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1.
Environ Sci Technol ; 48(9): 4699-706, 2014 May 06.
Article in English | MEDLINE | ID: mdl-24712677

ABSTRACT

Despite the global importance of As in rice, research has primarily focused on Bangladesh, India, China, and the United States with limited attention given to other countries. Owing to both indigenous As within the soil and the possible increases arising from the onset of irrigation with groundwater, an assessment of As in rice within Cambodia is needed, which offers a "base-case" comparison against sediments of similar origin that comprise rice paddy soils where As-contaminated water is used for irrigation (e.g., Bangladesh). Here, we evaluated the As content of rice from five provinces (Kandal, Prey Veng, Battambang, Banteay Meanchey, and Kampong Thom) in the rice-growing regions of Cambodia and coupled that data to soil-chemical factors based on extractions of paddy soil collected and processed under anoxic conditions. At total soil As concentrations ranging 0.8 to 18 µg g(-1), total grain As concentrations averaged 0.2 µg g(-1) and ranged from 0.1 to 0.37 with Banteay Meanchey rice having significantly higher values than Prey Veng rice. Overall, soil-extractable concentrations of As, Fe, P, and Si and total As were poor predictors of grain As concentrations. While biogeochemical factors leading to reduction of As(V)-bearing Fe(III) oxides are likely most important for predicting plant-available As, husk and straw As concentrations were the most significant predictors of grain-As levels among our measured parameters.


Subject(s)
Arsenic/analysis , Crops, Agricultural/chemistry , Environmental Exposure , Food Contamination/analysis , Oryza/chemistry , Soil Pollutants/analysis , Water Pollutants, Chemical/analysis , Cambodia , Environmental Monitoring , Humans , Iron/analysis , Phosphorus/analysis , Silicon/analysis , Spectrophotometry, Atomic
2.
Am J Physiol Heart Circ Physiol ; 301(2): H497-505, 2011 Aug.
Article in English | MEDLINE | ID: mdl-21602472

ABSTRACT

Secreted protein, acidic, and rich in cysteine (SPARC) is a matricellular protein that functions in the extracellular processing of newly synthesized collagen. Collagen deposition to form a scar is a key event following a myocardial infarction (MI). Because the roles of SPARC in the early post-MI setting have not been defined, we examined age-matched wild-type (WT; n=22) and SPARC-deficient (null; n=25) mice at day 3 post-MI. Day 0 WT (n=28) and null (n=20) mice served as controls. Infarct size was 52 ± 2% for WT and 47 ± 2% for SPARC null (P=NS), indicating that the MI injury was comparable in the two groups. By echocardiography, WT mice increased end-diastolic volumes from 45 ± 2 to 83 ± 5 µl (P < 0.05). SPARC null mice also increased end-diastolic volumes but to a lesser extent than WT (39 ± 3 to 63 ± 5 µl; P < 0.05 vs. day 0 controls and vs. WT day 3 MI). Ejection fraction fell post-MI in WT mice from 57 ± 2 to 19 ± 1%. The decrease in ejection fraction was attenuated in the absence of SPARC (65 ± 2 to 28 ± 2%). Fibroblasts isolated from SPARC null left ventricle (LV) showed differences in the expression of 22 genes encoding extracellular matrix and adhesion molecule genes, including fibronectin, connective tissue growth factor (CTGF; CCN2), matrix metalloproteinase-3 (MMP-3), and tissue inhibitor of metalloproteinase-2 (TIMP-2). The change in fibroblast gene expression levels was mirrored in tissue protein extracts for fibronectin, CTGF, and MMP-3 but not TIMP-2. Combined, the results of this study indicate that SPARC deletion preserves LV function at day 3 post-MI but may be detrimental for the long-term response due to impaired fibroblast activation.


Subject(s)
Extracellular Matrix Proteins/metabolism , Myocardial Infarction/metabolism , Myocardium/metabolism , Osteonectin/metabolism , Ventricular Function, Left , Ventricular Remodeling , Analysis of Variance , Animals , Blotting, Western , Disease Models, Animal , Extracellular Matrix Proteins/genetics , Female , Fibroblasts/metabolism , Gene Expression Profiling/methods , Gene Expression Regulation , Heart Rupture, Post-Infarction/metabolism , Heart Rupture, Post-Infarction/pathology , Male , Mice , Mice, Inbred C57BL , Mice, Knockout , Myocardial Contraction , Myocardial Infarction/diagnostic imaging , Myocardial Infarction/genetics , Myocardial Infarction/physiopathology , Myocardium/pathology , Oligonucleotide Array Sequence Analysis , Osteonectin/deficiency , Osteonectin/genetics , Stroke Volume , Time Factors , Ultrasonography , Ventricular Remodeling/genetics
3.
J Mol Cell Cardiol ; 48(3): 544-9, 2010 Mar.
Article in English | MEDLINE | ID: mdl-19577572

ABSTRACT

The cardiac interstitium is a unique and adaptable extracellular matrix (ECM) that provides a milieu in which myocytes, fibroblasts, and endothelial cells communicate and function. The composition of the ECM in the heart includes structural proteins such as fibrillar collagens and matricellular proteins that modulate cell:ECM interaction. Secreted Protein Acidic and Rich in Cysteine (SPARC), a collagen-binding matricellular protein, serves a key role in collagen assembly into the ECM. Recent results demonstrated increased cardiac rupture, dysfunction and mortality in SPARC-null mice in response to myocardial infarction that was associated with a decreased capacity to generate organized, mature collagen fibers. In response to pressure overload induced-hypertrophy, the decrease in insoluble collagen incorporation in the left ventricle of SPARC-null hearts was coincident with diminished ventricular stiffness in comparison to WT mice with pressure overload. This review will focus on the role of SPARC in the regulation of interstitial collagen during cardiac remodeling following myocardial infarction and pressure overload with a discussion of potential cellular mechanisms that control SPARC-dependent collagen assembly in the heart.


Subject(s)
Extracellular Matrix/metabolism , Fibrillar Collagens/metabolism , Myocardium/metabolism , Osteonectin/metabolism , Animals , Humans , Mice , Models, Biological , Myocardium/pathology , Osteonectin/genetics
4.
J Org Chem ; 62(21): 7278-7287, 1997 Oct 17.
Article in English | MEDLINE | ID: mdl-11671841

ABSTRACT

A new method for the synthesis of N3'-->P5' phosphoramidate oligodeoxynucleotides is demonstrated. Described herein is the synthesis of the monomers utilized in the phosphoramidite amine-exchange process and the experimental details pertaining to this new mode of chain assembly. The phosphoramidite amine-exchange method generates coupling yields in the 92-95% range per cycle and further enables the synthesis of chimeric phosphoramidate/phosphodiester or phosphoramidate/phosphorothioate oligonucleotides with no instrument modifications.

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