Biomedical subjects

M Burnet

Publications and source records attributed to M Burnet.

At least 19 recordsLinked to original sources

PubMed2006

Early infiltration of CD8+ macrophages/microglia to lesions of rat traumatic brain injury.

Local inflammatory responses play an important role in mediating secondary tissue damage in traumatic brain injury. Characterization of leukocytic subpopulations contributing to the early infiltration of the damaged tissue might aid in further understanding of lesion development and contribute to definition of cellular targets for selective immunotherapy. In a rat traumatic brain injury model, significant CD8+ cell accumulation was observed 3 days post-injury. The CD8+ cells were strictly distributed to the pannecrotic areas and around the pannecrotic perimeter. The morphology, time course of accumulation and distribution of CD8+ cells were similar to that of reactive ED1+ and endothelial monocyte-activating polypeptide II+ microglia/macrophages, but different from W3/13+ T cells. Further double-labeling experiments confirmed that the major cellular sources of CD8 were reactive macrophages/microglia. Both the location of these CD8+ macrophages/microglia to the border of the pannecrosis and their co-expression of endothelial monocyte-activating polypeptide II and P2X4 receptor suggest they might have a central role in lesion development and might thus be candidates for development of immunotherapeutic, anti-inflammatory strategies.

Animals↗

PubMed2006

Bone morphogenetic protein-6 is expressed early by activated astrocytes in lesions of rat traumatic brain injury.

We have analyzed early expression of bone morphogenetic protein-6 in rat brains subjected to traumatic brain injury. Bone morphogenetic protein-6 was expressed in neurons of the hippocampus and cortex in normal adult rat brains. A pronounced expression of bone morphogenetic protein-6 in astroglia located to the lesion became obvious 48 h postinjury. Bone morphogenetic protein-6(+) glia were distributed around the lesion, thus demarcating the injured tissue from normal brain. Double labeling by immunohistochemistry revealed that the major glial sources for bone morphogenetic protein-6 were reactive astrocytes and few ED1(+) or W3/13(+) cells co-expressed bone morphogenetic protein-6. Furthermore, bone morphogenetic protein-6 expression in neurons located to hippocampus and cortex of the lesioned hemisphere was up-regulated 3 days postinjury. In conclusion, this is the first description of bone morphogenetic protein-6 expression in traumatic brains. Our data suggest that bone morphogenetic protein-6 might be involved in astrogliosis and neuron protection following traumatic brain injury.

Animals↗

PubMed2000

The Spectroscopic Orbit of the Planetary Companion Transiting HD 209458.

We report a spectroscopic orbit with period P=3.52433+/-0.00027 days for the planetary companion that transits the solar-type star HD 209458. For the metallicity, mass, and radius of the star, we derive [Fe/H&sqbr0;=0.00+/-0.02, M*=1.1+/-0.1 M middle dot in circle, and R*=1.2+/-0.1 R middle dot in circle. This is based on a new analysis of the iron lines in our HIRES template spectrum and also on the absolute magnitude, effective temperature, and color of the star, and it uses isochrones from four different sets of stellar evolution models. Using these values for the stellar parameters, we reanalyze the transit data and derive an orbital inclination of i=86&fdg;1+/-1&fdg;6. For the planet, we derive a mass of Mp=0.69+/-0.05 MJup, a radius of Rp=1.40+/-0.17 RJup, and a density of rho=0.31+/-0.07 g cm-3.

Journal Article↗

PubMed1999

Plasma volume expansion with solutions of hemoglobin, albumin, and Ringer lactate in sheep.

We have measured plasma volume expansion (Evans blue and hematocrit changes) and hemodynamic responses in conscious hemorrhaged and normovolemic splenectomized sheep after a 30-min infusion of either 20 ml/kg of diaspirin cross-linked hemoglobin (DCLHb), 20 ml/kg of human albumin (Alb), or 60 ml/kg of a solution of Ringer lactate (RL). All regimens expanded blood volume and increased blood pressure and cardiac output after hemorrhage. However, only 15 +/- 3% of the infused volume of RL was evident as intravascular expansion 10-min postinfusion, compared with 67 +/- 16% and 139 +/- 139% for Alb and DCLHb, respectively. DCLHb infusions were associated with higher blood pressures and lower cardiac outputs compared with RL and Alb infusions, but the increased oxygen content of blood with DCLHb resulted in systemic delivery of oxygen similar to that of the other infusions. These differences in hemodynamics and vascular volume continued for 6 h, and at 24 h vascular volume and all hemodynamics were similar in all three groups. The better volume expansion with DCLHb may be due to greater mobilization of endogenous interstitial protein or reduced transcapillary loss as total intravascular endogenous plasma protein increased after infusion of DCLHb, whereas there was an apparent loss of endogenous intravascular protein after infusions of Alb and RL. Vasoconstriction by DCLHb is one mechanism that could lower blood-to-tissue transport of fluid and protein. In addition to its oxygen-carrying capacity and vasoactivity, DCLHb is associated with volume expansion properties out of proportion to its colloid osmotic pressure.

Animals↗

PubMed1998

cDNA cloning and sequence determination of the pheromone biosynthesis activating neuropeptide of Mamestra brassicae: a new member of the PBAN family.

Sex pheromone biosynthesis in a number of moth species is induced by a conserved 33-amino acid amidated neuropeptide PBAN (pheromone biosynthesis activating neuropeptide). Here, using immunoblotting and bioassay, we present evidence for the presence of a very similar peptide, called Mab-PBAN, in the brain-subesophageal ganglion complex of Mamestra brassicae females. A partial Mab-PBAN encoding cDNA was isolated using 3'RACE. The deduced amino acid sequence for Mab-PBAN is: LADDMPATPADQEMYRPDPEQIDSRTKYFSPRL with a presumed amidated C-terminus. Mab-PBAN has high homology to the other members of the PBAN peptide family: 94% with Hez-PBAN, 87.9% with Lyd-PBAN and 78.8% with Bom-PBAN. The Mab-PBAN gene encodes, beside Mab-PBAN, at least three putative amidated peptides in the same reading frame, all of them having a common C-terminal pentapeptide motif F(T/S)P(R/K)L-NH2.

Amino Acid Sequence↗

PubMed1997

Choline monooxygenase, an unusual iron-sulfur enzyme catalyzing the first step of glycine betaine synthesis in plants: prosthetic group characterization and cDNA cloning.

Plants synthesize the osmoprotectant glycine betaine via the route choline --> betaine aldehyde --> glycine betaine. In spinach, the first step is catalyzed by choline monooxygenase (CMO), a ferredoxin-dependent stromal enzyme that has been hypothesized to be an oligomer of identical subunits and to be an Fe-S protein. Analysis by HPLC and matrix-assisted laser desorption ionization MS confirmed that native CMO contains only one type of subunit (Mr 42,864). Determination of acid-labile sulfur and nonheme iron demonstrated that there is one [2Fe-2S] cluster per subunit, and EPR spectral data indicated that this cluster is of the Rieske type--i.e., coordinated by two Cys and two His ligands. A full-length CMO cDNA (1,622 bp) was cloned from spinach using a probe generated by PCR amplification for which the primers were based on internal peptide sequences. The ORF encoded a 440-amino acid polypeptide that included a 60-residue transit peptide. The deduced amino acid sequence included two Cys-His pairs spaced 16 residues apart, a motif characteristic of Rieske-type Fe-S proteins. Larger regions that included this motif also showed some sequence similarity (approximately 40%) to Rieske-type proteins, particularly bacterial oxygenases. Otherwise there was very little similarity between CMO and proteins from plants or other organisms. RNA and immunoblot analyses showed that the expression of CMO in leaves increased several-fold during salinization. We conclude that CMO is a stress-inducible representative of a new class of plant oxygenases.

Amino Acid Sequence↗

PubMed1994

Osmoprotective compounds in the Plumbaginaceae: a natural experiment in metabolic engineering of stress tolerance.

In common with other zwitterionic quarternary ammonium compounds (QACs), glycine betaine acts as an osmoprotectant in plants, bacteria, and animals, with its accumulation in the cytoplasm reducing adverse effects of salinity and drought. For this reason, the glycine betaine biosynthesis pathway has become a target for genetic engineering of stress tolerance in crop plants. Besides glycine betaine, several other QAC osmoprotectants have been reported to accumulate among flowering plants, although little is known about their distribution, evolution, or adaptive value. We show here that various taxa of the highly stress-tolerant family Plumbaginaceae have evolved four QACs, which supplement or replace glycine betaine-namely, choline O-sulfate and the betaines of beta-alanine, proline, and hydroxyproline. Evidence from bacterial bioassays demonstrates that these QACs function no better than glycine betaine as osmoprotectants. However, the distribution of QACs among diverse members of the Plumbaginaceae adapted to different types of habitat indicates that different QACs could have selective advantages in particular stress environments. Specifically, choline O-sulfate can function in sulfate detoxification as well as in osmoprotection, beta-alanine betaine may be superior to glycine betaine in hypoxic saline conditions, and proline-derived betaines may be beneficial in chronically dry environments. We conclude that the evolution of osmoprotectant diversity within the Plumbaginaceae suggests additional possibilities to explore in the metabolic engineering of stress tolerance in crops.

Aldehyde Oxidoreductases↗

PubMed1985