Changes in hepatic nitrogen balance in plasma concentrations of amino acids and hormones and in cell volume after overnight fasting in perinatal and adult rat

Important regulatory factors of intrahepatic protein synthesis and proteolysis are amino acids, glucagon, insulin, and cell volume. We have investigated the changes in these factors with development and after an overnight fast and evaluated their contribution to changes in the hepatic nitrogen balance in vivo. In the fed state, glucagon levels were highest in suckling animals and gradually declined in older rats, whereas the concentration of insulin increased during development. The amino acid concentrations in liver and plasma declined during the suckling period to levels that in vitro are highly permissive for induction of autophagic proteolysis. In all age groups investigated, fasting was associated with a drop in hepatic protein content, together with a marked decrease in hepatocellular volume and insulin concentrations. On the other hand, glucagon concentrations and the concentration of many amino acids in plasma and liver responded to fasting with a pronounced decrease in perinatal and suckling animals, but this response had become blunted at weaning and had disappeared in adult animals. These findings suggest that insulin and/or hepatocellular volume are more likely candidates as short-term physiologic regulators of the hepatic nitrogen balance than are glucagon or amino acids. In glucose-supplemented fetuses, high levels of insulin could not compensate for a decreased hepatocellular volume in averting a catabolic state, suggesting that cell volume is the more important factor. Although our study cannot discriminate between the effects of fasting on protein synthesis and degradation, our findings show unequivocally that, for a rapid growth of the liver, suckling animals have to be fed around-the-clock.     

Fission yeast pak1+ encodes a protein kinase that interacts with Cdc42p and is involved in the control of cell polarity and mating

A STE20/p65pak homolog was isolated from fission yeast by PCR. The pak1+ gene encodes a 72 kDa protein containing a putative p21-binding domain near its amino-terminus and a serine/threonine kinase domain near its carboxyl-terminus. The Pak1 protein autophosphorylates on serine residues and preferentially binds to activated Cdc42p both in vitro and in vivo. This binding is mediated through the p21 binding domain on Pak1p and the effector domain on Cdc42p. Overexpression of an inactive mutant form of pak1 gives rise to cells with markedly abnormal shape with mislocalized actin staining. Pak1 overexpression does not, however, suppress lethality associated with cdc42-null cells or the morphologic defeat caused by overexpression of mutant cdc42 alleles. Gene disruption of pak1+ establishes that, like cdc42+, pak1+ function is required for cell viability. In budding yeast, pak1+ expression restores mating function to STE20-null cells and, in fission yeast, overexpression of an inactive form of Pak inhibits mating. These results indicate that the Pak1 protein is likely to be an effector for Cdc42p or a related GTPase, and suggest that Pak1p is involved in the maintenance of cell polarity and in mating.     

Structural and functional analogy between pneumolysin and proaerolysin

Pneumolysin and proaerolysin are bacterial toxins that form pores in host cells by oligomerization. We propose that they may have similar structures despite a poor sequence identity. The crystal structure of proaerolysin reveals a protein composed of four domains, arranged in the shape of an elongated comma. Electron microscopy of the pneumolysin monomer shows a similar arrangement of domains. The sequence of pneumolysin recognizes the template of proaerolysin from a library of protein folds. A three-dimensional model of pneumolysin has been constructed by the comparative approach using the structure of proaerolysin. This model, together with results on the activity of site- specific mutants and the positions of antigenic sites, has been used to propose functional roles of individual domains.      

Interpreting enhanced Hg oxidation with Br addition at Plant Miller

This paper introduces the first detailed reaction mechanisms for Br/Hg chemistry in flue gas, and interprets the Hg oxidation performance across a broad range of Br injection rates in recent field tests at Plant Miller. Homogeneous chemistry with Br species is much faster than with Cl species because the Br atom concentrations at the furnace exit are three to four orders of magnitude greater. The dominant channels with Br are analogous to those for Cl, whereby a Br atom partially oxidizes Hg⁰ into HgBr which is then oxidized into HgBr₂ by Br₂. Mercury also oxidizes heterogeneously on unburned carbon (UBC) with Br species. This mechanism is also analogous to the surface mechanism for Cl species, except that (i) Hg⁰ adsorption is faster on brominated sites and (ii) the high Br atom concentrations promote recombination reactions which maintain very low surface coverages of Hg/Br species. Hence, Br addition does not promote the production of particulate-Hg. Catalytic Hg⁰ oxidation on SCR monoliths by Br species is more than 40 times faster than by Cl species and follows a similar mechanism. For all Br loadings over 10 ppmw in the field tests, essentially all Hg⁰ entering the SCR was oxidized.     

Unique peptide maps of the three largest proteins specified by the flavivirus Kunjin

Tryptic digests of four polypeptides found in Kunjin virus-infected Vero cells, NV5, NV4, V3, and NV3, were compared by peptide mapping. The polypeptides to be analyzed were labeled with radioactive methionine and separated by electrophoresis through polyacrylamide gels containing sodium dodecyl sulfate. Because infection of Vero cells by Kunjin virus does not inhibit host cell protein synthesis, radioactively labeled viral polypeptides prepared from infected cells migrate coincidentally during sodium dodecyl sulfate-gel electrophoresis with some of the labeled host proteins. Thus, the genuine viral methionine-containing peptides in tryptic digests of viral proteins have been identified by co-analyzing polypeptides from [3H]methionine-labeled uninfected cells and [35S]methionine-labeled infected cells and determining the 35S/3H ratio in the peptides resolved in two dimensions on thin-layer chromatography plates. The peptide map of NV3 demonstrated that it is host coded, whereas NV5, NV4, and V3 have unique peptide maps and, therefore, account for approximately one-half of the coding potential of Kunjin virus RNA.     

Spontaneous buccolinguofacial dyskinesia in the elderly

Buccolinguofacial dyskinesia consists of repetitive, non-rhythmic abnormal movements which occur at the speed of normal voluntary movement. To the observer they do not suggests a normal activity of mastication or phonation. This type of dyskinesia was evidenced in 88 patients out of a total of 240 elderly examined. It is more frequent in females than in males. Incidence does not increase with age. Frequency is highly variable individually. Every subject seems to have a comparatively stable frequency of his own. Dyskinesia is reduced or suppressed by neuroleptics, whereas stereotyped movements of the limbs are not affected. Individualization of bucolinguofacial dyskinesia from other abnormal movements should consequently rest on both its clinical features and its pharmacological sensitivity.