scholarly journals Proteomic responses to hypoxia at different temperatures in the Great Scallop (Pecten maximus)

2014 ◽  
Author(s):  
Sébastien SA Artigaud ◽  
Camille CL Lacroix ◽  
Joëlle JR Richard ◽  
Jonathan Flye-Sainte-Marie ◽  
Luca LB Bargelloni ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Anaerobic Metabolism ◽  
Pecten Maximus ◽  
Thermal Window ◽  
Great Scallop ◽  
Coastal Marine ◽  
Proteomic Approach ◽  
Different Temperatures ◽  
Proteomic Responses ◽  
Octopine Dehydrogenase

Hypoxia and hyperthermia are two connected consequences of the ongoing global change that constitute major threats for coastal marine organisms. In the present study, we used a proteomic approach to characterize the changes induced by hypoxia in individuals of the great scallop, Pecten maximus, subjected to three different temperatures, i.e. 10°C, 18°C and 25°C. We did not observe any significant change induced by hypoxia in animals acclimated at 10°C. Contrastingly at 18°C and 25°C, 16 and 11 protein spots were differentially accumulated between normoxia and hypoxia, respectively. Moreover, biochemical data, i.e. octopine dehydrogenase activity and arginine assays suggests that animals grown at 25°C switched their metabolism towards anaerobic metabolism when exposed to either normoxia or hypoxia, suggesting that this temperature is out of the scallops’ optimal thermal window. In all, 11 proteins could be unambiguously identified by mass spectrometry, involved in protein modifications and signaling (e.g. CK2, TBK1), metabolism (e.g. ENO3) or cytoskeleton (GSN). The potential roles of these proteins in the thermal-dependent response of scallops to hypoxia are discussed.

scholarly journals Proteomic responses to hypoxia at different temperatures in the Great Scallop (Pecten maximus)

2014 ◽  
Author(s):  
Sébastien SA Artigaud ◽  
Camille CL Lacroix ◽  
Joëlle JR Richard ◽  
Jonathan Flye-Sainte-Marie ◽  
Luca LB Bargelloni ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Anaerobic Metabolism ◽  
Pecten Maximus ◽  
Thermal Window ◽  
Great Scallop ◽  
Coastal Marine ◽  
Proteomic Approach ◽  
Different Temperatures ◽  
Proteomic Responses ◽  
Octopine Dehydrogenase

Hypoxia and hyperthermia are two connected consequences of the ongoing global change that constitute major threats for coastal marine organisms. In the present study, we used a proteomic approach to characterize the changes induced by hypoxia in individuals of the great scallop, Pecten maximus, subjected to three different temperatures, i.e. 10°C, 18°C and 25°C. We did not observe any significant change induced by hypoxia in animals acclimated at 10°C. Contrastingly at 18°C and 25°C, 16 and 11 protein spots were differentially accumulated between normoxia and hypoxia, respectively. Moreover, biochemical data, i.e. octopine dehydrogenase activity and arginine assays suggests that animals grown at 25°C switched their metabolism towards anaerobic metabolism when exposed to either normoxia or hypoxia, suggesting that this temperature is out of the scallops’ optimal thermal window. In all, 11 proteins could be unambiguously identified by mass spectrometry, involved in protein modifications and signaling (e.g. CK2, TBK1), metabolism (e.g. ENO3) or cytoskeleton (GSN). The potential roles of these proteins in the thermal-dependent response of scallops to hypoxia are discussed.

scholarly journals Proteomic responses to hypoxia at different temperatures in the great scallop (Pecten maximus)

PeerJ ◽  
2015 ◽  
Vol 3 ◽  
pp. e871 ◽  
Author(s):  
Sébastien Artigaud ◽  
Camille Lacroix ◽  
Joëlle Richard ◽  
Jonathan Flye-Sainte-Marie ◽  
Luca Bargelloni ◽  
...  
Keyword(s):  
Pecten Maximus ◽  
Great Scallop ◽  
Different Temperatures ◽  
Proteomic Responses

scholarly journals Listeria monocytogenes utilizes the ClpP1/2 proteolytic machinery for fine-tuned substrate degradation under heat stress

2021 ◽  
Author(s):  
Dóra Balogh ◽  
Konstantin Eckel ◽  
Christian Fetzer ◽  
Stephan A. Sieber
Keyword(s):  
Mass Spectrometry ◽  
Listeria Monocytogenes ◽  
Elevated Temperatures ◽  
Sos Response ◽  
Wild Type ◽  
Substrate Degradation ◽  
Proteomic Approach ◽  
Different Temperatures ◽  
Cellular Pathways

Listeria monocytogenes exhibits two ClpP isoforms (ClpP1/ClpP2) which assemble into a heterooligomeric complex with enhanced proteolytic activity. Herein, we demonstrate that the formation of this complex depends on temperature and reaches a maximum ratio of about 1:1 at heat shock conditions, while almost no complex formation occurred below 4 °C. In order to decipher the role of the two isoforms at elevated temperatures, we constructed L. monocytogenes ClpP1, ClpP2 and ClpP1/2 knockout strains and analyzed their protein regulation in comparison to the wild type (WT) strain via whole proteome mass-spectrometry (MS) at 37 °C and 42 °C. While ΔclpP1 strain only altered the expression of very few proteins, ΔclpP2 and ΔclpP1/2 strains revealed the dysregulation of many proteins at both temperatures. These effects were corroborated by crosslinking co-immunoprecipitation MS analysis. Thus, while ClpP1 serves as a mere enhancer of protein degradation in the heterocomplex, ClpP2 is essential for ClpX binding and thus functions as a gatekeeper for substrate entry. Applying an integrated proteomic approach combining whole proteome and co immunoprecipitation datasets, several putative ClpP2 substrates were identified in the context of different temperatures and discussed with regards to their function in cellular pathways such as the SOS response.

Characterization of Major Allergens of Local Mud Crab (Scylla serrata)

2015 ◽  
Vol 12 (1) ◽  
pp. 1 ◽  
Author(s):  
Rosmilah Misnan ◽  
Nurul Izzah Abdul Rahman ◽  
Zailatul Hani Mohd Yadzir ◽  
Noormalin Abdullah ◽  
Mohd Faizal Bakhtiar ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Arginine Kinase ◽  
Mass Spectrometry Analysis ◽  
Scylla Serrata ◽  
Mud Crab ◽  
Meat Allergy ◽  
Proteomic Approach ◽  
The World ◽  
Major Allergens ◽  
Crab Meat

Crab meat is widely consumed in several countries around the world. However, when consumed, crab meats are frequent cause of allergic reactions throughout the world. Scylla serrata is among the most common mud crab in Malaysia. In a previous study two major allergens of mud crab at 36 and 41 kDa was identified. Thus, the aim of this study is to further identify these major allergens by a proteomic approach. Protein extract was prepared and resolved by 2-dimensional electrophoresis (2-DE). Immunoblotting was then performed using reactive sera from patients with crab allergy. Major allergenic spots were then excised from the 2-DE gel and analysed by mass spectrometry. The 2-DE profile of the extract revealed approximately >100 protein spots between pH of 4.00 to 8.00. Mass spectrometry analysis has identified the 36 and 41 kDa proteins as tropomyosin and arginine kinase, respectively. Our findings indicated that tropomyosin and arginine kinase play a major role in allergic reaction to mud crab meat among local patients with crab meat allergy, and should be included in diagnostics and therapeutic strategies of this allergy.

Proteomic-based comparison between populations of the Great Scallop, Pecten maximus

2014 ◽  
Vol 105 ◽  
pp. 164-173 ◽  
Author(s):  
Sébastien Artigaud ◽  
Romain Lavaud ◽  
Julien Thébault ◽  
Fred Jean ◽  
Øivind Strand ◽  
...  
Keyword(s):  
Pecten Maximus ◽  
Great Scallop

Identification of differentially expressed proteins in retinoblastoma tumors using mass spectrometry-based comparative proteomic approach

2017 ◽  
Vol 159 ◽  
pp. 77-91 ◽  
Author(s):  
Jasmine Naru ◽  
Ritu Aggarwal ◽  
Ashok Kumar Mohanty ◽  
Usha Singh ◽  
Deepak Bansal ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Differentially Expressed ◽  
Differentially Expressed Proteins ◽  
Proteomic Approach

scholarly journals High frequency Barium profiles in shells of the Great Scallop <i>Pecten maximus</i>: a methodical long-term and multi-site survey in Western Europe

2008 ◽  
Vol 5 (5) ◽  
pp. 3665-3698 ◽  
Author(s):  
A. Barats ◽  
D. Amouroux ◽  
L. Chauvaud ◽  
C. Pécheyran ◽  
A. Lorrain ◽  
...  
Keyword(s):  
High Frequency ◽  
Western Europe ◽  
Pecten Maximus ◽  
Coastal Environments ◽  
Great Scallop ◽  
Site Survey ◽  
Scallop Shells ◽  
Bay Of Brest ◽  
Long Term Survey

Abstract. Skeletal barium/calcium ([Ba]/[Ca])shell ratios were measured every third daily striae in 39 flat valves of the Great Scallop Pecten maximus (2-year old; 3 shells/year) collected in temperate coastal environments of Western Europe. Variations of ([Ba]/[Ca])shell ratio were first demonstrated reproducible for several scallop individuals from the same population, over a 7-year period (1998–2004), and from different coastal environments in France (42–49° N). As in previous studies, ([Ba]/[Ca])shell profiles exhibited a background ratio punctuated by transient maxima occurring in summer. Background partition coefficient (DBa=0.11±0.03, in 2000) was similar to that previously reported in P. maximus shells (DBa=0.18), suggesting a direct shell uptake of dissolved seawater Ba (Gillikin et al., 2008). Special attention was then dedicated to the complete monitoring of high resolution ([Ba]/[Ca])shell profiles in bivalve shells (7 years, Bay of Brest) to better constrain environmental processes influencing both the occurrence and the amplitude of summer peaks. In 2000, seawater Ba analyses underlined significant particulate Ba inputs at the seawater interface (SWI) during ([Ba]/[Ca])shell peak events. These Ba inputs are suggested to be subsequent to and rather induced by a pelagic biogenic process. The long term survey revealed first that archived Ba within the shell cannot be used as a direct paleo productivity tracer, and second that complex pelagic/benthic processes in the Ba cycle are responsible of particulate Ba inputs to the SWI, subsequently taken up by the bivalve and recorded as higher ([Ba]/[Ca])shell ratios. When these processes will be better constrained, high frequency observations of Ba in scallop shells would provide new insights into filter feeding dynamics and into Ba biogeochemistry in coastal environments.

scholarly journals Aroma retention during drying of caja-umbu fruit pulp

2018 ◽  
Author(s):  
Narendra Narain ◽  
Anderson Santos Fontes ◽  
Maria Terezinha Santos Leite-Neta ◽  
Patricia Nogueira Matos ◽  
Hannah Caroline Santos Araújo ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Gas Chromatography ◽  
Phenolic Compounds ◽  
Volatile Compounds ◽  
Spray Drying ◽  
Gas Chromatography Mass Spectrometry ◽  
Total Phenolic ◽  
Fruit Pulp ◽  
Total Phenolic Compounds ◽  
Different Temperatures

This study was aimed to obtain and characterize the dried powder of cajá-umbu (Spondias spp) fruit pulp obtained by spray-drying and lyophilization. Spray-drying of the pulp was done at different temperatures. Analysis of bioactive compounds and volatile compounds was performed. The total phenolic compounds content was high in the dried powder obtained at the temperature of 140 °C. The volatiles analysis of dried powders revealed  that the powder dried at  140°C contained a larger number of compounds. The cajá-umbu powder showed that it is a better alternative for storage and conservation since it retained the majority of volatile compounds. Keywords: Cajá-umbu, volatile compounds, gas chromatography, mass spectrometry.

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