[Research progress on health hazards and occupational protection of prolymethylmethacrylate bone cement in the operating room].

There are many occupational risk factors in operating room work. Polymethyl methacrylate (PMMA) , as a kind of common bone filling and repairing material, is widely used in the fixation of artificial joints, oral braces and orthopedic prosthesis. However, PMMA will release methyl methacrylate (MMA) monomer when it is implanted into human tissues and polymerized to harden, which is toxic to the body. This paper analyzes harmful factors in using PMMA bone cement, and then explores corresponding occupational protection knowledge, in order to reduce the occurrence of occupational hazards related to PMMA bone cement and enhance the self-protection ability of the operation room medical staff.

Achieving biological nitrogen removal via nitrite by salt inhibition.

The principal aim of this paper is to develop and evaluate an approach to obtain nitrogen removal bypassing nitrate. The method is based on the addition of sodium chloride (NaCI), selective inhibitor of nitrite oxidizers, to influent. Validation of the new method was conducted on laboratory-scale experiments applying the SBR activated sludge process to domestic wastewater with low C/N ratio. With the aerobic-anoxic sequence, three parallel SBRs achieving complete nitrification-denitrification are dosed by a certain concentration of NaCI to influent. The high nitrite accumulation, depending on the salinity in the influent and the application duration of salt, was obtained in SBRs treating saline wastewater. Optimum dosage and application duration of salt, which interact to determine the performance and stabilization of nitrite accumulation, were determined by experiment. In order to evaluate the method, the response of the biological treatment system to salt concentration was also explored. The repeatability of the method was further verified under various operational conditions. Microbial population tests supported the presumption that nitrite oxidizers are inhibited by salt addition and washed out of the system. The presented method is valuable to offer a solution to realize nitrogen removal via nitrite under normal conditions.

Interaction between the conserved region in the C-terminal domain of GRK2 and rhodopsin is necessary for GRK2 to catalyze receptor phosphorylation.

The C-terminal domain of G protein-coupled receptor kinases (GRKs) consists of a conserved region and a variable region, and the variable region has been shown to direct the membrane translocation of cytosolic enzymes. The present work has revealed that the C-terminal domain may also be involved in kinase-receptor interaction that is primarily mediated by the conserved region. Truncation of the C-terminal domain or deletion of the conserved region in this domain of GRK2 resulted in a complete loss of its ability to phosphorylate rhodopsin and in an obvious decrease in its sensitivity to receptor-mediated phosphorylation of a peptide substrate. On the contrary, deletion of the betagamma subunit binding region in the C-terminal domain of GRK2 did not significantly alter the ability of the enzyme to phosphorylate rhodopsin. In addition, the recombinant proteins that represent the C-terminal domain and the conserved region of GRK2 could inhibit GRK2-mediated phosphorylation of rhodopsin and receptor-mediated activation of GRK2 but not GRK2-mediated phosphorylation of the peptide substrate. Furthermore, the conserved region as well as the C-terminal domain could directly bind rhodopsin in vitro. These results indicate that the C-terminal domain, or more precisely, the conserved region of this domain, is important for enzyme-receptor interaction and that this interaction is required for GRK2 to catalyze receptor phosphorylation.

The amino terminus with a conserved glutamic acid of G protein-coupled receptor kinases is indispensable for their ability to phosphorylate photoactivated rhodopsin.

To investigate functions of the consensus amino terminus of G protein-coupled receptor kinases (GRKs), two amino terminus-truncated mutants (delta30 or delta15) and two single-amino-acid mutants of conserved acidic residues (D2A or E7A) of human GRK1 were constructed and expressed in human embryonic kidney 293 cells. It was shown that truncated mutations and one single-point mutation (E7A) greatly decreased GRK1's activity to phosphorylate photoactivated rhodopsin (Rho*), whereas the abilities of these mutants to phosphorylate a synthetic peptide substrate and to translocate from cytosol to rod outer segments on light activation were unaffected. Further experiments demonstrated that the same truncated mutations (delta30 or delta15) of GRK2, representative of another GRK subfamily, also abolished the kinase's activity toward Rho*. The similar single-point mutation (E5A) of GRK2 heavily impaired its phosphorylation of Rho* but did not alter its ability to phosphorylate the peptide, and the G329-rhodopsin-augmented peptide phosphorylation by GRK2 (E5A) remained unchanged. Our data, taken together, suggest that the amino terminus as well as a conserved glutamic acid in the region of GRKs appears essential for their ability to functionally interact with G protein-coupled receptors.