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Kuruvilla, Jacob
Publications (4 of 4) Show all publications
Rodrigues, P. M., Campos, A., Kuruvilla, J., Schrama, D. & Cristobal, S. (2017). Chapter 17 - Proteomics in Aquaculture: Quality and Safety. In: Colgrave, Michelle L. (Ed.), Proteomics in Food Science: (pp. 279-295). Elsevier
Open this publication in new window or tab >>Chapter 17 - Proteomics in Aquaculture: Quality and Safety
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2017 (English)In: Proteomics in Food Science / [ed] Colgrave, Michelle L., Elsevier, 2017, p. 279-295Chapter in book (Other academic)
Abstract [en]

Aquaculture is a growing sector of the food industry that actively tries to integrate scientific knowledge into its management strategies. Aquaculture faces several key challenges including the provision of high-quality nutritional sources that serve to address both quality and safety, thus transforming production and management strategies to integrate sustainable principles. Proteomics has been established as a powerful and unbiased instrument in environmental monitoring and risk assessment. Proteomics in aquaculture has been applied to address welfare, nutrition, health, environmental quality, and safety. In this review, we will focus on the proteomics-based method developed and implemented for its application to elucidate the key challenges that face the fish and seafood industries: quality and safety. The latest methodological developments in high-throughput proteomics and metaproteomics are seeing rapid integration into aquaculture research contributing to the common goal of offering high quality food production processes and environmental sustainability.

Place, publisher, year, edition, pages
Elsevier, 2017
Keywords
Aquaculture, Assessment, Fish, Metaproteomics, Proteomics, Safety, Seafood, Shotgun proteomics
National Category
Environmental Management
Identifiers
urn:nbn:se:liu:diva-155982 (URN)10.1016/B978-0-12-804007-2.00017-5 (DOI)2-s2.0-85040579956 (Scopus ID)9780128040072 (ISBN)
Available from: 2019-04-01 Created: 2019-04-01 Last updated: 2019-07-02Bibliographically approved
Campos, A., Danielsson, G., Farinha, A. P., Kuruvilla, J., Warholm, P. & Cristobal, S. (2016). Shotgun proteomics to unravel marine mussel (Mytilus edulis) response to long-term exposure to low salinity and propranolol in a Baltic Sea microcosm. Journal of Proteomics, 137, 97-106
Open this publication in new window or tab >>Shotgun proteomics to unravel marine mussel (Mytilus edulis) response to long-term exposure to low salinity and propranolol in a Baltic Sea microcosm
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2016 (English)In: Journal of Proteomics, ISSN 1874-3919, E-ISSN 1876-7737, Vol. 137, p. 97-106Article in journal (Refereed) Published
Abstract [en]

Pharmaceuticals, among them the β-adrenoreceptor blocker propranolol, are an important group of environmental contaminants reported in European waters. Laboratory exposure to pharmaceuticals on marine species has been performed without considering the input of the ecosystem flow. To unravel the ecosystem response to long-term exposure to propranolol we have performed long-term exposure to propranolol and low salinity in microcosms. We applied shotgun proteomic analysis to gills of Mytilus edulis from those Baltic Sea microcosms and identified 2071 proteins with a proteogenomic strategy. The proteome profiling patterns from the 587 highly reproductive proteins among groups define salinity as a key factor in the mussel´s response to propranolol. Exposure at low salinity drives molecular mechanisms of adaptation based on a decrease in the abundance of several cytoskeletal proteins, signalling and intracellular membrane trafficking pathway combined with a response towards the maintenance of transcription and translation. The exposure to propranolol combined with low salinity modulates the expression of structural proteins including cilia functions and decrease the expression membrane protein transporters. This study reinforces the environment concerns of the impact of low salinity in combination with anthropogenic pollutants and anticipate critical physiological conditions for the survival of the blue mussel in the northern areas.

Place, publisher, year, edition, pages
Elsevier, 2016
Keywords
Mytilus edulis, shotgun proteomics, propranolol, low salinity, environmental monitoring, climate change
National Category
Biochemistry and Molecular Biology
Identifiers
urn:nbn:se:liu:diva-124213 (URN)10.1016/j.jprot.2016.01.010 (DOI)000374368800010 ()
Funder
Swedish Research Council
Note

Funding agencies: Swedish Research Council-Natural Science; VR-NT; Carl Trygger Foundation; Oscar and Lilli Lamms Minne Foundation; Angpanneforening Research Foundation; Magnus Bergsvall Foundation; IKERBASQUE; Basque Foundation for Science; VINNOVA; County Council of Oste

Available from: 2016-01-22 Created: 2016-01-22 Last updated: 2017-11-30Bibliographically approved
Helander, S., Montecchio, M., Pilstål, R., Su, Y., Kuruvilla, J., Johansson, M., . . . Sunnerhagen, M. (2015). Pre-Anchoring of Pin1 to Unphosphorylated c-Myc in a Fuzzy Complex Regulates c-Myc Activity. Structure, 23(12), 2267-2279
Open this publication in new window or tab >>Pre-Anchoring of Pin1 to Unphosphorylated c-Myc in a Fuzzy Complex Regulates c-Myc Activity
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2015 (English)In: Structure, ISSN 0969-2126, E-ISSN 1878-4186, Vol. 23, no 12, p. 2267-2279Article in journal (Refereed) Published
Abstract [en]

Hierarchic phosphorylation and concomitant Pin1-mediated proline isomerization of the oncoprotein c-Myc controls its cellular stability and activity. However, the molecular basis for Pin1 recognition and catalysis of c-Myc and other multisite, disordered substrates in cell regulation and disease is unclear. By nuclear magnetic resonance, surface plasmon resonance, and molecular modeling, we show that Pin1 subdomains jointly pre-anchor unphosphorylated c-Myc1–88 in the Pin1 interdomain cleft in a disordered, or “fuzzy”, complex at the herein named Myc Box 0 (MB0) conserved region N-terminal to the highly conserved Myc Box I (MBI). Ser62 phosphorylation in MBI intensifies previously transient MBI-Pin1 interactions in c-Myc1–88 binding, and increasingly engages Pin1PPIase and its catalytic region with maintained MB0 interactions. In cellular assays, MB0 mutated c-Myc shows decreased Pin1 interaction, increased protein half-life, but lowered rates of Myc-driven transcription and cell proliferation. We propose that dynamic Pin1 recognition of MB0 contributes to the regulation of c-Myc activity in cells

Place, publisher, year, edition, pages
Cell Press, 2015
National Category
Natural Sciences
Identifiers
urn:nbn:se:liu:diva-106184 (URN)10.1016/j.str.2015.10.010 (DOI)
Note

The previous status of this article was Manuscript and the original title was Pre-anchoring of Pin1 to unphosphorylated c-Myc in a dynamic complex affects c-Myc stability andactivity.

Funding Agencies|Knut and Alice Wallenberg Foundation; Swedish Cancer Foundation; Swedish Child Cancer Foundation; Carl Trygger foundation; LiU Cancer Research Network; Swedish Research Council; NCI [R01s CA129040, CA100855]

Available from: 2014-04-28 Created: 2014-04-28 Last updated: 2018-05-06Bibliographically approved
Irigoyen, S., Karlsson, P., Kuruvilla, J., Spetea Wiklund, C. & Versaw, W. K. (2011). The Sink-Specific Plastidic Phosphate Transporter PHT4;2 Influences Starch Accumulation and Leaf Size in Arabidopsis. Plant Physiology, 157(4), 1765-1777
Open this publication in new window or tab >>The Sink-Specific Plastidic Phosphate Transporter PHT4;2 Influences Starch Accumulation and Leaf Size in Arabidopsis
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2011 (English)In: Plant Physiology, ISSN 0032-0889, E-ISSN 1532-2548, Vol. 157, no 4, p. 1765-1777Article in journal (Refereed) Published
Abstract [en]

Nonphotosynthetic plastids are important sites for the biosynthesis of starch, fatty acids, and amino acids. The uptake and subsequent use of cytosolic ATP to fuel these and other anabolic processes would lead to the accumulation of inorganic phosphate (Pi) if not balanced by a Pi export activity. However, the identity of the transporter(s) responsible for Pi export is unclear. The plastid-localized Pi transporter PHT4;2 of Arabidopsis (Arabidopsis thaliana) is expressed in multiple sink organs but is nearly restricted to roots during vegetative growth. We identified and used pht4;2 null mutants to confirm that PHT4; 2 contributes to Pi transport in isolated root plastids. Starch accumulation was limited in pht4; 2 roots, which is consistent with the inhibition of starch synthesis by excess Pi as a result of a defect in Pi export. Reduced starch accumulation in leaves and altered expression patterns for starch synthesis genes and other plastid transporter genes suggest metabolic adaptation to the defect in roots. Moreover, pht4; 2 rosettes, but not roots, were significantly larger than those of the wild type, with 40% greater leaf area and twice the biomass when plants were grown with a short (8-h) photoperiod. Increased cell proliferation accounted for the larger leaf size and biomass, as no changes were detected in mature cell size, specific leaf area, or relative photosynthetic electron transport activity. These data suggest novel signaling between roots and leaves that contributes to the regulation of leaf size.

Place, publisher, year, edition, pages
American Society of Plant Biologists, 2011
National Category
Engineering and Technology
Identifiers
urn:nbn:se:liu:diva-74862 (URN)10.1104/pp.111.181925 (DOI)000298375600014 ()
Note
Funding Agencies|National Science Foundation|IOS-0416443IOS-0956486|Swedish Research Council|622-2007-517621-2007-5440|Swedish Research Council for Environment, Agriculture, and Space Planning|229-2007-1378|Available from: 2012-02-10 Created: 2012-02-10 Last updated: 2017-12-07
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