  
Vol 85 ◽  
pp. 106963
Author(s):  
Tao Ke ◽  
Lisa M. Prince ◽  
Aaron B. Bowman ◽  
Michael Aschner
Keyword(s):  
Caenorhabditis Elegans ◽  
Tyrosine Hydroxylase ◽  
Swimming Behavior ◽  
Methylmercury Exposure

scholarly journals Developmental Methylmercury Exposure Affects Swimming Behavior and Foraging Efficiency of Yellow Perch (Perca flavescens) Larvae

ACS Omega ◽  
2017 ◽  
Vol 2 (8) ◽  
pp. 4870-4877 ◽  
Author(s):  
Francisco X. Mora-Zamorano ◽  
Rebekah Klingler ◽  
Niladri Basu ◽  
Jessica Head ◽  
Cheryl A. Murphy ◽  
...  
Keyword(s):  
Yellow Perch ◽  
Perca Flavescens ◽  
Swimming Behavior ◽  
Foraging Efficiency ◽  
Methylmercury Exposure

Divergence in enzyme regulation between Caenorhabditis elegans and human tyrosine hydroxylase, the key enzyme in the synthesis of dopamine

2011 ◽  
Vol 434 (1) ◽  
pp. 133-141 ◽  
Author(s):  
Ana C. Calvo ◽  
Angel L. Pey ◽  
Antonio Miranda-Vizuete ◽  
Anne P. Døskeland ◽  
Aurora Martinez
Keyword(s):  
Caenorhabditis Elegans ◽  
Tyrosine Hydroxylase ◽  
Biochemical Characterization ◽  
Catalytic Domain ◽  
Feedback Inhibition ◽  
Substrate Inhibition ◽  
Enzyme Regulation ◽  
C Elegans ◽  
Key Enzyme ◽  
Human Orthologue

TH (tyrosine hydroxylase) is the rate-limiting enzyme in the synthesis of catecholamines. The cat-2 gene of the nematode Caenorhabditis elegans is expressed in mechanosensory dopaminergic neurons and has been proposed to encode a putative TH. In the present paper, we report the cloning of C. elegans full-length cat-2 cDNA and a detailed biochemical characterization of the encoded CAT-2 protein. Similar to other THs, C. elegans CAT-2 is composed of an N-terminal regulatory domain followed by a catalytic domain and a C-terminal oligomerization domain and shows high substrate specificity for L-tyrosine. Like hTH (human TH), CAT-2 is tetrameric and is phosphorylated at Ser35 (equivalent to Ser40 in hTH) by PKA (cAMP-dependent protein kinase). However, CAT-2 is devoid of characteristic regulatory mechanisms present in hTH, such as negative co-operativity for the cofactor, substrate inhibition or feedback inhibition exerted by catecholamines, end-products of the pathway. Thus TH activity in C. elegans displays a weaker regulation in comparison with the human orthologue, resembling a constitutively active enzyme. Overall, our data suggest that the intricate regulation characteristic of mammalian TH might have evolved from more simple models to adjust to the increasing complexity of the higher eukaryotes neuroendocrine systems.

Ecotoxicity Risk of Low-Dose Methylmercury Exposure to Caenorhabditis elegans: Multigenerational Toxicity and Population Discrepancy

2021 ◽  
Vol 34 (4) ◽  
pp. 1114-1123
Author(s):  
Kunyu Hu ◽  
Yun Xu ◽  
Shengmin Xu ◽  
Lei Cheng ◽  
Tong Zhou ◽  
...  
Keyword(s):  
Caenorhabditis Elegans ◽  
Low Dose ◽  
Methylmercury Exposure

Efficient nematode swimming in a shear thinning colloidal suspension

Soft Matter ◽  
2016 ◽  
Vol 12 (6) ◽  
pp. 1892-1897 ◽  
Author(s):  
Jin-Sung Park ◽  
Daeyeon Kim ◽  
Jennifer H. Shin ◽  
David A. Weitz
Keyword(s):  
Caenorhabditis Elegans ◽  
Colloidal Suspension ◽  
Shear Thinning ◽  
Swimming Behavior ◽  
C Elegans

The swimming behavior of a nematode Caenorhabditis elegans (C. elegans) is investigated in a non-Newtonian shear thinning colloidal suspension.

scholarly journals Methylmercury exposure increases lipocalin related (lpr) and decreases activated in blocked unfolded protein response (abu) genes and specific miRNAs in Caenorhabditis elegans

2013 ◽  
Vol 222 (2) ◽  
pp. 189-196 ◽  
Author(s):  
Martina Rudgalvyte ◽  
Natalia VanDuyn ◽  
Vuokko Aarnio ◽  
Liisa Heikkinen ◽  
Juhani Peltonen ◽  
...  
Keyword(s):  
Caenorhabditis Elegans ◽  
Unfolded Protein Response ◽  
Unfolded Protein ◽  
Methylmercury Exposure ◽  
Protein Response

The glycomes of Caenorhabditis elegans and other model organisms

2002 ◽  
Vol 69 ◽  
pp. 117-134 ◽  
Author(s):  
Stuart M. Haslam ◽  
David Gems ◽  
Howard R. Morris ◽  
Anne Dell
Keyword(s):  
Caenorhabditis Elegans ◽  
Current Knowledge ◽  
Structural Data ◽  
Model Organisms ◽  
Entire Genome ◽  
C Elegans ◽  
The Face ◽  
Area Of Concern ◽  
Nematode Worm

There is no doubt that the immense amount of information that is being generated by the initial sequencing and secondary interrogation of various genomes will change the face of glycobiological research. However, a major area of concern is that detailed structural knowledge of the ultimate products of genes that are identified as being involved in glycoconjugate biosynthesis is still limited. This is illustrated clearly by the nematode worm Caenorhabditis elegans, which was the first multicellular organism to have its entire genome sequenced. To date, only limited structural data on the glycosylated molecules of this organism have been reported. Our laboratory is addressing this problem by performing detailed MS structural characterization of the N-linked glycans of C. elegans; high-mannose structures dominate, with only minor amounts of complex-type structures. Novel, highly fucosylated truncated structures are also present which are difucosylated on the proximal N-acetylglucosamine of the chitobiose core as well as containing unusual Fucα1–2Gal1–2Man as peripheral structures. The implications of these results in terms of the identification of ligands for genomically predicted lectins and potential glycosyltransferases are discussed in this chapter. Current knowledge on the glycomes of other model organisms such as Dictyostelium discoideum, Saccharomyces cerevisiae and Drosophila melanogaster is also discussed briefly.

Colocalization of tyrosine hydroxylase and GAD65 mRNA in mesostriatal neurons

2001 ◽  
Vol 13 (1) ◽  
pp. 57-67 ◽  
Author(s):  
Tomas Gonzalez-Hernandez ◽  
Pedro Barroso-Chinea ◽  
Abraham Acevedo ◽  
Eduardo Salido ◽  
Manuel Rodriguez
Keyword(s):  
Tyrosine Hydroxylase
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