Background and aims Biochar has attracted research interest due to its ability to increase the soil carbon pool and improve crop productivity. The objective of this study was to evaluate the metal immobilizing impact of chicken manure-and green waste-derived biochars, and their effectiveness in promoting plant growth. Methods The immobilization and phytoavailability of Cd, Cu and Pb was examined using naturally contaminated shooting range and spiked soils. Biochar samples prepared from chicken manure and green waste were used as soil amendments. Results Application of biochar significantly reduced NH 4 NO 3 extractable Cd, Cu and Pb concentrations of soils, indicating the immobilization of these metals. Chicken manure-derived biochar increased plant dry biomass by 353 and 572% for shoot and root, respectively with 1% of biochar addition. This might be attributed to reduced toxicity of metals and increased availability of nutrients such as P and K. Both biochars significantly reduced Cd, Cu and Pb accumulation by Indian mustard (Brassica juncea), and the reduction increased with increasing amount of biochar application except Cu concentration. Metal sequential fractionation data indicated that biochar treatments substantially modified the partitioning of Cd, Cu and Pb from the easily exchangeable phase to less bioavailable organic bound fraction.Conclusions The results clearly showed that biochar application was effective in metal immobilization, thereby reducing the bioavailability and phytotoxicity of heavy metals.
Starch synthase IIIa (SSIIIa)-deficient rice (Oryza sativa) mutants were generated using retrotransposon insertion and chemical mutagenesis. The lowest migrating SS activity bands on glycogen-containing native polyacrylamide gel, which were identified to be those for SSIIIa, were completely absent in these mutants, indicating that they are SSIIIa null mutants. The amylopectin B 2 to B 4 chains with degree of polymerization (DP) $ 30 and the M r of amylopectin in the mutant were reduced to about 60% and 70% of the wild-type values, respectively, suggesting that SSIIIa plays an important part in the elongation of amylopectin B 2 to B 4 chains. Chains with DP 6 to 9 and DP 16 to 19 decreased while chains with DP 10 to 15 and DP 20 to 25 increased in the mutants amylopectin. These changes in the SSIIIa mutants are almost opposite images of those of SSI-deficient rice mutant and were caused by 1.3-to 1.7-fold increase of the amount of SSI in the mutants endosperm. Furthermore, the amylose content and the extralong chains (DP $ 500) of amylopectin were increased by 1.3-and 12-fold, respectively. These changes in the composition in the mutants starch were caused by 1.4-to 1.7-fold increase in amounts of granules-bound starch synthase (GBSSI). The starch granules of the mutants were smaller with round shape, and were less crystalline. Thus, deficiency in SSIIIa, the second major SS isozyme in developing rice endosperm affected the structure of amylopectin, amylase content, and physicochemical properties of starch granules in two ways: directly by the SSIIIa deficiency itself and indirectly by the enhancement of both SSI and GBSSI gene transcripts.
Osteoclasts are bone-resorbing cells that are derived from hematopoietic precursor cells and require macrophage-colony stimulating factor and receptor activator of nuclear factor-κB ligand (RANKL) for their survival, proliferation, differentiation, and activation. The binding of RANKL to its receptor RANK triggers osteoclast precursors to differentiate into osteoclasts. This process depends on RANKL-RANK signaling, which is temporally regulated by various adaptor proteins and kinases. Here we summarize the current understanding of the mechanisms that regulate RANK signaling during osteoclastogenesis. In the early stage, RANK signaling is mediated by recruiting adaptor molecules such as tumor necrosis factor receptor-associated factor 6 (TRAF6), which leads to the activation of mitogen-activated protein kinases (MAPKs), and the transcription factors nuclear factor-κB (NF-κB) and activator protein-1 (AP-1). Activated NF-κB induces the nuclear factor of activated T-cells cytoplasmic 1 (NFATc1), which is the key osteoclastogenesis regulator. In the intermediate stage of signaling, the co-stimulatory signal induces Ca2+ oscillation via activated phospholipase Cγ2 (PLCγ2) together with c-Fos/AP-1, wherein Ca2+ signaling facilitates the robust production of NFATc1. In the late stage of osteoclastogenesis, NFATc1 translocates into the nucleus where it induces numerous osteoclast-specific target genes that are responsible for cell fusion and function.
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