Selective IL-27 production by intestinal regulatory T cells permits gut-specific regulation of T17 cell immunity.

Regulatory T cells (T cells) are instrumental in establishing immunological tolerance. However, the precise effector mechanisms by which T cells control a specific type of immune response in a given tissue remains unresolved. By simultaneously studying T cells from different tissue origins under systemic autoimmunity, in the present study we show that interleukin (IL)-27 is specifically produced by intestinal T cells to regulate helper T17 cell (T17 cell) immunity.

miR-15/16 clusters restrict effector Treg cell differentiation and function.

Effector regulatory T cells (eTregs) exhibit distinct homeostatic properties and superior suppressor capacities pivotal for controlling immune responses mediated by their conventional T cell counterpart. While the role of microRNAs (miRNAs) in Tregs has been well-established, how miRNAs regulate eTregs remains poorly understood. Here, we demonstrate that miR-15/16 clusters act as key regulators in limiting eTreg responses.

Altruistic and Private Values For Saving Lives With an Oyster Consumption Safety Program.

We use data from an Internet-based survey and estimate the benefits of an oyster consumption safety policy with the contingent valuation method. In addition to providing a context-specific estimate of willingness-to-pay for oyster safety, we consider an important issue in the contingent valuation mortality risk reduction literature. A number of studies find that willingness-to-pay for mortality risk reduction is not sensitive to the scope of the risk change.

Molecular markers in breeding for virus resistance in barley.

The soil-borne barley yellow mosaic virus disease (BaMMV, BaYMV, BaYMV-2) and the aphid-transmitted barley yellow dwarf virus (BYDV) are serious threats to winter barley cultivation. Resistance to barley yellow mosaic virus disease has been identified in extensive screening programmes and several recessive resistance genes have been mapped, e.g.

Turnover of matrix proteins in mammalian mitochondria.

In cultured hepatocytes the turnover of several mitochondrial matrix proteins (e.g. acetyl-CoA acetyltransferase) appears to be initiated by CoA-mediated, sequential transformation into CoA-modified forms.

Molecular and serological relationships of Spartina mottle virus (SpMV) strains from Spartina spec. and from Cynodon dactylon to other members of the Potyviridae.

Spartina mottle virus (SpMV) was first reported 1980 and classified by physical and biological properties as a tentative member of the genus Rymovirus in the Potyviridae. This genus was recently separated into two genera: Rymovirus and Tritimovirus. Now the sequence of the 3'-terminal part of the genome of SpMV was determined.

Soil-borne rye mosaic and European wheat mosaic virus: two names for a furovirus with variable genome properties which is widely distributed in several cereal crops in Europe.

PCR and nucleotide sequence analyses have revealed that Soil-borne rye mosaic furovirus (SBRMV) which we have recently described is widely distributed in Europe. In Northern Germany, Poland and Denmark the virus affects mainly rye and triticale, but in France and Italy it is wheat which becomes infected. The partial RNA 1 and RNA 2 sequences which were determined for the various SBRMV sources form several clusters, but so far no correlation between molecular differences and the type of host which becomes infected under natural conditions was detected.

Molecular characterization of a new furovirus mainly infecting rye.

The complete or almost complete nucleotide sequences were determined for the two RNAs of three different sources of a new furovirus which mainly infects rye and for which the name Soil-borne rye mosaic furovirus (SBRMV) is proposed. The genome organization of this virus is virtually identical to that of Soil-borne wheat mosaic furovirus (SBWMV). However, SBRMV and SBWMV differ considerably in the nucleotide sequences of their genomes and in the derived amino acid sequences of their putative gene products.

First Report of Soilborne Rye Mosaic Virus in Rye in Denmark.

Soilborne wheat mosaic furovirus (SBWMV)-like particles were detected in rye (Secale cereale) grown in sandy soil in West Zealand during spring 1999. Infected plants showed yellow leaf mosaic and light stunting. Electron microscopy of negatively stained crude sap preparations revealed rigid rod-shaped particles with two average lengths, 296 and 162 nm; average diameter was 23 nm.

Immunochemical detection of CoA-modified mitochondrial matrix proteins.

An in vitro assay mixture consisting of mitochondrial matrix proteins from rat liver and CoA resulted in the formation of CoA-modified proteins. CoA-modified proteins were demonstrated by detection of CoA. CoA was released from the proteins by dithioerythritol treatment under denaturing conditions and was identified by (a) its retention time on HPLC, (b) its absorption spectrum and (c) its activity in a CoA-specific assay.

Turnover and transformation of mitochondrial acetyl-CoA acetyltransferase into CoA-modified forms.

Rat liver mitochondrial acetyl-CoA acetyltransferase (acetoacetyl-CoA thiolase, EC 2.3.1.

Differentiation of the four viruses of the sugarcane mosaic virus subgroup based on cytopathology.

A cytological comparison has been made of representative isolates of johnsongrass mosaic (JGMV), maize dwarf mosaic (MDMV), sorghum mosaic (SrMV) and sugarcane mosaic (SCMV) viruses. These four viruses now encompass the complex of virus strains which were formerly considered as strains of sugarcane mosaic and/or maize dwarf mosaic viruses. The structure of the cytoplasmic cylindrical inclusions induced by these viruses, together with other cytological alterations, allow the four viruses to be distinguished.

Identification of the CoA-modified forms of mitochondrial acetyl-CoA acetyltransferase and of glutamate dehydrogenase as nearest-neighbour proteins.

A 52 kDa protein could only be co-purified with the CoA-modified forms of acetyl-CoA acetyltransferase (acetoacetyl-CoA thiolase) (EC 2.3.1.

Evidence for an in vivo modification of mitochondrial proteins by coenzyme A.

Following denaturation of mitochondrial proteins by sodium dodecyl sulfate, a [1-14C]pantothenic acid-derived radioactivity proved to be acid precipitable in the outer membrane, the intermembrane space, the inner membrane and in the matrix of rat liver mitochondria, where it had the highest specific radioactivity of 541 +/- 29 cpm/100 micrograms protein. This tightly and/or covalently bound protein radioactivity could be released by incubation in the presence of dithioerythreitol; it was identified as [14C]coenzyme A by its HPLC retention time, its absorption spectrum and its radioactivity. This acid-stable and thiol-labile coenzyme A-binding apparently refers to specific protein binding sites.

Barley yellow mosaic virus (BaYMV) and BaYMV-M: two different viruses.

Serological and physical properties of isolated particles as well as reactions of barley cultivars after virus inoculation showed that the yellow disease of barley is caused by different viruses. Results summarized in this paper suggest that the European isolates BaYMV-So and BaYMV-NM are closely related to, or identical with, BaYMV-J first reported from Japan, whereas BaYMV-M differs in several properties. Therefore, it seems justified to describe BaYMV-M as a separate virus tentatively designated barley mild mosaic virus.

Identification of [1-14C]pantothenic-acid-mediated modified mitochondrial proteins.

The in vivo administration of [1-14C]pantothenic acid, which is the precursor of coenzyme A, resulted in the radioactive labelling of several mitochondrial proteins in rat liver. The incorporated radioactivity could be released by glutathione or 2-mercaptoethanol. Two mitochondrial matrix proteins acetyl-CoA acetyltransferase (liver and heart), an enzyme involved in the biosynthesis or degradation of ketone bodies, and 3-oxoacyl-CoA thiolase (liver), a protein participating in fatty acid oxidation were identified as modified proteins.

Mitochondrial acetyl-CoA acetyltransferase in liver and extrahepatic tissues: role of modification by coenzyme A.

The influence of clofibrate and di(2-ethylhexyl)phthalate on mitochondrial acetyl-CoA acetyltransferase (acetyl-CoA: acetyl-CoA C-acetyltransferase, EC 2.3.1.

Mitochondrial acetyl-CoA acetyltransferase in various organs from rat: form patterns and coenzyme-A-mediated modification.

The mitochondrial acetyl-CoA acetyltransferase (acetyl-CoA:acetyl-CoA C-acetyltransferase, EC 2.3.1.

On the mechanism of the chemical modification of the mitochondrial acetyl-CoA acetyltransferase by coenzyme A.

The liver mitochondrial acetyl-CoA acetyltransferase (acetyl-CoA:acetyl-CoA C-acetyltransferase, EC 2.3.1.

Modulation of rat-liver mitochondrial acetyl-CoA acetyltransferase activity by a reversible chemical modification with coenzyme A.

The mitochondrial acetyl-CoA acetyltransferase (acetoacetyl-CoA thiolase, EC 2.3.1.

Regulation of ketogenesis. Mitochondrial acetyl-CoA acetyltransferase from rat liver: initial-rate kinetics in the presence of the product CoASH reveal intermediary plateau regions.

The analysis of the initial-rate kinetics of the liver mitochondrial acetyl-CoA acetyltransferase (acetoacetyl-CoA thiolase) in the direction of acetoacetyl-CoA synthesis under product inhibition was performed. 1. Acetyl-CoA acetyltransferase shows a hyperbolic response of reaction velocity to changes in acetyl-CoA concentrations with an apparent Km of 0.

The charge heterogeneity of the mitochondrial acetyl-CoA acetyltransferase from rat liver.

The charge heterogeneity of the mitochondrial acetyl-CoA acetyltransferase (EC 2.3.1.

Threshold noise and the laser transient.

The energy in a laser cavity at threshold affects the time required for the laser to go from threshold to saturation. By determining the statistical distribution of laser turn-on times, i.e.

Immunochemical aspects, molecular and kinetic properties of multiple forms of acetyl-CoA acetyltransferase from rat liver mitochondria.

Acetyl-CoA acetyltransferase (EC 2.3.1.