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At least 307 records · Page 17Linked to original sources

Disseminated skeletal lesions associated with pathogenic actinomycetes in a Pygmy hog (Sus salvanius).

The clinical and pathological features of an unusual crippling bone disease in an adult male Pygmy Hog, Sus salvanius, born the smallest in a litter of five and representing the rarest of the known living Suidae, are described. Radiological studies revealed severe spondylosis deformans and focal sharply demarcated radiolucencies in virtually the whole skeleton, but particularly in the bones of the skull, the processes of multiple vertebrae, the ribs, scapulae and parts of the humeri and femora. The clinical chemistry measurements were indicative of pathological lytic processes in the skeleton. The focal bone lesions consisted of caseous necrosis, dystrophic calcification and peripheral fibroblastic demarcation. They contained colonies of filamentous bacteria identified as members of the Order Actinomycetales. Case history evidence suggests that the infection may have resulted from repeated skin trauma inflicted by litter-mates.

Actinomycetales Infections↗

Viral antigen and B and T lymphocytes in lymphoid tissues of gnotobiotic piglets infected with hog cholera virus.

Four 4-day-old gnotobiotic piglets infected intranasally with the Kanagawa/74 strain of hog cholera virus (HCV) did not develop severe illness over a period of 3 weeks. Large amounts of HCV were isolated from the lymphoid tissues and serum at necropsy. After the acute phase, hyperplasia of histiocytes and plasmacytopoiesis were observed in two pigs (killed 14 and 21 days after inoculation). The number of CD4+ and CD8+ T lymphocytes increased significantly and their location was consistent with the site of HCV replication. The results suggest that a CD8+ T-lymphocyte reaction is associated with persistent HCV infection.

Acute Disease↗

Immunohistochemical and ultrastructural evidence of hog cholera virus infection of megakaryocytes in bone marrow and spleen.

Twelve pigs were inoculated with a highly virulent strain of hog cholera virus (HCV) to study viral infection of megakaryocytes in the bone marrow and spleen. Immunohistochemical and ultrastructural examination revealed HCV infection in a small proportion (2.5-9.0%) of these cells from the 2nd to the 9th day after inoculation, at which time the experiment was terminated. Megakaryocyte infection accounts for the presence of viral antigens in platelets. The latter may represent a passive vehicle for spreading the virus in the animal.

Animals↗

Apoptosis is associated with an inhibition of aminophospholipid translocase (APTL) in CNS-derived HN2-5 and HOG cells and phosphatidylserine is a recognition molecule in microglial uptake of the apoptotic HN2-5 cells.

A balance of the activities of multiple enzymes maintains the typical asymmetry of plasma membrane lipids in healthy cells. Such enzyme activities are (a) the aminophopholipid translocase (APTL) (a lipid-selective P-type ATPase that catalyzes inward movement of aminophospholipids), (b) the scramblase (a calcium-dependent and ATP-independent enzyme that catalyzes both inward and outward movement of lipids), (c) the floppase (an ATP-dependent enzyme that catalyzes only outward movement of lipids). Activation or inhibition of any one of these enzymes would lead to a loss in this asymmetry. Apoptosis-associated externalization of phophatidylserine has been reported for many different cell-types, but the exact mechanism involved in this loss of membrane asymmetry has not been identified yet. In this report we demonstrate concurrence of APTL inhibition, caspase-3 activation and apoptosis in CNS-derived HN2-5 and HOG cells. Additionally, we provide data to demonstrate that the phagocytosis of apoptotic, CNS-derived HN2-5 cells by the microglial cells requires recognition through phosphatidylserine (PS). Thus the enzyme aminopholipid translocase is inhibited during apoptosis of CNS-derived cells and this alone could account for the loss of plasma membrane lipid-asymmetry observed in these cells.

Animals↗

Yeast go the whole HOG for the hyperosmotic response.

An evolutionarily conserved mitogen-activated protein kinase pathway--the high osmolarity glycerol (HOG) pathway--mediates the hyperosmotic response in Saccharomyces cerevisiae. A variety of powerful approaches has generated a comprehensive picture of how cells respond to this stress condition. Several presumptive osmosensors on the cell surface recruit and activate downstream signaling components, which regulate the activity of transcription factors to control gene expression.

Cell Compartmentation↗

Etoposide, ifosfamide and cisplatin (VIP) plus concurrent radiation therapy for previously untreated limited small cell lung cancer (SCLC): a Hoosier Oncology Group (HOG) phase II study.

Results of a previous Hoosier Oncology Group (HOG) study revealed a small survival advantage for VIP versus etoposide and cisplatin (EP) for patients with extensive stage small cell lung cancer (SCLC). This phase II study evaluated VIP with concurrent thoracic radiotherapy in patients with limited stage SCLC. Eligible patients had a Karnofsky Performance Score > or = 50, no prior chemotherapy or radiotherapy, and adequate end organ function. Fifty-three patients were entered. Radiotherapy was given as a daily fraction of 1.8 Gy, five fractions per week for 5 weeks for a total dose of 45 Gy, beginning on day 1 of VIP. The first 13 patients received etoposide 75 mg/m(2), cisplatin 20 mg/m(2), and ifosfamide 1.2 g/m(2) on days 1-4 with Mesna every 3 weeks for four cycles unless the patient demonstrated disease progression or undue toxicity. Excessive toxicity was seen in the first 13 patients; therefore, VIP was modified by deleting the 4th day for all subsequent patients. The major toxicity in this trial was myelosuppression. Grade 3/4 anemia, granulocytopenia, and thrombocytopenia occurred in 38, 75, and 34% of patients, respectively. There were four treatment-related deaths [three patients (23%) on the 4-day regimen and one patient (2.5%) on the 3-day regimen]. Twenty-five patients (47.2%) achieved a CR and 11 patients (20.8%) had a PR for an overall response rate of 68%. Minimum follow up for all patients is 5 years. Overall, 46 of 53 patients have died. Median, 1, 2 and 5 year overall survival for the entire group is 15.1 months, 69.8, 35.9, and 13.2, respectively. The results of this phase II trial of VIP with concurrent early thoracic radiotherapy failed to demonstrate a superior response rate over other series utilizing EP. In addition, treatment-related morbidity and mortality appears to be unacceptably high with the VIP regimen.

Adult↗

Microsporum nanum infection in hog farmers.

Microsporum nanum is a dermatophyte that can cause disease in both man and animals and is most frequently associated with ringworm infection in pigs. Human infections are rare in the literature. Three new cases of human M. nanum infection are reported here. Two patients had inflammatory tinea faciei and one had tinea cruris. The patients were successfully treated with clotrimazole or miconazole cream, sometimes combined with griseofulvin. All three patients were hog farmers and lived in the same small rural area. Occupational exposure is suggested as the cause of infection.

Adult↗

The vasopressin gene non-canonical Hogness box: effect on protein binding and promoter function.

Comparison of the promoter sequences of the genes encoding the neuropeptide hormone vasopressin from a number of organisms has revealed that they do not contain a classical Hogness box. In all vertebrate species examined, the canonical TATA box is replaced with a CATA sequence. We hypothesised that this conserved modified sequence may play a role in the regulation of vasopressin promoter activity. We used electrophoretic mobility shift assays to show that TATA and CATA sequences generate different complexes with SON nuclear proteins. Further, the transfection of wild-type (CATA) and mutated (TATA) VP promoter-reporter constructs into a heterologous cell line demonstrated a sequence-specific effect on transcriptional activity. The CATA sequence contributes to weaker promoter activity than a TATA box, but is able to interact with the upstream elements to increase the efficacy of an enhancer. The CATA box may thus be involved in the cell-specific and physiological regulation of the VP gene.

Animals↗

Affinity purification of kallikrein and elastase from hog pancrease powder.

The present report describes a method that is efficient for simultaneous isolation of kallikrein and elastase from hog pancrease powder. Both enzymes were separated by successive column chromatography on CM-cellulofine and p-aminobenzamidine-Sepharose 4B. Kallikrein was further purified by column chromatography on DEAE-Sephadex and elastase was purified by repeated gel chromatography on Sephadex G-75. The kallikrein obtained was composed of two components, which were separable by sodium dodecyl sulphate polyacrylamide gel electrophoresis, and the elastase had one component. The activity yields of kallikrein and elastase were 49 and 38%, respectively.

Amino Acids↗

Anaerobic codigestion of hog and poultry waste.

Anaerobic batch tests were performed using hog and poultry wastes in various proportions. Treatments that received both wastes produced higher yields of biogas, up to 200 +/- 30 mL/g volatile solids (VS) destroyed, and methane, up to 130 +/- 20 mL/g VS destroyed, compared to either waste alone.

Anaerobiosis↗

Estimation of the dynamics and rate of transmission of classical swine fever (hog cholera) in wild pigs.

Infectious diseases establish in a population of wildlife hosts when the number of secondary infections is greater than or equal to one. To estimate whether establishment will occur requires extensive experience or a mathematical model of disease dynamics and estimates of the parameters of the disease model. The latter approach is explored here. Methods for estimating key model parameters, the transmission coefficient (beta) and the basic reproductive rate (RDRS), are described using classical swine fever (hog cholera) in wild pigs as an example. The tentative results indicate that an acute infection of classical swine fever will establish in a small population of wild pigs. Data required for estimation of disease transmission rates are reviewed and sources of bias and alternative methods discussed. A comprehensive evaluation of the biases and efficiencies of the methods is needed.

Animals↗

Location of the carbohydrates present in the HK-ATPase vesicles isolated from hog gastric mucosa.

The glycosylation of H+K(+)-ATPase vesicles isolated from hog gastric mucosa was investigated by various methods. Following protein separation on sodium dodecyl sulfate reducing gels and transfer to poly(vinyl difluoride) membranes, binding of concanavalin A was confined to the 94-kDa band which corresponds to the catalytic subunit. In contrast, wheat germ agglutinin binding occurred in a region below the 94-kDa subunit, corresponding to the 60-85-kDa region, and also to protein just above the catalytic subunit. Treatment with glycopeptidase F removed most of the concanavalin A staining and also the wheat germ agglutinin staining found below the 94-kDa region, but spared the higher molecular weight wheat germ agglutinin reactive material. During the deglycosylation experiments a protein of 35-kDa was produced. Sequencing analysis of V8 protease generated peptide fragments of the 35-kDa protein show at least 30% homology with the Na+K(+)-ATPase beta-subunits. Labeling of the carbohydrates by galactosyltransferase and [3H]uridine diphosphate-galactose showed that the sites of labeling were extracellular and were confined to the wheat germ agglutinin staining regions. Two molecular weight regions, below the 94-kDa region, of 60 and 85 kDa were identified. Electron microscopy using postembedding staining techniques showed that both concanavalin A and wheat germ agglutinin staining occurred on the extracellular face of the gastric vesicles.(ABSTRACT TRUNCATED AT 250 WORDS)

Adenosine Triphosphatases↗

Studies on the chirality of sulfoxidation catalyzed by bacterial flavoenzyme cyclohexanone monooxygenase and hog liver flavin adenine dinucleotide containing monooxygenase.

The stereochemical outcome of oxygen transfer to the sulfur moiety of aryl alkyl sulfides catalyzed by two flavoenzyme monooxygenases has been determined by resolution of sulfoxide product enantionmers on a high-pressure liquid chromatography column [Pirkle, W. H., Finn, J. M. Schreiner, J. L., & Hamper, B. C. (1981) J. Am. Chem. Soc. 103, 3964-3966] containing a 3,5-dinitrobenzoyl-D-phenylglycine chiral stationary phase. With 4-tolyl ethyl sulfide as substrate, cyclohexanone monooxygenase from Acinetobacter produces predominantly the (S)-(-)-sulfoxide (82% S, 18% R), a modest enantioselectivity. In contrast, the flavin adenine dinucleotide (FAD) containing a monooxygenase purified from hog liver microsomes carries out sulfoxidation to yield the (R)-(+)-sulfoxide enantiomer as major product (95% R, 5% S). The presence of the minor sulfoxide enantiomer in each case appears to be due to incomplete chiral processing by each enzyme and not to a competing, achiral, nonenzymic sulfoxidation process. The mammalian FAD-containing monooxygenase also oxygenates the divalent sulfur of the antiarthritic drug sulindac sulfide to yield a single dextrorotatory isomer of the sulfoxide prodrug. Analysis of the chiral outcome of sulfoxidation catalyzed by rat liver microsomes indicated that phenobarbital treatment increases the capacity for S-(-)-oxygenation of 4-tolyl ethyl sulfide, suggesting that the phenobarbital-induced cytochrome P-450 isoenzymes catalyze formation of the (S)-(-)-sulfoxide preferentially, a surmise validated in the following paper [Waxman, D. J., Light, D. R., & Walsh, C. (1982) Biochemistry (following paper in this issue)]. With sulindac sulfide as substrate, though, both control and phenobarbital-induced microsomes catalyze sulfoxidation to yield the same (+)-sulfoxide enantiomer generated by the purified FAD-containing monoxygenase, suggesting a low degree of participation by the cytochrome P-450 isozymes in sulfoxidation of this compound.

Acinetobacter↗

Proton relaxation study of the hog kidney diamine oxidase active center.

Proton relaxation studies of the interactions with hog kidney diamine oxidase of water, substrate-analogue inhibitors, and product analogues indicate that the active site Cu(II) is not located near the oxidizing site of the enzyme, rather near the nonoxidized end of the binding substrate. The studies with histamine derivatives provide evidence for a concentration-dependent occupation of two sites. The site which is populated at high concentrations provides proximity of the imadazole ring nitrogen N1 to the Cu(II). Water binds at the Cu(II) of the native enzyme. However, this water is probably not involved in the hydrolysis of the enzyme-substrate imine bond to eliminate the first reaction product. O2 does not compete with H2O for a site on the Cu(II) ion. In the case of one of the probes, namely the ammonia (product) analogue dimethylamine, the validity of the protein relaxation results was verified by also observing the nitrogen (15N) relaxation rates of ammonia itself. The conclusion that the ammonium ions is not directly bonded to the active site Cu(II) is reached from both the proton and nitrogen relaxation experiments.

Amine Oxidase (Copper-Containing)↗

Inhibition of hog liver folylpolyglutamate synthetase by 5-substituted 5,8-dideaza analogues of folic acid bearing a terminal L-ornithine residue.

Five new N alpha-(5,8-dideazapteroyl)-L-ornithines have been prepared using multistep synthetic sequences. These include N alpha-[5-(trifluoromethyl)-5,8-dideazapteroyl]-L-ornithine, 3, as well as N alpha-[5-(trifluoromethyl)-5,8-dideazaisopteroyl]-L-ornithine, 4, and its 5-fluoro and 5-chloro analogues. Both of the compounds containing a 5-(trifluoromethyl) group (3 and 4) were found to be excellent inhibitors of homogeneous hog liver folylpolyglutamate synthetase, having Ki values in the same range as N alpha-(5-chloro-5,8-dideazapteroyl)-L-ornithine, 2, (approximately 10 nM). However, the bridge-reversed isomer of 2 was 60-fold less inhibitory than 2.

Animals↗

Formation of glutathionyl-spironolactone disulfide by rat liver cytochromes P450 or hog liver flavin-containing monooxygenases: a functional probe of two-electron oxidations of the thiosteroid?

We have previously reported that the diuretic thiosteroid spironolactone (SPL) inactivates rat liver microsomal cytochromes P450 [P450 (P450 3A and P450 2C11)] in a in a mechanism-based fashion, and we have identified two polar SPL metabolites (SPL-sulfinic acid and -sulfonic acid), formed in a partition ratio of approximately 20:1 in such rat liver microsomal incubations [Decker et al. (1989) Biochemistry 28, 5128-5136]. We proposed at the time that these metabolites were most likely derived from further enzymatic (or nonenzymatic) oxidations of the one-electron oxidation product [SPL-thiyl radical (SPL-S.)] and/or the two-electron-oxidized species [SPL-sulfenic acid (SPL-SOH)]. In those studies, glutathione (GSH) was found to attenuate both SPL-mediated P450 loss as well as polar metabolite formation by approximately 40%. We have now reexamined this in greater detail and report that it is due to GSH trapping of an electrophilic oxidized SPL species to form an adduct that we have isolated and unambiguously characterized by mass spectral analyses as the glutathionyl-SPL adduct (SPL-SSG). Moreover, we have found not only that rat liver microsomal formation of this adduct is enhanced at pH 9.0, the pH optimum for flavin-containing monooxygenase (FMO), but also that such adduct formation was indeed efficiently catalyzed by purified hog liver FMO. Because FMO oxidations of thiols are thought to entail a two-electron process to form the corresponding sulfenic acids, we infer that such a SPL-SSG adduct most likely reflects FMO-catalyzed oxidation of SPL to SPL-SOH, which on leaving the FMO active site is then trapped by GSH.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗

Studies on the transcobalamin receptor in hog kidney.

The binding of the cobalamin-transcobalamin complex by its solubilized receptor from hog kidney membrane was studied. The receptor bound the complex in a system containing bivalent cations, and the affinity was dependent on the NaCl concentration but not on temperature. The binding of cobalamin-transcobalamin to the receptor had an association constant of approximately 4.6 x 10(9) liter/mol and it was saturable and highly specific as competition by other proteins was not observed. The receptor had higher affinity for the cobalamin-transcobalamin complex (holo-TC) than for transcobalamin (apo-TC). Basic amino compounds known to interfere with tubular reabsorption of proteins did not inhibit the binding. Studies on subcellular fractions supported the view that the receptor was located on the brush border membrane of the kidney.

Animals↗

Nbp2 targets the Ptc1-type 2C Ser/Thr phosphatase to the HOG MAPK pathway.

The yeast high osmolarity glycerol (HOG) pathway signals via the Pbs2 MEK and the Hog1 MAPK, whose activity requires phosphorylation of Thr and Tyr in the activation loop. The Ptc1-type 2C Ser/Thr phosphatase (PP2C) inactivates Hog1 by dephosphorylating phospho-Thr, while the Ptp2 and Ptp3 protein tyrosine phosphatases dephosphorylate phospho-Tyr. In this work, we show that the SH3 domain-containing protein Nbp2 negatively regulates Hog1 by recruiting Ptc1 to the Pbs2-Hog1 complex. Consistent with this role, NBP2 acted as a negative regulator similar to PTC1 in phenotypic assays. Biochemical analysis showed that Nbp2, like Ptc1, was required to inactivate Hog1 during adaptation. As predicted for an adapter, deletion of NBP2 disrupted Ptc1-Pbs2 complex formation. Furthermore, Nbp2 contained separate binding sites for Ptc1 and Pbs2: the novel N-terminal domain bound Ptc1, while the SH3 domain bound Pbs2. In addition, the Pbs2 scaffold bound the Nbp2 SH3 via a Pro-rich motif distinct from that which binds the SH3 domain of the positive regulator Sho1. Thus, Nbp2 recruits Ptc1 to Pbs2, a scaffold for both negative and positive regulators.

Adaptor Proteins, Signal Transducing↗