2-DE proteomic analysis of HSP70 in mollusc Chamelea gallina

Foschi, Jurgen; Matozzo, Valerio; Rosmini, Roberto; Paolo, Serrazanetti Gian; Muñoz, Marta

doi:10.1016/j.fsi.2010.12.007

Cited by 9 publications

(5 citation statements)

References 28 publications

(29 reference statements)

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“…These proteins are recognised as important molecular stress markers . HSP 70 isoforms seem to be particularly affected by the polycyclic aromatic hydrocarbon benzo[ a ]pyrene in the bivalve species C. gallina . P4hb is also a regulator of the protein redox state and is a subunit of the microsomal triglyceride transfer protein complex .…”

Section: Discussionmentioning

confidence: 99%

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Protein extraction and two‐dimensional gel electrophoresis of proteins in the marine mussel Mytilus galloprovincialis: an important tool for protein expression studies, food quality and safety assessment

et al. 2012

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Section: Discussionmentioning

confidence: 99%

“…38 HSP 70 isoforms seem to be particularly affected by the polycyclic aromatic hydrocarbon benzo[a]pyrene in the bivalve species C. gallina. 39 P4hb is also a regulator of the protein redox state and is a subunit of the microsomal triglyceride transfer protein complex. 40 Its expression is affected also by chronic hypoxia stress.…”

Section: Chaperones (4)mentioning

confidence: 99%

Protein extraction and two‐dimensional gel electrophoresis of proteins in the marine mussel Mytilus galloprovincialis: an important tool for protein expression studies, food quality and safety assessment

et al. 2012

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“…A comprehensive study comparing field and laboratory responses to metal contamination in relation to thermal stress pointed out the potential of HSP70 isoforms as biomarker of marine pollution (Micovic et al, 2009). A laboratory study focusing on HSP70 revealed the impact of BaP on the inducible HSP70 and the constitutive HSC71 (Jurgen et al, 2011). An outcome of this study includes the hypothesis that HSC levels reflect the capability of tissues for normal protein synthesis and that instead the amount of the inducible isoform HSP represents a sensitive index of adaptation to stress.…”

Section: Proteome Analysis and Protein Identificationmentioning

confidence: 99%

Investigation on the proteome response of transplanted blue mussel (Mytilus sp.) during a long term exposure experiment at differently impacted field stations in the German Bight (North Sea)

Helmholz

Lassen

Ruhnau

et al. 2015

Marine Environmental Research

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In a pilot field study the proteome response of Mytilus sp. was analyzed in relation to the concentration of different trace metal contaminants. Over a period of eight month test organisms have been exposed at a near-shore station in the anthropogenic impacted estuary of the river Elbe and at an off-shore station in the vicinity of the Island of Helgoland in the German Bight (North Sea). The stations differ in their hydrological as well as chemical characteristics. The physiological biomarkers, such as condition index which have been continuously monitored during the experiment clearly indicate the effects of the different environmental conditions. Multiple protein abundance changes were detected utilizing the techniques of two dimensional gel electrophoresis (2dGE) and consequently proteins arising as potential candidates for ecotoxicological monitoring have been identified by MALDI-ToF and ToF/ToF mass spectrometry. Different cytoskeletal proteins, enzymes of energy metabolism, stress proteins and one protein relevant for metal detoxification have been pointed out.

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“…Eukaryotic cells contains different forms of heat-shock protein 70 [Jurgen et al, 2011] and most of the pollen tube heat-shock proteins 70 do not bind to microtubules; therefore, we investigated if a specific heat-shock protein 70 isoform binds to microtubules in the kinesin-binding assay. The ATP-MAP fraction was analyzed by two-dimensional electrophoresis (2-DE) along 4-7 pH gradients and subjected to immunoblot assay (Fig.…”

Section: The Atp-map Fraction Contains a Specific Isoform Of Heat-shomentioning

confidence: 99%

Heat‐shock protein 70 binds microtubules and interacts with kinesin in tobacco pollen tubes

2013

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The heat-shock proteins of 70 kDa are a family of ubiquitously expressed proteins important for protein folding. Heat-shock protein 70 assists other nascent proteins to achieve the spatial structure and ultimately helps the cell to protect against stress factors, such as heat. These proteins are localized in different cellular compartments and are associated with the cytoskeleton. We identified a heat-shock protein 70 isoform in the pollen tube of tobacco that binds to microtubules in an ATP-dependent manner. The heat-shock protein 70 was identified as part of the so-called ATP-MAP (ATP-dependent microtubule-associated protein) fraction, which also includes the 90-kDa kinesin, a mitochondria-associated motor protein. The identity of heat-shock protein 70 was validated by immunological assays and mass spectrometry. Sequence analysis showed that this heat-shock protein 70 is more similar to specific heat-shock proteins of Arabidopsis than to corresponding proteins of tobacco. Two-dimensional electrophoresis indicated that this heat-shock protein 70 isoform only is part of the ATP-MAP fraction and that is associated with the mitochondria of pollen tubes. Sedimentation assays showed that the binding of heat-shock protein 70 to microtubules is not affected by AMPPNP but it increases in the presence of the 90-kDa kinesin. Binding of heat-shock protein 70 to microtubules occurs only partially in the presence of ATP but it does not occur if, in addition to ATP, the 90-kDa kinesin is also present. Data suggest that the binding (but not the release) of heat-shock protein 70 to microtubules is facilitated by the 90-kDa kinesin.

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2-DE proteomic analysis of HSP70 in mollusc Chamelea gallina

Cited by 9 publications

References 28 publications

Protein extraction and two‐dimensional gel electrophoresis of proteins in the marine mussel Mytilus galloprovincialis: an important tool for protein expression studies, food quality and safety assessment

Protein extraction and two‐dimensional gel electrophoresis of proteins in the marine mussel Mytilus galloprovincialis: an important tool for protein expression studies, food quality and safety assessment

Investigation on the proteome response of transplanted blue mussel (Mytilus sp.) during a long term exposure experiment at differently impacted field stations in the German Bight (North Sea)

Heat‐shock protein 70 binds microtubules and interacts with kinesin in tobacco pollen tubes

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