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1.
J Comp Pathol ; 164: 27-31, 2018 Oct.
Article in English | MEDLINE | ID: mdl-30360909

ABSTRACT

Yersinia pseudotuberculosis and Yersinia enterocolitica are ubiquitous pathogens with wildlife and domestic animal reservoirs. Outbreaks of 'non-plague' yersiniosis in man and non-human primates are reported frequently (including zoological specimens and research breeding colonies) and are usually characterized by enteritis, mesenteric lymphadenitis and occasionally organ abscessation. In people, non-septic reactive arthritis is a common sequela to yersiniosis. However, there have been rare reports in people of septic arthritis and osteomyelitis because of active systemic infection with Y. pseudotuberculosis. Osteomyelitis has also been reported rarely in historical yersiniosis outbreaks in farmed turkeys in England and the USA. This paper reports the first case of osteomyelitis caused by systemic infection with Y. pseudotuberculosis O:1 in a non-human primate, a captive ring-tailed lemur (Lemur catta). The lemur had a short clinical history of hyporexia and weight loss with reduction in mobility, especially of the left hindlimb. On post-mortem examination there was evidence of multi-organ abscessation. In addition, severe necrosis, inflammation and large bacterial colonies were present in the musculature, periosteum and bone marrow in the hip, ribs and a vertebra at the cervicothoracic junction. Osteomyelitis should be considered as a rare clinical presentation in non-human primates with systemic Y. pseudotuberculosis infection.


Subject(s)
Lemur , Osteomyelitis/veterinary , Yersinia pseudotuberculosis Infections/veterinary , Animals , Male , Yersinia pseudotuberculosis
2.
New Microbes New Infect ; 22: 4-5, 2018 Mar.
Article in English | MEDLINE | ID: mdl-29556400

ABSTRACT

Acinetobacter species can be important opportunistic pathogens in humans, especially in healthcare settings. We report here the first isolation of Acinetobacter ursingii from an animal species; it was isolated from a canine urinary tract infection, and phenotypic identification proved unreliable.

3.
Parasitology ; 142(9): 1190-5, 2015 Aug.
Article in English | MEDLINE | ID: mdl-26027539

ABSTRACT

The nematode Angiostrongylus vasorum is becoming more widely recorded globally, and is of increasing concern as a cause of disease in dogs. Apparent geographic spread is difficult to confirm due to a lack of standardized disease recording systems, increasing awareness among veterinary clinicians, and recent improvements in diagnostic technologies. This study examines the hypothesis that A. vasorum has spread in recent years by repeating the methods of a previous survey of the fox population. The hearts and lungs of 442 foxes from across Great Britain were collected and examined by dissection and flushing of the pulmonary circulation and microscopic inspection of tracheal scrapes. Sampling and parasite extraction methods were identical to an earlier survey in 2005 to ensure comparability. Prevalence of A. vasorum was 18·3% (exact binomial confidence bounds 14·9-22·3), compared with 7·3% previously (5·3-9·9, n = 546), and had increased significantly in most regions, e.g. 7·4% in the Northern UK (previously zero) and 50·8% in the south-east (previously 23·2%). Other nematodes identified were Crenosoma vulpis (prevalence 10·8%, CI 8·1-14·2) and Eucoleus aerophilus (31·6%, CI 27·3-36·2). These data support the proposal that A. vasorum has increased in prevalence and has spread geographically in Great Britain.


Subject(s)
Angiostrongylus/classification , Foxes , Strongylida Infections/veterinary , Animals , Climate Change , Strongylida Infections/epidemiology , United Kingdom/epidemiology
4.
Brain Res ; 919(2): 292-301, 2001 Nov 23.
Article in English | MEDLINE | ID: mdl-11701141

ABSTRACT

We examined the effects of hippocampus (Hp) and area parahippocampalis (APH) lesions in pigeons on their ability to perform a battery of tasks including autoshaping, time discrimination, spatial memory, and pattern discrimination. Pigeons with Hp-APH lesions were impaired in the acquisition of an autoshaped response, emitting fewer pecks to the stimulus than control animals. Hp-APH pigeons were also impaired in the acquisition of a radial-arm maze analogue task, and those birds that did learn the task seemed to do so by adopting a stereotypic response strategy. In contrast, Hp-APH lesions had no effect on the ability of the birds to discriminate on the basis of either temporal or visual information. Overall, these studies complement our earlier studies and suggest that the avian hippocampus is important for the processing and retention of spatial rather than non-spatial information.


Subject(s)
Columbidae/physiology , Hippocampus/physiology , Memory/physiology , Orientation/physiology , Psychomotor Performance/physiology , Space Perception/physiology , Time Perception/physiology , Animals , Behavior, Animal/physiology , Columbidae/anatomy & histology , Denervation , Discrimination Learning/physiology , Hippocampus/cytology , Hippocampus/injuries , Maze Learning/physiology
5.
Science ; 290(5497): 1782-6, 2000 Dec 01.
Article in English | MEDLINE | ID: mdl-11099420

ABSTRACT

Area 5 in the parietal lobe of the primate brain is thought to be involved in monitoring the posture and movement of the body. In this study, neurons in monkey area 5 were found to encode the position of the monkey's arm while it was covered from view. The same neurons also responded to the position of a visible, realistic false arm. The neurons were not sensitive to the sight of unrealistic substitutes for the arm and were able to distinguish a right from a left arm. These neurons appear to combine visual and somatosensory signals in order to monitor the configuration of the limbs. They could form the basis of the complex body schema that we constantly use to adjust posture and guide movement.


Subject(s)
Body Image , Neurons/physiology , Parietal Lobe/physiology , Proprioception , Visual Perception , Animals , Arm , Cues , Humans , Macaca fascicularis , Male , Neural Pathways , Parietal Lobe/cytology
6.
J Biol Chem ; 273(45): 29530-9, 1998 Nov 06.
Article in English | MEDLINE | ID: mdl-9792661

ABSTRACT

We determined the contribution of all major energy substrates (glucose, glycogen, lactate, oleate, and triglycerides) during an acute increase in heart work (1 microM epinephrine, afterload increased by 40%) and the involvement of key regulatory enzymes, using isolated working rat hearts exhibiting physiologic values for contractile performance and oxygen consumption. We accounted for oxygen consumption quantitatively from the rates of substrate oxidation, measured on a minute-to-minute basis. Total beta-oxidation (but not exogenous oleate oxidation) was increased by the work jump, consistent with a decrease in the level of malonyl-CoA. Glycogen and lactate were important buffers for carbon substrate when heart work was acutely increased. Three mechanisms contributed to high respiration from glycogen: 1) carbohydrate oxidation was increased selectively; 2) stimulation of glucose oxidation was delayed at glucose uptake; and 3) glycogen-derived pyruvate behaved differently from pyruvate derived from extracellular glucose. Despite delayed activation of pyruvate dehydrogenase relative to phosphorylase, glycogen-derived pyruvate was more tightly coupled to oxidation. Also, glycogen-derived lactate plus pyruvate contributed to an increase in the relative efflux of lactate versus pyruvate, thereby regulating the redox. Glycogen synthesis resulted from activation of glycogen synthase late in the protocol but was timed to minimize futile cycling, since phosphorylase a became inhibited by high intracellular glucose.


Subject(s)
Heart/physiology , Myocardium/metabolism , Animals , Energy Metabolism , Fatty Acids/metabolism , Glucose/metabolism , Glycogen/metabolism , Glycogen Synthase/metabolism , Glycolysis , Male , Malonyl Coenzyme A/metabolism , Myocardial Contraction , Myocardium/enzymology , Oxidation-Reduction , Oxygen Consumption , Pyruvates/metabolism , Rats , Rats, Sprague-Dawley , Triglycerides/metabolism
9.
Biochim Biophys Acta ; 1134(1): 61-72, 1992 Feb 19.
Article in English | MEDLINE | ID: mdl-1311959

ABSTRACT

Extracellular ATP and UTP caused increases in the concentration of cytoplasmic free calcium ([Ca2+]i) and the intracellular level of inositol 1,4,5-trisphosphate (IP3), a second messenger for calcium mobilization, prior to the release of prostacyclin (PGI2) from cultured bovine pulmonary artery endothelial (BPAE) cells. The agonist specificity and dose-dependence were similar for nucleotide-mediated increases in IP3 levels, [Ca2+]i and PGI2 release. An increase in [Ca2+]; and PGI2 release was observed after addition of ionomycin, a calcium ionophore, to BPAE cells incubated in a calcium-free medium. The addition of ATP to the ionomycin-treated cells caused no further increase in [Ca2+]i or PGI2 release. The inability of ATP to cause an increase in [Ca2+]i or PGI2 release in ionomycin-treated cells was apparently due to the ionomycin-dependent depletion of intracellular calcium stores since the subsequent addition of extracellular calcium caused a significant increase in both [Ca2+]i and PGI2 release. Introduction of BAPTA, a calcium buffer, into BPAE cells inhibited ATP-mediated increases in [Ca2+]i and PGI2 release, further evidence that PGI2 release is dependent upon an increase in [Ca2+]i. The increase in [Ca2+]i elicited by ATP apparently caused the activation of a calmodulin-dependent phospholipase A2 since trifluoperazine, an inhibitor of calmodulin, and quinacrine, an inhibitor of phospholipase A2, prevented the stimulation of PGI2 release by ATP. Furthermore, ATP caused the specific hydrolysis of [14C]arachidonyl-labeled phosphatidylcholine and the generation of free arachidonic acid, the rate-limiting substrate for PGI2 synthesis, prior to the release of PGI2 from BPAE cells. These findings suggest that the increase in PGI2 release elicited by ATP and UTP is at least partially dependent upon a phospholipase C-mediated increase in [Ca2+]i and the subsequent activation of a phosphatidylcholine-specific phospholipase A2. ATP analogs modified in the adenine base or phosphate moiety caused PGI2 release with a rank order of agonist potency of adenosine 5'-O-(2-thiodiphosphate) (ADP beta S) greater than 2-methylthioATP (2-MeSATP) greater than ATP, whereas alpha, beta methyleneATP and beta, gamma methyleneATP had no effect on PGI2 release.


Subject(s)
Adenosine Triphosphate/pharmacology , Endothelium, Vascular/metabolism , Epoprostenol/metabolism , Uridine Triphosphate/pharmacology , Animals , Calcium/physiology , Cattle , In Vitro Techniques , Inositol 1,4,5-Trisphosphate/metabolism , Ionomycin/pharmacology , Lipid Metabolism , Phospholipases A/metabolism , Phospholipases A2 , Pulmonary Artery/cytology , Quinacrine/pharmacology , Receptors, Cell Surface/metabolism , Trifluoperazine/pharmacology
10.
J Biol Chem ; 264(26): 15242-6, 1989 Sep 15.
Article in English | MEDLINE | ID: mdl-2768260

ABSTRACT

We have shown that purified bovine soluble dopamine beta-hydroxylase can reconstitute onto preformed phosphatidylserine containing vesicles. The binding is dependent on pH and vesicle phosphatidylserine composition but does not require calcium. Reconstitution appears to be irreversible, with the lipid-bound enzyme possessing hydroxylase activity. Additionally, [14C] phosphatidylserine binds to soluble dopamine beta-hydroxylase and remains bound after several detergent washes. Thus the reconstituted soluble form of the enzyme appears to be functionally analogous to the membranous form. Both the reconstitution data and the lipid binding data suggest that multiple phosphatidylserine molecules bind to the soluble hydroxylase. We propose that noncovalently bound phosphatidylserine moieties, which copurify with the membrane bound form of the enzyme, alone are responsible for anchoring membranous dopamine beta-hydroxylase to chromaffin granule and model membranes.


Subject(s)
Dopamine beta-Hydroxylase/metabolism , Liposomes , Phospholipids/metabolism , Adrenal Medulla/enzymology , Animals , Cattle , Hydrogen-Ion Concentration , Kinetics , Models, Biological , Phosphatidylserines/metabolism , Protein Binding
11.
J Biol Chem ; 264(1): 14-6, 1989 Jan 05.
Article in English | MEDLINE | ID: mdl-2909511

ABSTRACT

Dopamine beta-hydroxylase exists in bovine adrenal medulla chromaffin granules in both soluble and membrane-bound forms. The mechanism by which membranous dopamine beta-hydroxylase is bound to granule membranes has been elusive. Recently, evidence that covalently attached phosphatidylinositol does not serve as an anchor for membranous dopamine beta-hydroxylase was reported (Stewart, L. C., and Klinman, J. P. (1988) J. Biol. Chem. 263, 12183-12186). It was suggested that an uncleaved signal sequence could serve as a mode of attachment for the membrane-bound hydroxylase. Amino-terminal sequence analysis of purified bovine membranous dopamine beta-hydroxylase demonstrates that this form of the enzyme possesses an amino-terminal sequence similar to the soluble enzyme. Additionally, the 75- and 72-kDa bands of membranous dopamine beta-hydroxylase were electrophoretically eluted from a preparative sodium dodecyl sulfate-polyacrylamide gel and sequenced. Both bands had the amino-terminal sequence characteristic of the soluble bovine enzyme. These sequence results eliminate the possibility that an uncleaved signal sequence serves as the membrane anchor.


Subject(s)
Chromaffin Granules/enzymology , Chromaffin System/enzymology , Dopamine beta-Hydroxylase/metabolism , Intracellular Membranes/enzymology , Protein Sorting Signals/metabolism , Adrenal Medulla/enzymology , Amino Acid Sequence , Animals , Binding Sites , Cattle , Molecular Sequence Data , Protein Binding
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