The Contribution of Environmental Science to Mental Health Research: A Scoping Review.

Mental health is influenced by multiple complex and interacting genetic, psychological, social, and environmental factors. As such, developing state-of-the-art mental health knowledge requires collaboration across academic disciplines, including environmental science. To assess the current contribution of environmental science to this field, a scoping review of the literature on environmental influences on mental health (including conditions of cognitive development and decline) was conducted.

Exploring the behind metric selection in network analysis: a systematic review.

Unlabelled: Network analysis is a useful tool to analyse the interactions and structure of graphs that represent the relationships among entities, such as sectors within an urban system. Connecting entities in this way is vital in understanding the complexity of the modern world, and how to navigate these complexities during an event. However, the field of network analysis has grown rapidly since the 1970s to produce a vast array of available metrics that describe different graph properties.

Assessing Self-Definition and Relatedness in Level of Personality Functioning.

The two polarities model (TPM) of personality organizes psychological assessment and psychotherapy and connects to personality disorder diagnosis using the Alternative Model for Personality Disorders (AMPD). The authors developed scales assessing the TPM from an existing self-report measure for level of personality functioning (LPF), a core component of the AMPD. Iterative content analyses of the LPF measure yielded scales for Autonomy and Communion corresponding to dimensions of the TPM.

Comparative Content Analysis of Self-Report Scales for Level of Personality Functioning.

Content validity analyses of eight self-report instruments for assessing severity of personality disorder (PD), also known as Level of Personality Functioning (LPF), were conducted using the conceptual scheme of the Alternative Model for Personality Disorders (AMPD; APA, 2013). The item contents of these eight inventories were characterized for the LPF constructs of Identity (ID), Self-Direction (SD), Empathy (EM), and Intimacy (IN) along with the pathological personality trait domains of Negative Affectivity, Detachment, Antagonism, Disinhibition, and Psychoticism. Severity of pathology (SV) reflected in item content was also rated.

Structural requirements for ligand binding by a probable plant vacuolar sorting receptor.

How sorting receptors recognize amino acid determinants on polypeptide ligands and respond to pH changes for ligand binding or release is unknown. The plant vacuolar sorting receptor BP-80 binds polypeptide ligands with a central Asn-Pro-Ile-Arg (NPIR) motif. tBP-80, a soluble form of the receptor lacking transmembrane and cytoplasmic sequences, binds the peptide SSSFADSNPIRPVTDRAASTYC as a monomer with a specificity indistinguishable from that of BP-80.

Molecular cloning and further characterization of a probable plant vacuolar sorting receptor.

BP-80 is a type I integral membrane protein abundant in pea (Pisum sativum) clathrin-coated vesicles (CCVs) that binds with high affinity to vacuole-targeting determinants containing asparagine-proline-isoleucine-arginine. Here we present results from cDNA cloning and studies of its intracellular localization. Its sequence and sequences of homologs from Arabidopsis, rice (Oryza sativa), and maize (Zea mays) define a novel family of proteins unique to plants that is highly conserved in both monocotyledons and dicotyledons.

Interaction of a potential vacuolar targeting receptor with amino- and carboxyl-terminal targeting determinants.

A protein of 80 kD from developing pea (Pisum sativum) cotyledons has previously been shown to exhibit characteristics of a vacuolar targeting receptor by means of its affinity for the amino-terminal vacuolar targeting sequence of proaleurain from barley (Hordeum vulgare). In this report we show that the same protein also binds to the amino-terminal targeting peptide of prosporamin from sweet potato (Ipomoea batatas) and to the carboxyl-terminal targeting determinant of pro-2S albumin from Brazil nut (Bertholletia excelsa). The receptor protein does not bind to the carboxyl-terminal propeptide (representing the targeting sequence) of barley lectin.

Purification and initial characterization of a potential plant vacuolar targeting receptor.

Clathrin-coated vesicles are known to be involved in the transport of proteins from the Golgi to the vacuole in plant cells. The mechanisms by which proteins are directed into this pathway are not known. Here we identify an integral membrane protein of approximately 80 kDa, extracted from clathrin-coated vesicles of developing pea (Pisum sativum L.

Uncoating of clathrin-coated vesicles by uncoating ATPase from developing peas.

A cytosolic ATPase (an enzyme that dissociates clathrin from clathrin-coated vesicles in the presence of ATP) was isolated from developing pea (Pisum sativum L.) cotyledons using chromatography on ATP-agarose. After chromatography on phenyl Sepharose, the fraction with uncoating activity was enriched in a doublet of 70-kD peptides.

Characterization of tonoplast polypeptides isolated from corn seedling roots.

Tonoplast vesicles were isolated by discontinuous sucrose gradient centrifugation in the presence of Mg(2+) from 5 day old corn (Zea mays L., Golden Cross Bantam) seedling roots. Marker enzyme assays indicated only a low degree of cross-contamination of tonoplast vesicles at the 10/23% (weight/weight) interface by other membrane components.

Essential arginine residues in the nitrate uptake system from corn seedling roots.

Three dicarbonyl reagents were used to demonstrate the presence of an essential arginine residue in the NO(3) (-) uptake system from corn seedling roots (Zea mays L., Golden Cross Bantam). Incubation of corn seedlings with 2,3-butanedione (0.

Coated Vesicles Are Involved in the Transport of Storage Proteins during Seed Development in Pisum sativum L.

During seed development, various storage proteins and hydrolases accumulate in specialized storage vacuoles, the protein bodies, via an elaborate intracellular transport system involving the rough endoplasmic reticulum, the Golgi apparatus, and transit vesicles. Clathrin-coated vesicles, similar to those which transport lysosomal proteins to lysosomes, an organelle analogous to the vacuole, in animal cells, could be involved in this intracellular transport mechanism. Clathrin-coated vesicles have been isolated from cotyledons of developing pea (Pisum sativum L.

Isozymes of beta-N-Acetylhexosaminidase from Pea Seeds (Pisum sativum L.).

Four isozymes of beta-N-acetylhexosaminidase (beta-NAHA) from pea seeds (Pisum sativum L.) have been separated, with one, designated beta-NAHA-II, purified to apparent homogeneity by means of an affinity column constructed by ligating p-aminophenyl-N-acetyl-beta-d-thioglucosaminide to Affi-Gel 202. The other three isozymes have been separated and purified 500- to 1750-fold by chromatography on Concanavalin A-Sepharose, Zn(2+) charged immobilized metal affinity chromatography, hydrophobic chromatography, and ion exchange chromatography on CM-Sephadex.

Regulation of nitrite reductase : cell-free translation and processing.

A protein with molecular mass of 67 kilodaltons is immunoprecipitated from in vitro translated products obtained from rabbit reticulocyte lysate primed with polyadenylated RNA from nitrate treated illuminated pea seedlings. This protein resembles the native nitrite reductase because of its competitive elimination when immunoprecipitation of in vitro translated products was carried out in the presence of cold unlabeled nitrite reductase or in vivo labeled pea leaf extract. This protein is of slightly higher molecular weight than that of the native nitrite reductase.

Regulation of synthesis of nitrite reductase in pea leaves: in-vivo and in-vitro studies.

Crude protein extracts from leaves of pea (Pisum sativum L.) labeled with an L-(14)C-amino-acid mixture or [(35)S]methionine, were treated with antibodies prepared against nitrite reductase (NiR; EC 1.6.

Protein bodies and vacuoles as lysosomes : investigations into the role of mannose-6-phosphate in intracellular transport of glycosidases in pea cotyledons.

We have failed to detect the presence of mannose-6-phosphate in the oligosaccharide moiety of glycoproteins from pea (Pisum sativum L. cv Burpeeana) cotyledons using an assay system sensitive to 10 picomoles of mannose-6-phosphate. We were also unable to demonstrate any retention of glycosidase activity from pea seedlings and pea cotyledons on Sepharose-coupled phosphomannosyl receptor proteins isolated from bovine liver which were, however, able to retain phosphomannosylated hexosaminidase purified from Dictyostelium discoideum secretions.

Synthesis and degradation of nitrite reductase in pea leaves.

We have shown in a previous publication (Gupta, Beevers 1983 J Exp Bot 34: 1455-1462) that the level of extractable nitrite reductase activity in pea (Pisum sativum cv Burpeeana) leaves is subject to environmental perturbations. In the current study, we have used rocket immunoelectrophoresis to quantitate the level of nitrite reductase protein in extracts from pea plants subjected to various environmental treatments. The level of nitrite reductase cross-reacting material closely followed the level of assayable nitrite reductase activity.

Sequestration of pea reserve proteins by rough microsomes.

Free polysomes, polysomes released from membranes, and rough microsomal vesicles isolated from developing cotyledons of Pisum sativum L. cv. Burpeeana were used to direct cell-free protein synthesis in a wheat germ system.

What is pea legumin - Is it glycosylated?

Since there is some question as to whether or not legumin is glycosylated, this storage protein was isolated by various procedures from developing cotyledons of Pisum sativum L. supplied with [(14)C]-labeled glucosamine and analyzed by sodium dodecylsulfate-polyacrylamide gel electrophoresis. Legumin isolated by the classical method of Danielsson [(1949) Biochem.

Incorporation of [C]Glucosamine and [C]Mannose into Glycolipids and Glycoproteins in Cotyledons of Pisum sativum L.

Developing pea cotyledons incorporate radioactivity in vivo from [(14)C]glucosamine and [(14)C]mannose into glycolipids and glycoproteins. Several different lipid components are labeled including neutral, ionicnonacidic, and acidic lipids. The acidic lipids labeled in vivo appear similar to the polyisoprenoid lipid intermediates formed in vitro in pea cotyledons.

Glycosylation of pea cotyledon membranes.

Pea cotyledons were injected with d-[(14)C]mannose or d-[(14)C]-glucosamine and incubated for 1 to 1.5 hours. Cotyledons were homogenized and subcellular fractions were isolated by differential centrifugation followed by linear sucrose density gradient centrifugation.

Membrane-associated Glycosyl Transferases in Cotyledons of Pisum sativum: Differential Effects of Magnesium and Manganese Ions.

In crude particulate fractions isolated from pea (Pisum sativum) cotyledons, the transfer of radioactivity from GDP-[(14)C]mannose to glycolipid appears to be preferentially stimulated by Mn(2+) while the transfer to lipid-free residue is enhanced by Mg(2+). In contrast, the transfer of radioactivity from UDP-N-acetyl-[(14)C]glucosamine to glycolipid shows preferential stimulation by Mg(2+) while the transfer to lipid-free residue prefers Mn(2+). These results are accounted for by the differential stimulation by Mg(2+) and Mn(2+) of glycosyl transferases associated with subcellular membranes which were separated by isopycnic sucrose density centrifugation.

Enzymology of Glutamine Metabolism Related to Senescence and Seed Development in the Pea (Pisum sativum L.).

The metabolism of glutamine in the leaf and subtended fruit of the aging pea (Pisum sativum L. cv. Burpeeana) has been studied in relation to changes in the protein, chlorophyll, and free amino acid content of each organ during ontogenesis.