비만아 부모의 돌봄 경험: q 방법론

Local mussels, Perna viridis, were transplanted from a relatively clean site to various polluted sites in Hong Kong. After a 30-day field exposure, different antioxidant parameters including glutathione S transferase (GST), superoxide dismutase (SOD), catalase (CAT), glutathione peroxidase (GPx), glutathione reductase (GR), NADPH DT-diaphorase (DT-d), glutathione (GSH) and lipid peroxidation were quantified, and tissue concentrations of benzo[a]pyrene (B[a]P) as well as a total of five polycyclic aromatic hydrocarbons (PAHs) with potential carcinogenicity were determined for individual mussels. Results indicated that: (1) tissue concentrations of B[a]P and total PAHs from the same site were highly variable; (2) gill SOD, DT-d and lipid peroxidation showed no response to tissue pollutants: (3) the majority of the antioxidant parameters were induced by increasing tissue pollutant concentrations; and (4) amongst the various parameters, oxyradical scavenger GSH [ best correlated with tissue concentrations of pollutants.

Relationships between tissue concentrations of polycyclic aromatic hydrocarbons and antioxidative responses of marine mussels, Perna viridis

Potential antioxidant and anticoagulant capacity of low molecular weight fucoidan fractions extracted from Laminaria japonica

Pesticide residues in honeybees, honey and bee pollen by LC-MS/MS screening: reported death incidents in honeybees.

http://scholar.ulethbridge.ca/gregpyle/files/3895.pdf

Metal-PAH mixtures in the aquatic environment: a review of co-toxic mechanisms leading to more-than-additive outcomes.

Biomarkers and bioaccumulation of clam Ruditapes philippinarum in response to combined cadmium and benzo[α]pyrene exposure.

Immune responses, ROS generation and the haemocyte damage of scallop Chlamys farreri exposed to Aroclor 1254.

Metabolites analysis, metabolic enzyme activities and bioaccumulation in the clam Ruditapes philippinarum exposed to benzo[a]pyrene.

Glutathione S-transferases (GSTs) are phase II enzymes involved in major detoxification reactions of xenobiotics in many organisms. In this study, a full-length cDNA of GST-pi was cloned from the gill of Venerupis philippinarum by rapid amplification of cDNA ends (RACE) method for the first time. The full-length cDNA of V. philippinarum GST-pi (denoted as VpGSTp) was 1142 bp, with a 5′ untranslated region (UTR) of 87 bp, a 3′ UTR of 438 bp, and an open reading frame (ORF) of 618 bp encoding a protein of 205 amino acid residues with an estimated molecular mass of 23.9 kDa and an predicted isoelectric point (pI) of 7.9. The comparison of the deduced amino acid sequences with GSTs from other species showed that the enzyme belongs to the pi-class, and the amino acids defining the binding sites of glutathione (G-site) and for xenobiotic substrates (H-site) were highly conserved. Tissue distribution analysis of the VpGSTp mRNA revealed that the GST-pi expression level was observed higher in gill, adductor muscle, mantle and foot while lower in digestive gland. Using quantitative real-time PCR, the dose- and time-related effects of benzo[α]pyrene (B[α]P) on VpGSTp mRNA expression were investigated in gills and digestive gland. The results showed that a time-dependant increase in the expression of VpGSTp was induced by B[α]P and appeared a good linear relationship with B[α]P concentrations. All these results suggested that GST-pi in bivalve had an antioxidant role and VpGSTp expression may be a useful biomarker candidate for monitoring environmental contaminants such as PAHs.

Cloning, characterization and tissue distribution of a pi-class glutathione S-transferase from clam (Venerupis philippinarum): Response to benzo[α]pyrene exposure

In this study, the cDNAs of a crustin and an anti-lipopolysaccharide factor (ALF) were cloned from the hemocytes of swimming crab Portunus trituberculatus using rapid amplification of cDNA ends (RACE) approaches. The full-length cDNA of P. trituberculatus crustin (denoted as PtCrustin) was of 584 bp, including an open reading frame (ORF) of 333 bp encoding a 21 amino acids signal peptide and a mature polypeptide of 89 amino acids with the predicted molecular mass of 10.08 kDa. The typical conserved cysteine residues containing WAP domain at the C-terminal displayed high similarity to other crustins. Moreover, the full-length cDNA of P. trituberculatus ALF (denoted as PtALF) was of 1050 bp, including an ORF of 372 bp encoding a 26 amino acids signal peptide and a mature polypeptide of 97 amino acids with the predicted molecular mass of 11.35 kDa. PtALF contained two conserved cysteine residues and showed high similarity to other crab ALFs. Using fluorescent real-time quantitative PCR, PtCrustin mRNA was expressed at the highest level in hemocytes and higher level in stomach while extremely low in hepatopancreas, muscle, gill and heart. In contrast, the PtALF mRNA expression was observed in all tissues. The relative expression levels of PtCrustin and PtALF in hemocytes of P. trituberculatus showed a clear time-dependent response after challenge with Vibrio alginolyticus. These results indicate that PtCrustin and PtALF are two acute-phase proteins involved in the immune responses of P. trituberculatus.

Molecular cloning, characterization and mRNA expression of two antibacterial peptides: crustin and anti-lipopolysaccharide factor in swimming crab Portunus trituberculatus.

Jingjing Miao

Papers

Biomarkers and bioaccumulation of clam Ruditapes philippinarum in response to combined cadmium and benzo[α]pyrene exposure.

Immune responses, ROS generation and the haemocyte damage of scallop Chlamys farreri exposed to Aroclor 1254.

Metabolites analysis, metabolic enzyme activities and bioaccumulation in the clam Ruditapes philippinarum exposed to benzo[a]pyrene.

Cloning, characterization and tissue distribution of a pi-class glutathione S-transferase from clam (Venerupis philippinarum): Response to benzo[α]pyrene exposure

Molecular cloning, characterization and mRNA expression of two antibacterial peptides: crustin and anti-lipopolysaccharide factor in swimming crab Portunus trituberculatus.