Molecular cloning and characterization of Cpn60 in the free-living nematode Plectus acuminatus

S.R. Sturzenbaum, M.S.J. Arts, J.E. Kammenga

Research output: Contribution to journalArticleAcademicpeer-review

8 Citations (Scopus)

Abstract

Heat shock proteins (Hsps) have provoked interest not only because of their involvement in human diseases but also for their potential as biomarkers of environmental pollution. Whereas the former interest is covered by numerous reports, the latter is an exciting new field of research. We report the isolation of the full-length cpn60 messenger ribonucleic acid (mRNA) and partial genomic deoxyribonucleic acid from the free-living, environmental sentinel nematode Plectus acuminatus, a species used in classical ecotoxicity tests. Although the primary sequence displays high identity scores to other nematodes and human Cpn60 (75% and 70%, respectively), the intron-exon structure differs markedly. Furthermore, although mRNA levels remained constant after exposure to ZnCl2 (0¿330 ¿M) under laboratory conditions, protein levels increased significantly in a dose-dependent manner. In conclusion, this first account of molecular genetic similarities and differences of Cpn60 in a neglected nematode taxon provides a valuable insight into its potential uses in gene-based ecotoxicological risk assessment exercises
Original languageEnglish
Pages (from-to)79-85
JournalCell Stress and Chaperones
Volume10
Issue number2
DOIs
Publication statusPublished - 2005

Fingerprint

Cloning
Molecular Cloning
RNA
Environmental Pollution
Biomarkers
Heat-Shock Proteins
Risk assessment
Introns
Molecular Biology
Exons
Pollution
Genes
DNA
Research
Proteins
cyhalothrin

Keywords

  • shock-protein hsp60
  • heat-shock
  • stress-proteins
  • expression
  • gene
  • identification
  • chaperonin
  • atherosclerosis
  • autoimmune
  • regions

Cite this

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title = "Molecular cloning and characterization of Cpn60 in the free-living nematode Plectus acuminatus",
abstract = "Heat shock proteins (Hsps) have provoked interest not only because of their involvement in human diseases but also for their potential as biomarkers of environmental pollution. Whereas the former interest is covered by numerous reports, the latter is an exciting new field of research. We report the isolation of the full-length cpn60 messenger ribonucleic acid (mRNA) and partial genomic deoxyribonucleic acid from the free-living, environmental sentinel nematode Plectus acuminatus, a species used in classical ecotoxicity tests. Although the primary sequence displays high identity scores to other nematodes and human Cpn60 (75{\%} and 70{\%}, respectively), the intron-exon structure differs markedly. Furthermore, although mRNA levels remained constant after exposure to ZnCl2 (0¿330 ¿M) under laboratory conditions, protein levels increased significantly in a dose-dependent manner. In conclusion, this first account of molecular genetic similarities and differences of Cpn60 in a neglected nematode taxon provides a valuable insight into its potential uses in gene-based ecotoxicological risk assessment exercises",
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language = "English",
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Molecular cloning and characterization of Cpn60 in the free-living nematode Plectus acuminatus. / Sturzenbaum, S.R.; Arts, M.S.J.; Kammenga, J.E.

In: Cell Stress and Chaperones, Vol. 10, No. 2, 2005, p. 79-85.

Research output: Contribution to journalArticleAcademicpeer-review

TY - JOUR

T1 - Molecular cloning and characterization of Cpn60 in the free-living nematode Plectus acuminatus

AU - Sturzenbaum, S.R.

AU - Arts, M.S.J.

AU - Kammenga, J.E.

PY - 2005

Y1 - 2005

N2 - Heat shock proteins (Hsps) have provoked interest not only because of their involvement in human diseases but also for their potential as biomarkers of environmental pollution. Whereas the former interest is covered by numerous reports, the latter is an exciting new field of research. We report the isolation of the full-length cpn60 messenger ribonucleic acid (mRNA) and partial genomic deoxyribonucleic acid from the free-living, environmental sentinel nematode Plectus acuminatus, a species used in classical ecotoxicity tests. Although the primary sequence displays high identity scores to other nematodes and human Cpn60 (75% and 70%, respectively), the intron-exon structure differs markedly. Furthermore, although mRNA levels remained constant after exposure to ZnCl2 (0¿330 ¿M) under laboratory conditions, protein levels increased significantly in a dose-dependent manner. In conclusion, this first account of molecular genetic similarities and differences of Cpn60 in a neglected nematode taxon provides a valuable insight into its potential uses in gene-based ecotoxicological risk assessment exercises

AB - Heat shock proteins (Hsps) have provoked interest not only because of their involvement in human diseases but also for their potential as biomarkers of environmental pollution. Whereas the former interest is covered by numerous reports, the latter is an exciting new field of research. We report the isolation of the full-length cpn60 messenger ribonucleic acid (mRNA) and partial genomic deoxyribonucleic acid from the free-living, environmental sentinel nematode Plectus acuminatus, a species used in classical ecotoxicity tests. Although the primary sequence displays high identity scores to other nematodes and human Cpn60 (75% and 70%, respectively), the intron-exon structure differs markedly. Furthermore, although mRNA levels remained constant after exposure to ZnCl2 (0¿330 ¿M) under laboratory conditions, protein levels increased significantly in a dose-dependent manner. In conclusion, this first account of molecular genetic similarities and differences of Cpn60 in a neglected nematode taxon provides a valuable insight into its potential uses in gene-based ecotoxicological risk assessment exercises

KW - shock-protein hsp60

KW - heat-shock

KW - stress-proteins

KW - expression

KW - gene

KW - identification

KW - chaperonin

KW - atherosclerosis

KW - autoimmune

KW - regions

U2 - 10.1379/CSC-84R.1

DO - 10.1379/CSC-84R.1

M3 - Article

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SP - 79

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JO - Cell Stress and Chaperones

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SN - 1355-8145

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