Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “HOGS”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 145 records · Page 8Linked to original sources

The effects of in utero viral infection on embryonic, fetal, and neonatal survival: a comparison of SMEDI (porcine picorna) viruses with hog cholera vaccinal virus.

SMEDI and hog cholera viruses were shown to have marked effects upon the survival of the embryo (from conception to 30 days of gestation), the fetus (from 30 days of gestation until birth), and the neonatal pig (from birth until five days after birth). Embryonic infection was characterized by death and absorption of the embryo and in some instances the return to estrus after an irregular estrous cycle. Embryonic infection also may have been responsible for the development of some abnormal pigs. Fetal infection caused death with mummification of one or more fetuses and occasionally all fetuses in the uterus. Infection established in early gestation produced effects on the fetus which apparently persisted until after birth and varied from a persistent viremia (as in hog cholera infection) to an undefined lack of resistance in the newborn (as in SMEDI virus infection). Hog cholera vaccinal virus was the more virulent of the two virus types and reacted somewhat like rubella virus, in that infection apparently could be established in the fetus even in middle trimester of pregnancy, and possibly later. SMEDI viruses, in contrast, were less virulent and were most pathogenic when the dam was infected during the first 30 days of pregnancy. Immunity against either virus could be established in the nonpregnant gilt and was most effective in preventing intrauterine infections with that virus. However, with as many as 10 enteroviruses (five are known to cause intrauterine infection) it was believed that maintaining a closed breeding herd and introducing new stock into contact with the breeding herd at least 30 days before breeding time might be a safer means of control.

Abortion, Missed↗

[Hog cholera virus: influence of colostral passive antibody on immune response of pig following vaccination with the rabbit adapted Chinese strain (author's transl)].

Using the rabbit adapted chinese strain of Hog cholera, active immunization of piglets having passive colostral antibodies was studied. 65 piglets born from 11 sows were used. Concerning sows, vaccination was performed 5-6 months and 1 month before service (3 sows), 30 days (2 sows) and 60 days (3 sows) after service. Divided in 5 lots, piglets were vaccinated at 4 different periods after birth (15, 30, 60 and 90 days). Hog cholera immunity was determined for each animal by means of kinetic of serum neutralizing antibodies and resistance to virulent challenge performed 5 months after birth. High levels of neutralizing antibodies were observed in serum of each vaccinated sow at the time of farrowing. In piglets having ingested low quantities of colostrum, vaccination induces a good antigenic stimulation characterized by a normal humoral immune response and challenge resistance. But in piglets having ingested a normal quantities of colostrum, colostral passive antibodies have a partial or complete suppressive effect on primary immune response which is characterized by a delay in serum antibodies formation and by a low level at the time of challenge. According the conditions of sows vaccination, differences were observed in the properties of colostral passive antibodies (intensity of suppressive effect on active immune response, in vitro "avidity" for Hog cholera virus, mean value of half-life) present in piglets serum. On practical aspect, vaccination with the chinese strain becomes fully effective in piglets having passive immunity when they are 30-60 days old.

Animals↗

Serologic survey of California wild hogs for antibodies against selected zoonotic disease agents.

Blood samples were collected from trapped or hunter-killed wild hogs (Sus scrofa) in 4 areas of California. Sera were tested for antibodies against 7 zoonotic disease agents. Antibodies against Brucella sp were detected in 21 (15%) of 136 samples. Antibodies against Coxiella burnetii were found in 50% of the collected samples (67 of 135 tested). Of the 135 wild hogs screened for pseudorabies virus, 4 (3%) were seropositive. Leptospira interrogans antibodies were discovered in 118 (87%) of the 136 samples tested. Of the 130 samples screened for antibodies against Mycobacterium avium complex, 111 (85%) were seropositive. Antibodies against Toxoplasma gondii were detected in 17 (13%) of 135 wild hogs. Antibodies against Yersinia pestis were found in 9 (15%) of 59 sera tested.

Animal Population Groups↗

End-point dilution-fluorescent antibody technique for cloning hog cholera virus.

Hog cholera virus was cloned by incubating selected pretitrated dilutions of the virus on PK-15 cell cultures for 2 hours. After a thorough washing, the coverslip cell cultures were overlaid with medium containing 0.1% hog cholera immune serum to prevent secondary foci. Forty-eight hours later, the cultures were vigorously washed and maintenance medium containing 5% bovine fetal serum was added. When examined by the fluorescent antibody technique 18 hours later, single plaques were observed in some cultures with no evidence of secondary foci. The virus clone subsequently yielded a homogeneous population of hog cholera virus that retained the characteristics of the parent strain; pathogenicity of the virus clone in pigs was demonstrated, and specific immunofluorescence occurred in infected cell cultures stained with fluorescein isothiocyanate-labeled antibody. The method used gave reasonable assurance of the cloned virus' freedom from extraneous agents.

Classical Swine Fever Virus↗

Salmonella in the mesenteric lymph nodes of healthy sows and hogs.

Mesenteric lymph nodes were collected from healthy sow and slaughter hogs that had been kept in holding pens for an average of 10 and 2 days, respectively, before slaughter at an abattoir. Salmonella was isolated from 58.2% (67/115) of the sows and 31.3% (16/51) of the slaughter hogs. This difference in Salmonella prevalence was significant (chi 2 = 10.22, P less than 0.005); therefore, the hypothesis that there would be no significant difference in the infection rates of sows and slaughter hogs was rejected.

Abattoirs↗

Respiratory effects and dust exposures in hog confinement farming.

Fifty-three hog confinement farmers and 43 control farmers were studied. Pulmonary function, total and respirable personal dust levels, and responses to a health status questionnaire were obtained for all farmers. The hog farmers' total and respirable personal dust exposures were significantly higher than the respective levels of the control farmers. Higher dust levels were associated with the use of floor (scatter) feeding, indoor feed grinding, and the use of high moisture corn feed. Pork producers reported respiratory symptoms significantly more often than controls. Lung function did not differ between the two groups of farmers, nor could dust exposure levels be related to lung function.

Adult↗

The HOG pathway controls osmotic regulation of transcription via the stress response element (STRE) of the Saccharomyces cerevisiae CTT1 gene.

The HOG signal pathway of the yeast Saccharomyces cerevisiae is defined by the PBS2 and HOG1 genes encoding members of the MAP kinase kinase and of the MAP kinase family, respectively. Mutations in this pathway (deletions of PBS2 or HOG1, or point mutations in HOG1) almost completely abolish the induction of transcription by osmotic stress that is mediated by stress response elements (STREs). We have demonstrated previously that STREs also mediate induction of transcription by heat shock, nitrogen starvation and oxidative stress. This study shows that they are also activated by low external pH, sorbate, benzoate or ethanol stress. Induction by these other stress signals appears to be HOG pathway independent. HOG1-dependent osmotic induction of transcription of the CTT1 gene encoding the cytosolic catalase T occurs in the presence of a protein synthesis inhibitor and can be detected rapidly after an increase of tyrosine phosphorylation of Hog1p triggered by high osmolarity. Consistent with a role of STREs in the induction of stress resistance, a number of other stress protein genes (e.g. HSP104) are regulated like CTT1. Furthermore, catalase T was shown to be important for viability under severe osmotic stress, and heat shock was demonstrated to provide cross-protection against osmotic stress.

Adaptation, Physiological↗

Glycerol formation during wine fermentation is mainly linked to Gpd1p and is only partially controlled by the HOG pathway.

Glycerol 3-phosphate dehydrogenase, a key enzyme in the production of glycerol, is encoded by GPD1 and GPD2. The isoforms encoded by these genes have different functions, in osmoregulation and redox balance, respectively. We investigated the roles of GPD1, GPD2 and HOG1-the kinase involved in the response to osmotic stress-in glycerol production during wine fermentation. We found that the deletion of GPD2 in a wine yeast-derived strain did not affect growth or fermentation performance and reduced glycerol production by only 20%. In contrast, a gpd1delta mutant displayed a prolonged lag phase, and produced 40% less glycerol than the wild-type strain. The deletion of HOG1 resulted in a slight decrease in growth rate and a 20% decrease in glycerol production, indicating that the HOG pathway operates under wine fermentation conditions. However, the hog1delta mutant was not as severely affected as the gpd1delta mutant during the first few hours of fermentation, and continued to express GPD1 strongly. The hog1delta mutant was able to increase glycerol production in response to high sugar concentration (15-28% glucose), to almost the same extent as the wild-type, whereas this response was totally abolished in the gpd1delta mutant. These data show that Gpd1p plays a major role in glycerol formation, particularly during the first few hours of exposure to high sugar concentration, and that GPD2 is only of little significance in anaerobic fermentation by wine yeast. The results also demonstrate that the HOG pathway exerts only limited control over GPD1 expression and glycerol production during wine fermentation.

Blotting, Northern↗

Inhibition of (H+ + K+)-ATPase and H+ accumulation in hog gastric membranes by trifluoperazine, verapamil and 8-(N,N-diethylamino)octyl-3,4,5-trimethoxybenzoate.

The mechanism of gastric antisecretory action for trifluoperazine, verapamil and 8-(N,N-diethylamino)octyl-3,4,5-trimethoxybenzoate (TMB-8) has been studied utilizing isolated hog gastric membranes enriched with (H+ + K+)-ATPase. The drugs inhibited the gastric ATPase due to their apparent competition with K+ for the luminal high-affinity K+-site of the ATPase. The dose to inhibit 50% (ID50) of the ATPase in the membranes rendered freely permeable to K+ (20 mM) was 50 microM for trifluoperazine and 1.5 mM for verapamil and TMB-8. In intact hog gastric membranes which develop a pH gradient in the presence of valinomycin, ATP and KCl, however, trifluoperazine at 4 microM, verapamil and TMB-8 at 15 microM inhibited 40 and 30% of the valinomycin-stimulated ATPase activity, respectively, and also blocked the ionophore-dependent intravesicular acidification as measured by aminopyrine accumulation. The enhanced potency of the drugs to inhibit the ATPase in the intact membrane vesicles may be attributed to the accumulation of the drugs as a weak base within the vesicles, where the luminal K+-site of the ATPase is accessible. Calmodulin and Ca2+ had no effect on the extent of H+-accumulation as measured by aminopyrine accumulation in the membrane vesicles which were prepared in the presence of 1 mM EGTA. Since the drugs showed similar potency in interfering with H+ movements either in the membrane vesicles or isolated rabbit gastric glands stimulated by dibutyryl cAMP, it is reasonable to suggest the inhibitory effect of the drugs on (H+ + K+)-ATPase as a primary cause for such interferences in both cases. A trifluoperazine analog and other lipophilic amine drugs similarly inhibited (H+ + K+)-ATPase and H+ accumulation in the membrane vesicles or in the glands. We have concluded that a tertiary amine, the only common functional group among these drugs, is primarily responsible for their ability to interact with the high-affinity K+ site of the gastric ATPase.

Adenosine Triphosphatases↗

H+/K(+)-ATPase contents of human, rabbit, hog and rat gastric mucosa.

A monoclonal antibody (mAb 95-111) was used to titrate the amounts of H+/K(+)-ATPase in subcellular fractions of the fundus of rats, pigs, rabbits and humans. All four had similar amounts of H+/K(+)-ATPase: 2.1 +/- 0.5 (human), 1.9 +/- 0.4 (rabbit), 4.4 +/- 0.5 (rat) and 4.2 +/- 0.8 (hog) mg ATPase/g wet tissue. The antigen concentrations and H+/K(+)-ATPase enzymatic activities of subcellular fractions were linearly correlated in all species but rat suggesting that human, rabbit and hog H+/K(+)-ATPases have similar rates of catalysis (223 mumol Pi/h per mg ATPase). The non-correlation of rat data probably reflects the known lability of the rat enzyme. Hence, immuno-titration promises to be a more reliable method of estimating rat ATPase than the currently used enzymatic assay. The H+/K(+)-ATPase content of human biopsies was 20-fold higher than previously-published (Smolka, A. and Weinstein, W.M. (1986) Gastroenterology 90, 532-539) suggesting that the previous immuno-titration underestimated the H+/K(+)-ATPase content of the human fundus.

Adenosine Triphosphatases↗

Isolation and properties of crystalline quinolinate phosphoribosyltransferase from hog kidney.

Crystalline quinolinate phosphoribosyltransferase (nicotinatenucleotide: pyrophosphate phosphoribosyltransferase (carboxylating), EC 2.4.2.19) was isolated from hog kidney and compared with the same enzyme prepared from hog liver. The enzyme preparation was homogeneous as shown by polyacrylamide gel electrophoresis and ultracentrifugation analysis. The enzyme had a molecular weight of 220 000 and the subunit 35 000. The physicochemical properties of the enzyme were: sedimentation coefficient (S200,W), 7.75 . 10(-13) s; difussion coefficient (D200,W), 5.04 . 10(-7) cm2/s; Stokes radius, 62.05 A, frictional ratio (f/f0), 1.62 and isoelectric point (pI), 4.5. The enzyme was stable at 37 degrees C for 30 min between pH 4.5 and 9.5. Enzyme activity was inhibited by various carboxylic acids; however, this inhibition was reversed by raising the Mg2+ concentration. Optimum pH was 5.5, and no detectable amounts of Mg2+, Mn2+, Fe2+, Cu2+, Zn2+ and Ca2+ were found by atomic absorption spectrophotometry. The enzyme was found to contain sugar. Mg2+ was completely replaceable by Mn2+. The reaction mechanism of this enzyme was suggested to be of the 'ping-pong' type. Km values of quinolinic acid and 5-phosphoribosyl 1-pyrophosphate were 4 . 10(-5) and 1.4 . 10(-4) M, respectively.

Amino Acids↗

Terminal residues of hog pancreatic amylase.

Studies on the identification of the terminal residues in protease-free hog pancreatic alpha-amylase, prepared by glycogen precipitation, demonstrated the absence of free amino terminals when four different chemical procedures were used. These methods were based on reaction with fluorodinitrobenzene, trinitrobenzenesulfonic acid, dansyl chloride, and cyanate. In the search for the presence of a possible alpha-N-blocking group, an acetyl group was detected as acetic acid dinitrophenyl hydrazide after hydrazinolysis and dinitrophenylation. Quantitation of acetyl groups by a gas chromatographic or a specific enzymatic method yielded 0.7 mol of acetyl group per 51,000 g of protein. Other acyl groups, such as formyl or propionyl, were not found. Leucine was shown to be the carboxyl terminal residue by hydrazinolysis or by carboxypeptidase A digestion of acid denatured amylase. With either procedure, 0.8 mol of carboxyl terminal leucine was found per 51,000 g of protein. These findings are consistent with the proposal that hog pancreatic alpha-amylase is composed of a single, alpha-N-acetylated chain of molecular weight 50,000. Claims of other investigators for subunit and multichain structures for this enzyme are discussed in view of these end group data.

Amino Acid Sequence↗

Findings of trigonelline demethylating enzyme activity in various organisms and some properties of the enzyme from hog liver.

Trigonelline demethylating enzyme activity was found widely in animals, plants and microorganisms. Very high enzyme activity of this enzyme was detected in hog liver. Properties of the hog liver enzyme were investigated. Optimum pH for the enzymic reaction was observed at 8.5. The Km value for trigonelline was calculated at 2.77 mM. Addition of any cofactor is not required for the reaction The enzyme activity was inhibited by heavy metal ions. The reaction product was identified as nicotinic acid. Proposed enzyme reaction mechanism and the role of this enzyme in biosynthesis and metabolism of NAD are discussed.

Alkaloids↗

Binding site of omeprazole in hog gastric H+,K(+)-ATPase.

Omeprazole transforms into an active compound in an acidic environment, which is able to modify a sulfhydryl group of gastric H+,K(+)-ATPase. Omeprazole was transformed into a strongly fluorescent molecule by UV-light irradiation (excitation wavelength = 290 nm, emission wavelength = 335 nm). The omeprazole-modified residue of hog H+,K(+)-ATPase was estimated by the fluorescence of the omeprazole moiety and limited tryptic digestion of the enzyme. Among the four main tryptic digested subfragments, omeprazole was bound to the 67, 42 and 32-kDa subfragments, but not to the 52-kDa subfragment. Taking the amino acid sequence of this ATPase into consideration, we propose that omeprazole specifically binds with Cys322 in hog H+,K(+)-ATPase (Cys321 in rat).

Adenosine Triphosphatases↗

Effects of papaverine on the relative distribution of 45Ca ions in subcellular fractions of hog biliary muscles.

The mechanisms by which papaverine (Pap) relaxes smooth muscles of hog bile ducts were investigated with respect to the effects of Pap on the distribution of Ca ions in intracellular organelles. Muscles loaded with 45Ca ions in 139 mM KCl-Tyrode's solution were incubated with Pap, [3H]Pap or theophylline (ThP) in Tyrode's solution. The Pap and Ca contents of various subcellular fractions were measured. Pap (40 microM) had no effect on Ca influx into the muscle in normal and 139 mM KCl-Tyrode's solutions. Pap was distributed to a greater extent in the cytosol fraction (F4) than in microsome and mitochondria-enriched fractions (F3) and in the nuclei-enriched fraction (F2). Pap selectively accumulated in the plasma membrane-enriched fraction (PM-F) and was negligible in the sarcoplasmic reticulum-enriched fraction (SR-F) and the mitochondria-enriched fraction (Mit-F). The Ca release of PM-F was greater and more rapid than the release from SR-F or Mit-F. The increase in the content of Ca in PM-F induced by Pap was enhanced by oxalate, suggesting that the increase is based on the increase in Ca uptake, not on the reduced efflux. Pap increased dose-dependently the Ca content of PM-F and appeared to decrease the Ca contents of SR-F and Mit-F. ThP and cyclic AMP (4 microM) had no effect on the Ca uptake of PM-F and no influence on the effects of Pap. These results suggest that Pap relaxation of hog biliary smooth muscle results from the interaction of the drug with the plasma membrane causing cyclic AMP-independent sequestration of Ca.

Animals↗

Identification and characterization of adrenergic receptors and catecholamine-stimulated adenylate cyclase in hog pial membranes.

In order to define the adrenergic receptors in small pial blood vessels, we studied [3H]dihydroalprenolol (DHA) binding, [3H]dihydroergocryptine (DHE) binding, and catecholamine-stimulated adenylate cyclase in membranes prepared from the hog pia. [3H]dha bound to a saturable number of sites (0.09 pmol/mg protein) with a high affinity to (10 mM). The ability of a small series of adrenergic agents to compete for [3H]DHA binding was as expected for binding to beta-adrenergic membrane receptors. The receptor binding appeared to be composed largely of beta 2-adrenergic sites but some sites with beta 1 properties were detected. The beta-adrenergic agonist, isoproterenol, stimulated adenylate cyclase activity by 20% in pial membranes in the presence of GTP. The potency of catecholamines in stimulating adenylate cyclase correlated well with theif sites (0.39 pmol/mg) on these membranes. alpha-Adrenergic agents were potent competitors for [3H]DHE binding but dopamine, serotonin and histamine had effects only at high concentrations. These data demonstrate the presence of alpha- and beta-adrenergic membrane receptors and beta-adrenergically stimulated adenylate cyclase activity in small pial blood vessels from the hog.

Adenosine Triphosphate↗

Hog cholera virus--characterization of specific antiserum and identification of cDNA clones.

A specific antiserum was raised against the pestivirus inducing hog cholera (hog cholera virus, HCV). Using immunoprecipitation and SDS-PAGE, this antiserum served for comparison of HCV-induced proteins with those from a related and better characterized pestivirus, bovine viral diarrhea virus (BVDV). In addition to immunological relationships, the apparent molecular weights of some proteins induced by both viruses were quite similar. HCV genomic RNA was found to be about 12 kb in length, comparable to BVDV RNA. cDNA was synthesized starting from RNA isolated from partially purified virions and cloned in lambda gt11. Screening with the antiserum resulted in identification of several positive clones. Partial sequencing of one HCV-derived cDNA clone revealed a high degree of homology to a portion of the BVDV sequence.

Amino Acid Sequence↗

Hog cholera diagnostic techniques.

Clinical signs and lesions can sometimes provide the basis for a presumptive diagnosis of hog cholera (HC). However, an accurate diagnosis requires laboratory testing. The usual procedure for the detection of viral antigen is the examination of cryostat sections stained with fluorescein-conjugated HC antiserum. A more definitive technique is isolation of the virus in PK-15 cell cultures and identification of the viral antigen in cells using an HC fluorescent antibody conjugate. As bovine viral diarrhea (BVD) virus will cross-react with HC virus, isolation must be confirmed by the comparison of BVD and HC staining or, preferably, by the use of monoclonal antibodies that can differentiate between HC and BVD viruses. Hog cholera surveillance must rely on serology. The fluorescent antibody virus neutralization (FAVN) test is the classical technique, and HC and BVD antibody can usually be differentiated if HC-positive serum samples are tested against both viruses. Recently the enzyme-linked immunosorbent assay (ELISA) and peroxidase-labeled antibody tests have become the commonly used techniques.

Animals↗