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1.
Physiol Plant ; 176(2): e14261, 2024.
Article in English | MEDLINE | ID: mdl-38527955

ABSTRACT

In response to our ever-increasing demand for metals, phytotechnologies are being developed to limit the environmental impact of conventional metal mining. However, the development of these technologies, which rely on plant species able to tolerate and accumulate metals, is partly limited by our lack of knowledge of the underlying molecular mechanisms. In this work, we aimed to better understand the role of metal transporters of the IRON REGULATED 1/FERROPORTIN (IREG/FPN) family from the nickel hyperaccumulator Leucocroton havanensis from the Euphorbiaceae family. Using transcriptomic data, we identified two homologous genes, LhavIREG1 and LhavIREG2, encoding divalent metal transporters of the IREG/FPN family. Both genes are expressed at similar levels in shoots, but LhavIREG1 shows higher expression in roots. The heterologous expression of these transporters in A. thaliana revealed that LhavIREG1 is localized to the plasma membrane, whereas LhavIREG2 is located on the vacuole. In addition, the expression of each gene induced a significant increase in nickel tolerance. Taken together, our data suggest that LhavIREG2 is involved in nickel sequestration in vacuoles of leaf cells, whereas LhavIREG1 is mainly involved in nickel translocation from roots to shoots, but could also be involved in metal sequestration in cell walls. Our results suggest that paralogous IREG/FPN transporters may play complementary roles in nickel hyperaccumulation in plants.


Subject(s)
Cation Transport Proteins , Nickel , Metals , Plants/metabolism , Cation Transport Proteins/genetics , Cation Transport Proteins/metabolism
2.
PeerJ ; 11: e15422, 2023.
Article in English | MEDLINE | ID: mdl-37304885

ABSTRACT

Mangroves are coastal wetlands with high biodiversity and productivity, with great interaction with coastal environments. In the face of worldwide mangrove loss, restoration projects attempt to recover ecosystem composition and functioning over time. Our objective was to examine and compare the food webs in mangrove areas with different restoration times and in a reference mangrove in Términos Lagoon, Mexico. We estimated the trophic structure, identified the carbon resources that maintain aquatic consumers through the analysis of stable isotopes, and compared the trophic niche of the restored mangroves with the reference mangrove. We analyzed environmental variables, trophic structure, and contributions of resources during three seasons: rainy, dry, and "nortes". Environmental changes and food structure changed in response to regional seasons. Bayesian mixing models indicated that food webs varied seasonally as a response to the primary productivity developed at Términos Lagoon. As expected, the assimilation of C3 plants in the reference mangrove was highest, as a primary ("nortes" season) and secondary resource (dry and rainy seasons). The restored mangroves depended mainly on allochthonous resources (seagrass, epiphytes, and phytoplankton). The assimilation of these resources highlighted the importance of connectivity and the input of sources of carbon from nearby coastal environments. Trophic niche analysis showed that the area with longer restoration time was more similar to the reference mangrove, which is evidence of the importance and efficacy of the restoration process, as well as the restoration of the ecosystem function over time.


Subject(s)
Ecosystem , Food Chain , Bayes Theorem , Gulf of Mexico , Carbon
3.
Bioinformatics ; 38(11): 3141-3142, 2022 05 26.
Article in English | MEDLINE | ID: mdl-35380605

ABSTRACT

SUMMARY: To advance biomedical research, increasingly large amounts of complex data need to be discovered and integrated. This requires syntactic and semantic validation to ensure shared understanding of relevant entities. This article describes the ELIXIR biovalidator, which extends the syntactic validation of the widely used AJV library with ontology-based validation of JSON documents. AVAILABILITY AND IMPLEMENTATION: Source code: https://github.com/elixir-europe/biovalidator, Release: v1.9.1, License: Apache License 2.0, Deployed at: https://www.ebi.ac.uk/biosamples/schema/validator/validate. SUPPLEMENTARY INFORMATION: Supplementary data are available at Bioinformatics online.


Subject(s)
Biological Science Disciplines , Metadata , Semantics , Software
4.
J Mol Model ; 28(2): 31, 2022 Jan 07.
Article in English | MEDLINE | ID: mdl-34997307

ABSTRACT

We have developed two ligand- and receptor-based computational approaches to study the physicochemical properties relevant to the biological activity of vasopressin V2 receptor (V2R) antagonist and eventually to predict the expected binding mode to V2R. The obtained quantitative structure activity relationship (QSAR) model showed a correlation of the antagonist activity with the hydration energy (EH2O), the polarizability (P), and the calculated partial charge on atom N7 (q6) of the common substructure. The first two descriptors showed a positive contribution to antagonist activity, while the third one had a negative contribution. V2R was modeled and further relaxed on a 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocoline (POPC) membrane by molecular dynamics simulations. The receptor antagonist complexes were guessed by molecular docking, and the stability of the most relevant structures was also evaluated by molecular dynamics simulations. As a result, amino acid residues Q96, W99, F105, K116, F178, A194, F307, and M311 were identified with the probably most relevant antagonist-receptor interactions on the studied complexes. The proposed QSAR model could explain the molecular properties relevant to the antagonist activity. The contributions to the antagonist-receptor interaction appeared also in agreement with the binding mode of the complexes obtained by molecular docking and molecular dynamics. These models will be used in further studies to look for new V2R potential antagonist molecules.


Subject(s)
Antidiuretic Hormone Receptor Antagonists/chemistry , Chemical Phenomena , Models, Molecular , Receptors, Vasopressin/chemistry , Algorithms , Amino Acid Sequence , Antidiuretic Hormone Receptor Antagonists/pharmacology , Binding Sites , Cluster Analysis , Ligands , Molecular Conformation , Molecular Docking Simulation , Molecular Dynamics Simulation , Molecular Structure , Protein Binding , Quantitative Structure-Activity Relationship , Structure-Activity Relationship
5.
Metallomics ; 13(8)2021 08 19.
Article in English | MEDLINE | ID: mdl-34320190

ABSTRACT

Plants have developed a diversity of strategies to take up and store essential metals in order to colonize various types of soils including mineralized soils. Yet, our knowledge of the capacity of plant species to accumulate metals is still fragmentary across the plant kingdom. In this study, we have used the X-ray fluorescence technology to analyze metal concentration in a wide diversity of species of the Neotropical flora that was not extensively investigated so far. In total, we screened more than 11 000 specimens representing about 5000 species from herbaria in Paris and Cuba. Our study provides a large overview of the accumulation of metals such as manganese, zinc, and nickel in the Neotropical flora. We report 30 new nickel hyperaccumulating species from Cuba, including the first records in the families Connaraceae, Melastomataceae, Polygonaceae, Santalaceae, and Urticaceae. We also identified the first species from this region of the world that can be considered as manganese hyperaccumulators in the genera Lomatia (Proteaceae), Calycogonium (Melastomataceae), Ilex (Aquifoliaceae), Morella (Myricaceae), and Pimenta (Myrtaceae). Finally, we report the first zinc hyperaccumulator, Rinorea multivenosa (Violaceae), from the Amazonas region. The identification of species able to accumulate high amounts of metals will become instrumental to support the development of phytotechnologies in order to limit the impact of soil metal pollution in this region of the world.


Subject(s)
Fluorescence , Manganese/analysis , Nickel/analysis , Plants/metabolism , Zinc/analysis , X-Rays
6.
J Mol Model ; 26(11): 294, 2020 Oct 05.
Article in English | MEDLINE | ID: mdl-33015729

ABSTRACT

Ghrelin is a peptide hormone involved in multiple functions, including growth hormone release stimulation, food intake regulation, and metabolic and cytoprotective effect. A novel family of peptides with internal cycles was designed as ghrelin analogs and the biological activity of two of them (A228 and A233) was experimentally studied in-depth. In this work, an in silico strategy was developed for describing and assessing the binding modes of A228 and A233 to GHS-R1a (ghrelin receptor) comparing it with ghrelin and GHRP-6 peptides. Several reported structures of different G protein coupled receptors were used as templates, to obtain a good quality model of GHS-R1a. The best model was selected by preliminary molecular docking with ghrelin and GHRP-6. Docking was used to estimate peptide orientations in the binding site of the best model, observing a superposition of its N-terminal and its first aromatic residue. To test the complex stability in time, the C-terminal fragments of each peptide were added and the complexes were inserted a 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC) membrane, performing a molecular dynamic simulation for 100 ns using the CHARMM36 force field. Despite of the structural differences, the studied peptides share a common binding mode; the N-terminal interacts with E124 and the aromatic residue close to it, with the aromatic cluster (F279, F309, and F312). A preliminary pharmacophore model, consisting in a positive charged amine and an aromatic ring at an approximate distance of 0.79 nm, can be proposed. The results here described could represent a step forward in the efficient search of new ghrelin analogs.


Subject(s)
Computer Simulation , Peptides/metabolism , Peptides/pharmacology , Receptors, Ghrelin/agonists , Amino Acid Sequence , Animals , Humans , Molecular Docking Simulation , Molecular Dynamics Simulation , Peptides/chemistry , Protein Binding/drug effects , Receptors, Ghrelin/chemistry , Receptors, Ghrelin/metabolism
7.
Mar Pollut Bull ; 156: 111174, 2020 Jul.
Article in English | MEDLINE | ID: mdl-32510356

ABSTRACT

Globally, oxygen concentration in many coastal areas is depleting. River nutrient discharges may produce hypoxia events. The Southern Gulf of Mexico receives the discharges of the Grijalva-Usumacinta River System, the second largest in the Gulf of Mexico. To evaluate the influence of river discharges on dissolved oxygen concentrations in the receiving coastal ecosystem, we studied the variation of physicochemical variables in the water column. During the dry season, the influence of the river waters to the coastal area is scarce, but during the rainy season the river plume reached ~9 km offshore. The lowest concentration of dissolved oxygen (3.6 mg L-1) was observed within the river plume. We concluded that, in the studied area, hypoxia events (oxygen concentrations ≤ 2 mg L-1) would occur during the rainy season, low winds and in deeper waters (>80 m depth).


Subject(s)
Ecosystem , Rivers , Gulf of Mexico , Humans , Hypoxia , Mexico , Seasons
8.
In. Cardellá Rosales, Lidia; Hernández Fernández, Rolando; Vicedo Tomey, Agustín. Bioquímica Médica. Tomo III. Metabolismo intermediario y su regulación. Segunda edición. La Habana, Editorial Ciencias Médicas, 2ed; 2020. , ilus, tab.
Monography in Spanish | CUMED | ID: cum-76691
9.
In. Cardellá Rosales, Lidia; Hernández Fernández, Rolando; Vicedo Tomey, Agustín. Bioquímica Médica. Tomo III. Metabolismo intermediario y su regulación. Segunda edición. La Habana, Editorial Ciencias Médicas, 2ed; 2020. , ilus, tab.
Monography in Spanish | CUMED | ID: cum-76690
10.
In. Cardellá Rosales, Lidia; Hernández Fernández, Rolando; Vicedo Tomey, Agustín. Bioquímica Médica. Tomo III. Metabolismo intermediario y su regulación. Segunda edición. La Habana, Editorial Ciencias Médicas, 2ed; 2020. , ilus, tab.
Monography in Spanish | CUMED | ID: cum-76689
11.
In. Cardellá Rosales, Lidia; Hernández Fernández, Rolando; Vicedo Tomey, Agustín. Bioquímica Médica. Tomo III. Metabolismo intermediario y su regulación. Segunda edición. La Habana, Editorial Ciencias Médicas, 2ed; 2020. , ilus, tab.
Monography in Spanish | CUMED | ID: cum-76688
12.
In. Cardellá Rosales, Lidia; Hernández Fernández, Rolando; Vicedo Tomey, Agustín. Bioquímica Médica. Tomo III. Metabolismo intermediario y su regulación. Segunda edición. La Habana, Editorial Ciencias Médicas, 2ed; 2020. , ilus, tab.
Monography in Spanish | CUMED | ID: cum-76687
13.
In. Cardellá Rosales, Lidia; Hernández Fernández, Rolando; Vicedo Tomey, Agustín. Bioquímica Médica. Tomo III. Metabolismo intermediario y su regulación. Segunda edición. La Habana, Editorial Ciencias Médicas, 2ed; 2020. , ilus, tab.
Monography in Spanish | CUMED | ID: cum-76686
14.
In. Cardellá Rosales, Lidia; Hernández Fernández, Rolando; Vicedo Tomey, Agustín. Bioquímica Médica. Tomo III. Metabolismo intermediario y su regulación. Segunda edición. La Habana, Editorial Ciencias Médicas, 2ed; 2020. , ilus, tab.
Monography in Spanish | CUMED | ID: cum-76685
15.
In. Cardellá Rosales, Lidia; Hernández Fernández, Rolando; Vicedo Tomey, Agustín. Bioquímica Médica. Tomo III. Metabolismo intermediario y su regulación. Segunda edición. La Habana, Editorial Ciencias Médicas, 2ed; 2020. , ilus, tab.
Monography in Spanish | CUMED | ID: cum-76684
16.
In. Cardellá Rosales, Lidia; Hernández Fernández, Rolando; Vicedo Tomey, Agustín. Bioquímica Médica. Tomo III. Metabolismo intermediario y su regulación. Segunda edición. La Habana, Editorial Ciencias Médicas, 2ed; 2020. , ilus, tab.
Monography in Spanish | CUMED | ID: cum-76683
17.
In. Cardellá Rosales, Lidia; Hernández Fernández, Rolando; Vicedo Tomey, Agustín. Bioquímica Médica. Tomo III. Metabolismo intermediario y su regulación. Segunda edición. La Habana, Editorial Ciencias Médicas, 2ed; 2020. , ilus, tab.
Monography in Spanish | CUMED | ID: cum-76682
18.
In. Cardellá Rosales, Lidia; Hernández Fernández, Rolando; Vicedo Tomey, Agustín. Bioquímica Médica. Tomo III. Metabolismo intermediario y su regulación. Segunda edición. La Habana, Editorial Ciencias Médicas, 2ed; 2020. , ilus, tab.
Monography in Spanish | CUMED | ID: cum-76681
19.
In. Cardellá Rosales, Lidia; Hernández Fernández, Rolando; Vicedo Tomey, Agustín. Bioquímica Médica. Tomo III. Metabolismo intermediario y su regulación. Segunda edición. La Habana, Editorial Ciencias Médicas, 2ed; 2020. , ilus, tab.
Monography in Spanish | CUMED | ID: cum-76680
20.
In. Cardellá Rosales, Lidia; Hernández Fernández, Rolando; Vicedo Tomey, Agustín. Bioquímica Médica. Tomo III. Metabolismo intermediario y su regulación. Segunda edición. La Habana, Editorial Ciencias Médicas, 2ed; 2020. , ilus, tab.
Monography in Spanish | CUMED | ID: cum-76679

Subject(s)
Humans , Lipolysis , Biochemistry
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