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PubMed1981

A trisialosyl ganglioside GT3 of hog kidney. Structure and biosynthesis in vitro.

A trisialosyl ganglioside was isolated from hog kidney cortex and purified with a yield of 6.8 nmol/g tissue or 13 mol % of total gangliosides. The homogeneous ganglioside was subjected to graded neuraminidase treatment, mild acid hydrolysis, periodate oxidation-borohydride reduction, permethylation analysis and chromium trioxide oxidation. The results suggested that the structure of this ganglioside is NeuAc alpha 2-8NeuAc alpha 2-8NeuAc alpha 2-3Gal beta 1-4Glc beta 1-1Cer (GT3). On the addition of exogenous disialosyl ganglioside GD3 and radioactive CMP-NeuAc, a GT3 synthesis activity was demonstrated in a crude membrane fraction of hog kidney. The activity was greatest in the presence of detergents and had a pH optimum of 6.4. Apparent Km values for CMP-NeuAc and GD3 were about 0. 6 and 0.1 mM, respectively. The reaction produce was assigned as GT3 by chromatographic separation, carbohydrate analysis and periodate oxidation followed by borohydride reduction.

Animals↗
PubMed1982

Purification and characterization of multiple forms of mutarotase from hog kidney cortex.

The enzyme mutarotase [aldose 1-epimerase, EC 5.1.3.3] from hog kidney cortex was separated into four fractions (designated types I, II, III, and IV in order of elution) by column chromatography on DEAE-cellulose. Two major forms, types I and II, were purified to homogeneity as judged by polyacrylamide gel electrophoresis and isoelectric focusing on thin layer polyacrylamide gel. Types I, II, III, and IV had isoelectric points of 5.78, 5.48, 5.23, and 5.10, respectively. The following physicochemical properties were common to all four types: molecular weight, 41,000; Km for alpha-D-glucose at pH 7.4 and 25 degrees C, 19 mM; optimum pH, 6.5-7.5; optimum temperature, 30-37 degrees C; heat stability, up to 50 degrees C. On double immunodiffusion, the four types of mutarotase gave single precipitin lines, which fused completely with each other, against the antibody to purified type II enzyme. Types I and II had an identical amino-terminal residue, arginine, and an identical carboxyl-terminal sequence, -(Phe-Phe-Ser-Val)-Val-Ala. The amino acid composition of type I was almost identical with that of type II. Very similar tryptic peptide maps were obtained from types I and II, with only a few points of variance. These results suggest that the four types of hog kidney mutarotase are quite similar but not identical.

Amino Acids↗
PubMed1993

The effect of nerve root lesioning on various somatosensory evoked potentials in the hog.

Somatosensory evoked potentials (SEPs) were recorded at the lumbar spine following stimulation of the tibial nerve (mixed-nerve SEP; MSEP), the sural nerve (specific nerve SEP; SSEP), and the skin corresponding to the L6 and S1 dermatomes (dermatomal field SEP; DSEP-L and DSEP-S) in the hog. To determine the sensitivity of these three SEPs to the single nerve root (S1 root) function, the effects of nerve roots lesioning were investigated. Cutting S1 nerve root reduced the peak-to-peak amplitude of MSEP by only 28% in comparison with baseline values. The relative amplitudes of SSEP, DSEP-L, and DSEP-S were decreased by 46%, 11% and 51%, respectively. When S1 nerve root was left intact and L5, L6, and S2 nerve roots were cut, the relative amplitudes of MSEP, SSEP, DSEP-L, and DSEP-S were decreased to 68%, 73%, 31%, and 74%, respectively. These results indicate that DSEP-S is as sensitive to the function of S1 nerve root as SSEP but the sensitivities of DSEP-S and SSEP are low in the hog. MSEP is shown unsuitable to monitor the single nerve root dysfunction.

Animals↗
PubMed2006

Adaptor protein Ste50p links the Ste11p MEKK to the HOG pathway through plasma membrane association.

In a variety of yeast cellular pathways, the Ste50p protein regulates the kinase function of the mitogen extracellular signal-regulated kinase kinase (MEKK) Ste11p. Both Ste11p and Ste50p contain sterile alpha motif (SAM) domains; these are interchangeable, and can be replaced by other protein-interacting modules. Furthermore, the function of the Ras association (RA)-like domain of Ste50p can be mimicked by a plasma membrane recruiting signal, and direct plasma membrane targeting of Ste11p bypasses the requirement of Ste50p for Ste11p function. Thus the regulatory role of Ste50p requires both the N-terminal SAM domain to bind Ste11p and the C-terminal RA-like domain to direct kinase localization. We have identified Opy2p, an integral membrane protein that can interact with Ste50p, as a new component in the Sho1p-Ste11p/Ste50p signaling branch of the high-osmolarity glycerol (HOG) pathway. We propose that Opy2p can serve as a membrane anchor for the Ste50p/Ste11p module in the activation of the HOG pathway.

Cell Membrane↗
PubMed1966

Characterization of hog cholera virus. I. Determination of buoyant density.

Horzinek, Marian (Tierärztliche Hochschule, Hannover, West Germany). Characterization of hog cholera virus. I. Determination of buoyant density. J. Bacteriol. 92:1723-1726. 1966.-Hog cholera virus was subjected to cesium chloride density gradient centrifugation. Most of the infectious activity was detected in fractions with densities between 1.15 and 1.20 g/ml, with a peak at 1.16 g/ml. Infectivity was assayed by use of either the exaltation of Newcastle disease virus method or the hemagglutination exaltation and inhibition of cytopathic effect method.

Centrifugation, Density Gradient↗
PubMed1994

Reverse transcriptase-PCR assay for detection of hog cholera virus.

A reverse transcriptase-PCR strategy was developed for the detection of hog cholera virus. Hog cholera virus template was amplified from tissue culture fluids and from tissues and blood of infected pigs, but not from samples containing other pestiviruses. Restriction endonuclease analysis identified samples as historic or recent isolates.

Animals↗
PubMed1999

Repressors and upstream repressing sequences of the stress-regulated ENA1 gene in Saccharomyces cerevisiae: bZIP protein Sko1p confers HOG-dependent osmotic regulation.

The yeast ENA1/PMR2A gene encodes a cation extrusion ATPase in Saccharomyces cerevisiae which is essential for survival under salt stress conditions. One important mechanism of ENA1 transcriptional regulation is based on repression under normal growth conditions, which is relieved by either osmotic induction or glucose starvation. Analysis of the ENA1 promoter revealed a Mig1p-binding motif (-533 to -544) which was characterized as an upstream repressing sequence (URSMIG-ENA1) regulated by carbon source. Its function was abolished in a mig1 mig2 double-deletion strain as well as in either ssn6 or tup1 single mutants. A second URS at -502 to -513 is responsible for transcriptional repression regulated by osmotic stress and is similar to mammalian cyclic AMP response elements (CREs) that are recognized by CREB proteins. This URSCRE-ENA1 element requires for its repression function the yeast CREB homolog Sko1p (Acr1p) as well as the integrity of the Ssn6p-Tup1p corepressor complex. When targeted to the GAL1 promoter by fusing with the Gal4p DNA-binding domain, Sko1p acts as an Ssn6/Tup1p-dependent repressor regulated by osmotic stress. A glutathione S-transferase-Sko1 fusion protein binds specifically to the URSCRE-ENA1 element. Furthermore, a hog1 mitogen-activated protein kinase deletion strain could not counteract repression on URSCRE-ENA1 during osmotic shock. The loss of SKO1 completely restored ENA1 expression in a hog1 mutant and partially suppressed the osmotic stress sensitivity, qualifying Sko1p as a downstream effector of the HOG pathway. Our results indicate that different signalling pathways (HOG osmotic pathway and glucose repression pathway) use distinct promoter elements of ENA1 (URSCRE-ENA1 and URSMIG-ENA1) via specific transcriptional repressors (Sko1p and Mig1/2p) and via the general Ssn6p-Tup1p complex. The physiological importance of the relief from repression during salt stress was also demonstrated by the increased tolerance of sko1 or ssn6 mutants to Na+ or Li+ stress.

Adenosine Triphosphatases↗
PubMed2001

Ptc1, a type 2C Ser/Thr phosphatase, inactivates the HOG pathway by dephosphorylating the mitogen-activated protein kinase Hog1.

The HOG (high-osmolarity glycerol) mitogen-activated protein kinase (MAPK) pathway regulates the osmotic stress response in the yeast Saccharomyces cerevisiae. Three type 2C Ser/Thr phosphatases (PTCs), Ptc1, Ptc2, and Ptc3, have been isolated as negative regulators of this pathway. Previously, multicopy expression of PTC1 and PTC3 was shown to suppress lethality of the sln1Delta strain due to hyperactivation of the HOG pathway. In this work, we show that PTC2 also suppresses sln1Delta lethality. Furthermore, the phosphatase activity of these PTCs was needed for suppression, as mutation of a conserved Asp residue, likely to coordinate a metal ion, inactivated PTCs. Further analysis of Ptc1 function in vivo showed that it inactivates the MAPK, Hog1, but not the MEK, Pbs2. In the wild type, Hog1 kinase activity increased transiently, approximately 12-fold in response to osmotic stress, while overexpression of PTC1 limited activation to approximately 3-fold. In contrast, overexpression of PTC1 did not inhibit phosphorylation of Hog1 Tyr in the phosphorylation lip, suggesting that Ptc1 does not act on Pbs2. Deletion of PTC1 also strongly affected Hog1, leading to high basal Hog1 activity and sustained Hog1 activity in response to osmotic stress, the latter being consistent with a role for Ptc1 in adaptation. In vitro, Ptc1 but not the metal binding site mutant, Ptc1D58N, inactivated Hog1 by dephosphorylating the phosphothreonine but not the phosphotyrosine residue in the phosphorylation lip. Consistent with its role as a negative regulator of Hog1, which accumulates in the nucleus upon activation, Ptc1 was found in both the nucleus and the cytoplasm. Thus, one function of Ptc1 is to inactivate Hog1.

Active Transport, Cell Nucleus↗
PubMed1984

Release of active and inactive renin from hog renal cortical slices in vitro.

Both inactive and active renin were released from renal cortical slices of the hog. Isoproterenol, prostaglandin E1, and dibutyryl cAMP stimulated the release of both inactive and active renin. Renal kallikrein caused selective stimulation of the release of active renin and suppressed the release of inactive renin. Bradykinin and kallidin did not stimulate renin release. The effect of kallikrein was abolished by aprotinin but not by indomethacin. These observations indicate that the effect of kallikrein is not mediated via kinin formation or prostaglandin generation. The data suggest that there may be at least two types of mechanism for renin release from hog kidney. One is of the nonselective type by which both active and inactive renin are released, as in the case of beta-adrenergic or prostaglandin stimulation. The other is a selective mechanism by which only active renin is preferentially released, as in the case of urinary or renal kallikrein stimulation.

1-Methyl-3-isobutylxanthine↗
PubMed2004

Hog barn dust extract augments lymphocyte adhesion to human airway epithelial cells.

The dust of hog confinement facilities induces airway inflammation. Mechanisms by which this dust modulates inflammation are not completely defined, although it is clear that exposure to dust can modulate both epithelial cell and inflammatory cell function. In this work, we demonstrate that airway epithelial cell (BEAS-2B) treatment with hog barn dust extract (HDE) results in augmentation of peripheral blood lymphocyte adhesion to epithelial cell cultures in vitro. The augmentation of lymphocyte adhesion to epithelial cells is dependent on the concentration of HDE and time of HDE exposure, with twofold increases observed by 3 h and maintained at 24 h. Similar results are seen with primary human bronchial epithelial cells in culture. Lymphocyte adhesion to epithelial cells is inhibited in a concentration-dependent fashion by the treatment of epithelial cells with antibody to intercellular adhesion molecule-1 (ICAM-1). In addition, HDE exposure of epithelial cells results in an approximate twofold increase in ICAM-1 expression as determined by flow cytometry analysis. Pretreatment of epithelial cells with a protein kinase C-alpha (PKC-alpha) inhibitor, Gö-6976, also inhibited subsequent lymphocyte adhesion to HDE-exposed epithelial cells. These data suggest that airway epithelial cell HDE exposure enhances subsequent lymphocyte adhesion to epithelial cells that is mediated in part by HDE modulation of ICAM-1 expression and PKC-alpha.

Agriculture↗
PubMed1987

Identification of Na+,K+-ATPase inhibitors of volume-expanded hog plasma.

Na+,K+-adenosine triphosphatase (ATPase) inhibitors possessing inhibitory activities against the specific binding of ouabain to Na+,K+-ATPase and 86Rb uptake into hog erythrocytes have been purified from the plasma of hog acutely infused with saline. The purifications were performed by a combination of Amberlite XAD-2 adsorption chromatography and several steps of high performance liquid chromatography using four different types of columns. Inhibitors purified to homogeneity were identified as linoleic and oleic acids, gamma-stearoyllysophosphatidylcholine, gamma-arachidoyllysophosphatidylcholine, gamma-linoleoyllysophosphatidylcholine, and gamma-oleoyllysophosphatidylcholine. Small amounts of beta-arachidoyllysophosphatidylcholine, gamma-docosapentaenoyllysophosphatidylcholine, gamma-eicosatrienoyllysophosphatidylcholine, and gamma-palmitoyllysophosphatidylcholine were also detected by both fast atom bombardment mass and proton nuclear magnetic resonance spectrometric studies. Only gamma-acyllysophosphatidylcholines showed inhibitory activities on Na+,K+-ATPase and ouabain-binding activities. These lysophosphatidylcholines and unsaturated free fatty acids were effective at 100 microM levels in attaining 50% inhibition of the enzyme activity. The ouabain-displacing activity in plasma caused by these compounds increased with time during saline infusion. The maximal plasma levels of these components were approximately 10 times higher than that in the preinfusion plasma sample.

Animals↗
PubMed1982

Energy cost of membrane depolarization in hog carotid artery.

Past studies have shown that during stable stepwise activations of vascular smooth muscle with varying concentrations of high-K+, both cytoplasmic free-Ca++ and membrane depolarization vary. On the other hand, during stepwise activations with varying concentrations of external Ca++ in the presence of constant external Ca++ in the presence of constant external depolarizing high-K+, cytoplasmic free-Ca++ varies, while membrane depolarization remains relatively constant. In this study, the rates at which suprabasal energy metabolism (oxygen consumption and lactic acid production) increased with increasing isometric tension maintenance were measured under both circumstances. Suprabasal energy metabolism with increasing membrane depolarization (increasing external K+) exceeded that with constant depolarizing-[K+] and varying Ca++ by less than 2.5% at all levels of activation, which was not statistically significant (P greater than 0.70). We conclude therefore that the steady state metabolic energy cost of membrane depolarization per se during contractile activity in vascular smooth muscle from a tonic conducting vessel (hog carotid artery) is negligible. Although the possibility cannot be excluded, we find no metabolic evidence that increased cytoplasmic free-Ca++ itself activates an ATPase associated with Ca++ sequestration and/or extrusion beyond that present in the relaxed state. Activation of hog carotid artery with an isosmotic K+-for-Na+-substituted medium fails to stimulate aerobic glycolysis at all levels of K+ substitution. Experiments were performed at the muscle length optimal for isometric tension generation and at 37 degrees C.

Adenosine Triphosphate↗
PubMed1982

Effect of histamine on the energy metabolism of K+-depolarized hog carotid artery.

In a previous study (Peterson and Glück, 1982), activation of hog carotid artery with high-K+ medium caused no increase in aerobic glycolysis (lactic acid production). In contrast, histamine alone is found to stimulate aerobic glycolysis in a tension-dependent fashion (GLück and Paul, 1977). In this study, the addition of histamine to the already K+-depolarized hog carotid artery induced additional contraction, elevated tissue cyclic adenosine 3',5'-monophosphate [cAMP] levels, coupled the rate of aerobic glycolysis to external [Ca++] and isometric tension, and caused suprabasal energy utilization to exceed that required to support the contraction alone by approximately 25%. Increased cytoplasmic free-[Ca++] per se does not stimulate aerobic glycolysis. In the presence of histamine, however, aerobic glycolysis is Ca++-sensitive. Whereas a cycle of Ca++ depletion and restoration has only a small effect on basal metabolic rates in arteries activated with high-K+ alone, the same procedure with arteries stimulated by high-K+ with added histamine causes a dramatic shift in basal metabolic rates toward higher levels of glycolysis.

Adenosine Triphosphate↗
PubMed1988

A new Ca-antagonist, CD-349, binding to the Ca-channel of rat myocardium and brain and hog coronary artery.

The binding to a Ca-channel of a novel 1,4-dihydropyridine (DHP) Ca-antagonist, 2-nitratopropyl 3-nitratopropyl 2,6-dimethyl-4-(3-nitrophenyl)-1,4-dihydropyridine-3,5-dicarboxylate (CD-349), was studied in rat myocardium and brain and hog coronary artery, and the binding was compared with that of other DHPs. In rat myocardium, the binding reaction of [3H]CD-349 was faster than that of nitrendipine (NTD). The association rate constant of [3H]CD-349 was about 10 times higher than that of [3H]NTD. The dissociation rate was also higher than that of [3H]NTD. Scatchard plot analysis of [3H]CD-349 binding showed one high affinity site for CD-349. The dissociation constant (Kd) and maximum number of binding sites (Bmax) were 333 pM and 286 fmoles/mg protein. They were almost the same as those for [3H]NTD. [3H]CD-349 and [3H]NTD bindings were dose dependently inhibited by 1,4-DHPs: nifedipine, nimodipine, nicardipine and CD-349. The order of the inhibitory potency of these drugs was CD-349 greater than nicardipine greater than nimodipine greater than nifedipine, when [3H]CD-349 and [3H]NTD were used as the ligands. Similar results were obtained for rat brain and hog coronary artery. [3H]CD-349 binding was not changed by alpha- or beta-adrenergic, cholinergic, histaminergic or serotonergic agents in rat myocardium. From these results, it is suggested that CD-349 binds to the Ca-channel reversibly with high affinity due to its high association rate for the site.

Animals↗
PubMed1989

Spectrophotometric kinetic studies and substrate inhibition of hog kidney histaminase activity by an improved 2,4-dinitrophenylhydrazine method.

We improved the experimental procedure for the measurement of hog kidney histaminase activity using histamine as a substrate on the basis of a spectrophotometric estimation of the 2,4-dinitrophenylhydrazone of imidazole acetaldehyde and studied the steady-state kinetics to obtain the basic data for further investigations of the oxidative deamination of histamine. The initial and mean velocities of the enzymatic reaction were calculated and plotted against the amount of enzyme. It was found that the initial velocity increased linearly. The time t alpha necessary to reach the extent of reaction alpha was calculated and plotted against the reciprocal of the enzyme concentration eO. It was found that t alpha was linearly proportional to 1/eO. From Lineweaver-Burk plots, inhibition by high concentration of substrate was evident, and the v-pS curve was bell-shaped, with a pS maximum at 3.2. Km and V were obtained: Km = 7.7 x 10(-5) M, V = 0.0026 mumol/min (0.00075 mumol/min/mg protein). It was concluded that our DNP method was useful for the measurement of hog kidney histaminase activity using histamine as a substrate, basic steady-state kinetic studies and further investigations of substrate inhibition and inhibitory effect.

Amine Oxidase (Copper-Containing)↗
PubMed1975

The effect of iodide administration on hog thyroid gland and the composition of thyroglobulin and 27-S iodoprotein.

The effect of excess iodide on hog thyroid gland has been examined with regard to the change in the chemical composition of thyroglobulin and in the accumulation of 27-S iodoprotein by the in vivo treatment of hogs with iodide for various lengths of time. The iodine content of thyroglobulin was either unchanged by short term administration of excess iodide, or somewhat lowered. However, the iodine content as well as the total amount of thyroglobulin increased in the glands enlarged by prolonged treatment with iodide. The iodine highest reached 1.17% of the protein on an average. On the other hand, 27-S iodoprotein decreased and finally disappeared after the chronic treatment. Monoiodotyrosine and diiodotyrosine increased in parallel with the increase in the iodine content (0.15 to 1.17%) caused by the iodide treatment, while thyroxine increased but reached a plateau at the level of three residues per mole of thyroglobulin, and no change was observed even in the proteins with the higher iodine content than 0.75%. Proteolytic activity measured by amino acid release from the thyroid protein was depressed by the chronic treatment. On the other hand, the amount of iodocompound released by the autoproteolysis, which may reflect hormone secretion, increased, possibly because of the marked increase in the iodine content of thyroglobulin.

Animals↗
PubMed1981

Stimulation of protein-bound iodine formation by lipid extracts from hog thyroid microsomes.

The lipid materials extracted from hog thyroid microsomes were found to contain factors which stimulated both the NADPH oxidation by NADPH-cytochrome c reductase and PBI formation by a reconstituted system containing the reductase as a hydrogen peroxide generator and thyroid peroxidase. For both reactions, the stimulating activity in the extracts from the other subcellular fractions was less than that observed in the extracts from microsomal fraction. Lipids extracted from hog liver microsomes did not show any NADPH oxidation stimulating activity. Thin-layer chromatography of the lipid extracts from thyroid microsomes revealed the presence of at least two stimulating factors differing in chromatographic behaviour. At least one of the stimulating factors separated on TLC stimulated the oxygen consumption accompanied by generation of hydrogen peroxide due to the NADPH oxidation by NADPH-cytochrome c reductase. From these results it was suggested that in thyroid microsomes, but not in liver microsomes, there were stimulating factors extractable by chloroform-methanol. The factors could stimulate NADPH oxidation by NADPH-cytochrome c reductase followed by generation of hydrogen peroxide, resulting in the enhancement of PBI formation coupled with thyroid peroxidase.

Animals↗
PubMed1998

Effects of preslaughter management on the quality of carcasses from porcine stress syndrome heterozygous market hogs.

The objectives of this study were to determine whether two preslaughter management treatments, rest and mixing, influence the muscle quality of porcine stress syndrome (PSS) heterozygous (Nn) market hogs and to verify the expected quality characteristics of carcasses produced from PSS-normal (NN) and PSS-susceptible (nn) animals. Twenty-nine Nn, 14 NN, and 9 nn market hogs were randomly assigned to preslaughter handling treatments. One-half of the animals in each genotype group received 16 h of rest before slaughter, and the remaining pigs were slaughtered immediately upon arrival at the Iowa State University Meat Laboratory. Within each group, half of the Nn animals were mixed with unfamiliar pigs during transport and lairage. Length, backfat, and loin muscle area (LMA) were not affected by mixing and rest treatment. The carcasses from nn pigs had less fat (P < .05) measured at the 10th rib (off midline) and last lumbar vertebra (midline) and possessed larger LMA than carcasses from NN pigs. Heterozygous pigs were intermediate for most carcass traits. Carcass pH values among heterozygous groups were not significantly different, except that the rested animals had higher ultimate pH values (P < .01) and higher 45-min pH values. Resting had no effect on pH of NN or nn pigs. The 45-min pH values of nn carcasses were lower (P < .01) than those of NN carcasses, but ultimate pH values were similar. Values of unrested Nn animals were between those of NN and nn genotypes but with rest approached values of NN pigs. Loin muscle Minolta-Y and Hunter-L values from unrested Nn animals were higher ( P < .05) than those of rested Nn animals. Mixing did not influence these traits. The longissimus muscle lipid content was not influenced by treatment but differed among genotypes (P < .01). Glycogen levels of rested Nn animals tended to be lower than those of NN animals and approached those of nn pigs. Mixing of Nn animals resulted in higher (P < .05) chewiness scores of cooked loin chops. No significant cooking loss or InstronTM tenderness differences were observed between the PSS-Nn treatment groups. Even though 16 h of rest before slaughter improved the color and water-holding capacity of Nn pigs, effects were small and were much less than those that were due to the PSS gene.

Animals↗