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Author |
Nicol, C.J.; Adachi, M.; Akiyama, T.E.; Gonzalez, F.J. |
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Title |
PPARgamma in endothelial cells influences high fat diet-induced hypertension |
Type |
Journal Article |
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Year |
2005 |
Publication |
American journal of hypertension : journal of the American Society of Hypertension |
Abbreviated Journal |
Am J Hypertens |
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Volume |
18 |
Issue |
4 Pt 1 |
Pages |
549-556 |
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Keywords  |
Administration, Oral; Animals; Antihypertensive Agents/pharmacology; Blood Pressure/drug effects; Diabetes Mellitus, Type 2/physiopathology; Dietary Fats/*administration & dosage/pharmacology; Dose-Response Relationship, Drug; Endothelial Cells/*metabolism; Female; Heart Rate/drug effects; Hypertension/*etiology; Ligands; Male; Mice; Mice, Knockout; PPAR gamma/*metabolism; Sodium Chloride/administration & dosage/pharmacology; Thiazolidinediones/pharmacology |
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Abstract |
BACKGROUND: Peroxisome proliferator-activated receptor gamma (PPARgamma) ligands improve human hypertension. However, the mechanism and site of this effect remains unknown, confounded by PPARgamma expression in many cell types, including endothelial cells (ECs). METHODS: To evaluate the vascular role of PPARgamma we used a conditional null mouse model. Specific disruption of PPARgamma in ECs was created by crossing Tie2-Cre+ transgenic (T2T+) and PPARgamma-floxed (fl/fl) mice to generate PPARgamma (fl/fl)T2T+ (PPARgamma E-null) mice. Conscious 8- to 12-week-old congenic PPARgamma (fl/fl)Cre- (wild type) and PPARgamma E-null mice were examined for changes in systolic blood pressure (BP) and heart rate (HR), untreated, after 2 months of salt-loading (drinking water), and after treatment for 3 months with high fat (HF) diet alone or supplemented during the last 2 weeks with rosiglitazone (3 mg/kg/d). RESULTS: Untreated PPARgamma E-nulls were phenotypically indistinguishable from wild-type littermates. However, compared to similarly treated wild types, HF-treated PPARgamma E-nulls had significantly elevated systolic BP not seen after normal diet or salt-loading. Despite sex-dependent baseline differences, salt-loaded and HF-treated PPARgamma E-nulls of either sex had significantly elevated HR versus wild types. Interestingly, rosiglitazone improved serum insulin levels, but not HF diet-induced hypertension, in PPARgamma E-null mice. CONCLUSIONS: These results suggest that PPARgamma in ECs not only is an important regulator of hypertension and HR under stressed conditions mimicking those arising in type 2 diabetics, but also mediates the antihypertensive effects of rosiglitazone. These data add evidence supporting a beneficial role for PPARgamma-specific ligands in the treatment of hypertension, and suggest therapeutic strategies targeting ECs may prove useful. |
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Laboratory of Metabolism, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892, USA |
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0895-7061 |
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PMID:15831367 |
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Call Number |
refbase @ user @ |
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69 |
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Kasashima, Y.; Takahashi, T.; Smith, R.K.W.; Goodship, A.E.; Kuwano, A.; Ueno, T.; Hirano, S. |
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Title |
Prevalence of superficial digital flexor tendonitis and suspensory desmitis in Japanese Thoroughbred flat racehorses in 1999 |
Type |
Journal Article |
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Year |
2004 |
Publication |
Equine Veterinary Journal |
Abbreviated Journal |
Equine Vet J |
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Volume |
36 |
Issue |
4 |
Pages |
346-350 |
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Keywords |
Age Factors; Animals; Female; Forelimb; Hindlimb; Horse Diseases/*epidemiology/etiology; Horses; Inflammation/epidemiology/etiology/*veterinary; Japan/epidemiology; Ligaments/injuries/*pathology; Male; Musculoskeletal Diseases/epidemiology/etiology/veterinary; *Physical Conditioning, Animal; Prevalence; Retrospective Studies; Risk Factors; Sex Factors; Sports; Tendinopathy/epidemiology/etiology/*veterinary; Tendon Injuries/epidemiology/etiology/*veterinary |
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Abstract |
REASONS FOR PERFORMING STUDY: Overstrain injuries to the superficial digital flexor tendon (SDFT) and suspensory ligament (SI) are among the most common musculoskeletal injuries which contribute to the considerable wastage of racing Thoroughbreds. Many epidemiological studies have demonstrated the prevalence of and risk factors for tendon injury when racing but have not included those injuries sustained during training. However, since tendon injury during training is seen commonly in clinical practice, it is appropriate to determine the overall prevalence of tendon injury sustained during both training and racing. OBJECTIVE: To determine the prevalence of overstrain injury to the SDFT and SL during training and racing among Thoroughbred flat racehorses in Japan in 1999. METHODS: A retrospective study was performed using a sample population of 10,262 Thoroughbred racehorses. The medical information database of Thoroughbred racehorses registered by the Japan Racing Association (JRA) in 1999 was analysed for SDFT and SL overstrain injury diagnosed by a veterinarian employed by JRA during training and racing. Jump racehorses were excluded from this study. RESULTS: The prevalence of forelimb SDFT tendonitis and SL desmitis was 11.1% (1130 cases) and 3.61% (370 cases) of the population, respectively. In the hindlimb, there were 0.06% (6 cases) and 0.14% (14 cases), respectively. Risks of SDF tendonitis in the forelimb in 3-year-olds or older horses were significantly higher than in 2-year-olds. In contrast, the risk of SL desmitis in the forelimb at age 3 and 4 years was 2.23 and 2.11 times higher, respectively, than in 2-year-olds, but this increased to 5.07 times in those age > or = 5 years. Entire males were at greater risk in comparison to females and geldings. CONCLUSIONS: The results suggest that the prevalence of SDF tendonitis and SL desmitis in the forelimb was associated with the horse's age and sex. The prevalence of SL desmitis increased further with age compared with SDF tendonitis, possibly reflecting a more rapid accumulation of degeneration in this structure. POTENTIAL RELEVANCE: The age-related risk demonstrated in this study provides further support that overstrain injuries are associated with accumulated degeneration. These data provide a valuable resource for further research into the aetiology of tendon injury in the racehorse. |
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Equine Research Institute, Japan Racing Association, 321-4, Tokami-cho, Utsunomiya-shi, Tochigi, 320-0856, Japan |
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0425-1644 |
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PMID:15163043 |
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Call Number |
Equine Behaviour @ team @ |
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3775 |
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Weber-Mzell, D.; Kotanko, P.; Hauer, A.C.; Goriup, U.; Haas, J.; Lanner, N.; Erwa, W.; Ahmaida, I.A.; Haitchi-Petnehazy, S.; Stenzel, M.; Lanzer, G.; Deutsch, J. |
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Title |
Gender, age and seasonal effects on IgA deficiency: a study of 7293 Caucasians |
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Journal Article |
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Year |
2004 |
Publication |
European Journal of Clinical Investigation |
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Volume |
34 |
Issue |
3 |
Pages |
224-228 |
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Age- and gender-related variability; immunoglobulin A; seasonal variability; serum IgA deficiency |
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Background The frequency of serum IgA deficiency (SIgAD) differs between populations. We examined the prevalence of SIgAD in healthy Caucasians. Materials and methods Serum immunoglobulin A (SIgA) was measured in 7293 volunteers (2264 women, 5029 men) aged 30 ± 14·2 years (mean ± SD; range: 12–66). Serum immunoglobulin A and subnormal SIgA levels were defined by a SIgA level < 0·07 g L-1, and between 0·07 and 0·7 g L-1, respectively. Means were compared by analysis of variance (anova) and analysis of covariance (ancova); frequencies by the χ2 test. Results Fifteen subjects (0·21%; one woman, 14 men) had SIgAD. Subnormal SIgA levels were found in 155 persons (2·13%): 21 females (0·93% of the females) and 134 males (2·66% of the males; difference: 1·74%; 95% CI: 1·12–2·33%; P < 0·001). Males were more likely to have subnormal SIgA levels or SIgAD (odds ratio 3·09, 95% CI: 1·97–4·85). The prevalence of SIgAD and subnormal SIgA was lowest in winter (χ2 = 14·8; P = 0·002; 3 d.f.; and χ2 = 43·2; P < 0·001; 3 d.f., respectively). Serum immunoglobulin A concentrations were significantly higher during winter. Serum immunoglobulin A levels increased with age on average by 0·2 ± 0·06 g L-1 per decade of life (P < 0·001). Taking into account the influence of age, SIgA concentration was lower in females as compared with males. Conclusion The prevalence of SIgAD and subnormal SIgA levels is increased in males. There exists a significant influence of gender, age and seasons on SIgA levels. |
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Blackwell Science Ltd |
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1365-2362 |
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Equine Behaviour @ team @ |
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6127 |
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Author |
Andersson, P.; Kvassman, J.; Lindstrom, A.; Olden, B.; Pettersson, G. |
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Title |
Effect of NADH on the pKa of zinc-bound water in liver alcohol dehydrogenase |
Type |
Journal Article |
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Year |
1981 |
Publication |
European Journal of Biochemistry / FEBS |
Abbreviated Journal |
Eur J Biochem |
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Volume |
113 |
Issue |
3 |
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425-433 |
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Alcohol Oxidoreductases/*metabolism; Aldehydes/metabolism; Animals; Binding Sites; Cinnamates/metabolism; Horses; Hydrogen-Ion Concentration; Kinetics; Ligands; Liver/*metabolism; NAD/*metabolism; Water/metabolism; Zinc/metabolism |
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Equilibrium constants for coenzyme binding to liver alcohol dehydrogenase have been determined over the pH range 10--12 by pH-jump stop-flow techniques. The binding of NADH or NAD+ requires the protonated form of an ionizing group (distinct from zinc-bound water) with a pKa of 10.4. Complex formation with NADH exhibits an additional dependence on the protonation state of an ionizing group with a pKa of 11.2. The binding of trans-N,N-dimethylaminocinnamaldehyde to the enzyme . NADH complex is prevented by ionization of the latter group. It is concluded from these results that the pKa-11.2-dependence of NADH binding most likely derives from ionization of the water molecule bound at the catalytic zinc ion of the enzyme subunit. The pKa value of 11.2 thus assigned to zinc-bound water in the enzyme . NADH complex appears to be typical for an aquo ligand in the inner-sphere ligand field provided by the zinc-binding amino acid residues in liver alcohol dehydrogenase. This means that the pKa of metal-bound water in zinc-containing enzymes can be assumed to correlate primarily with the number of negatively charged protein ligands coordinated by the active-site zinc ion. |
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0014-2956 |
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PMID:7011796 |
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Equine Behaviour @ team @ |
Serial |
3810 |
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Author |
Hirota, S.; Suzuki, M.; Watanabe, Y. |
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Title |
Hydrophobic effect of trityrosine on heme ligand exchange during folding of cytochrome c |
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Journal Article |
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Year |
2004 |
Publication |
Biochemical and Biophysical Research Communications |
Abbreviated Journal |
Biochem Biophys Res Commun |
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314 |
Issue |
2 |
Pages |
452-458 |
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Amino Acids/chemistry; Animals; Cytochromes c/*chemistry; Heme/*chemistry; Histidine/chemistry; Horses; Hydrogen-Ion Concentration; Kinetics; Ligands; Myocardium/chemistry; Peptides/chemistry; Protein Folding; Spectrophotometry; Spectrum Analysis, Raman; Tyrosine/*analogs & derivatives/*chemistry |
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Abstract |
Effect of a hydrophobic peptide on folding of oxidized cytochrome c (cyt c) is studied with trityrosine. Folding of cyt c was initiated by pH jump from 2.3 (acid-unfolded) to 4.2 (folded). The Soret band of the 2-ms transient absorption spectrum during folding decreased its intensity and red-shifted from 397 to 400 nm by interaction with trityrosine, whereas tyrosinol caused no significant effect. The change in the transient absorption spectrum by interaction with trityrosine was similar to that obtained with 100 mM imidazole, which showed that the population of the intermediate His/His coordinated species increased during folding of cyt c by interaction with trityrosine. The absorption change was biphasic, the fast phase (82+/-9s(-1)) corresponding to the transition from the His/H(2)O to the His/Met coordinated species, whereas the slow phase (24+/-3s(-1)) from His/His to His/Met. By addition of trityrosine, the relative ratio of the slow phase increased, due to increase of the His/His species at the initial stage of folding. According to the resonance Raman spectra of cyt c, the high-spin 6-coordinate and low-spin 6-coordinate species were dominated at pH 2.3 and 4.2, respectively, and these species were not affected by addition of trityrosine. These results demonstrated that the His/His species increased by interaction with trityrosine at the initial stage of cyt c folding, whereas the heme coordination structure was not affected by trityrosine when the protein was completely unfolded or folded. Hydrophobic peptides thus may be useful to study the effects of hydrophobic interactions on protein folding. |
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Department of Physical Chemistry, Kyoto Pharmaceutical University, Yamashina-ku, 607-8414 Kyoto, Japan. hirota@mb.kyoto-phu.ac.jp |
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0006-291X |
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PMID:14733927 |
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Equine Behaviour @ team @ |
Serial |
3777 |
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Skandakumar, S.; Stodulski, G.; Hau, J. |
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Title |
Salivary IgA: a Possible Stress Marker In Dogs |
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1995 |
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Animal Welfare |
Abbreviated Journal |
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4 |
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4 |
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339-350 |
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Animal Welfare; Behaviour; Cortisol; Dog; Salivary Iga (S-Iga); Stress; Well-Being |
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Stress in humans has been reported to be associated with a decrease in the salivary immunoglobulin A (s-IgA) levels enabling the possible use of s-IgA to assess stress. Prolonged stress, if reliably assessed in a non-invasive manner, may be used to assess animal welfare. This study analysed groups of dogs undergoing physical and temperamental training and s-IgA levels were measured by rocket immunoelectrophoresis in prospective samples. Behavioural assessment was carried out and cortisol levels in saliva were measured by ELISA. A significant negative correlation (P < 0.007) between the logarithmic cortisol concentrations and s-IgA levels in saliva was recorded. The behavioural assessment of the dogs agreed well with the biochemical markers. It is concluded that IgA levels in saliva may be a useful marker of dog well-being and that stress results in decreased s-IgA levels. |
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Equine Behaviour @ team @ |
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5964 |
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Abbruzzetti, S.; Viappiani, C.; Small, J.R.; Libertini, L.J.; Small, E.W. |
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Title |
Kinetics of histidine deligation from the heme in GuHCl-unfolded Fe(III) cytochrome C studied by a laser-induced pH-jump technique |
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Journal Article |
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Year |
2001 |
Publication |
Journal of the American Chemical Society |
Abbreviated Journal |
J Am Chem Soc |
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Volume |
123 |
Issue |
27 |
Pages |
6649-6653 |
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Animals; *Bacterial Proteins; Cytochrome c Group/*chemistry; Guanidine/*chemistry; Heme/*chemistry; Histidine/*chemistry; Horses; Hydrogen-Ion Concentration; Kinetics; *Lasers; Ligands; Protein Folding |
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Abstract |
We have developed an instrumental setup that uses transient absorption to monitor protein folding/unfolding processes following a laser-induced, ultrafast release of protons from o-nitrobenzaldehyde. The resulting increase in [H(+)], which can be more than 100 microM, is complete within a few nanoseconds. The increase in [H(+)] lowers the pH of the solution from neutrality to approximately 4 at the highest laser pulse energy used. Protein structural rearrangements can be followed by transient absorption, with kinetic monitoring over a broad time range (approximately 10 ns to 500 ms). Using this pH-jump/transient absorption technique, we have examined the dissociation kinetics of non-native axial heme ligands (either histidine His26 or His33) in GuHCl-unfolded Fe(III) cytochrome c (cyt c). Deligation of the non-native ligands following the acidic pH-jump occurs as a biexponential process with different pre-exponential factors. The pre-exponential factors markedly depend on the extent of the pH-jump, as expected from differences in the pK(a) values of His26 and His33. The two lifetimes were found to depend on temperature but were not functions of either the magnitude of the pH-jump or the pre-pulse pH of the solution. The activation energies of the deligation processes support the suggestion that GuHCl-unfolded cyt c structures with non-native histidine axial ligands represent kinetic traps in unfolding. |
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Dipartimento di Fisica, Universita di Parma, Istituto Nazionale per la Fisica della Materia, 43100 Parma, Italy |
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0002-7863 |
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PMID:11439052 |
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Equine Behaviour @ team @ |
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3788 |
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Dyson, H.J.; Beattie, J.K. |
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Spin state and unfolding equilibria of ferricytochrome c in acidic solutions |
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Journal Article |
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Year |
1982 |
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The Journal of Biological Chemistry |
Abbreviated Journal |
J Biol Chem |
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257 |
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5 |
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2267-2273 |
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Animals; *Cytochrome c Group; Electron Spin Resonance Spectroscopy; Heme; Horses; Hydrogen-Ion Concentration; Kinetics; Ligands; Myocardium; Protein Binding; Protein Conformation; Spectrophotometry; Temperature |
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Equilibrium, stopped flow, and temperature-jump spectrophotometry have been used to identify processes in the unfolding of ferricytochrome c in acidic aqueous solutions. A relaxation occurring in approximately 100 microseconds involves perturbation of a spin-equilibrium between two folded conformers of the protein with methionine-80 coordinated or dissociated from the heme iron. The protein unfolds more slowly, in milliseconds, with dissociation and protonation of histidine-18. These two transitions appear cooperative in equilibrium measurements at low (0.01 M) ionic strength, but are separated at higher (0.10 M) ionic strength. They are resolved under both conditions in the dynamic measurements. The spin-equilibrium description permits a unified explanation of a number of properties of ferricytochrome c in acidic aqueous solutions. |
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0021-9258 |
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PMID:6277891 |
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Equine Behaviour @ team @ |
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3807 |
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Rollot, Y.; Lecuyer, E.; Chateau, H.; Crevier-Denoix, N. |
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Title |
Development of a 3D model of the equine distal forelimb and of a GRF shoe for noninvasive determination of in vivo tendon and ligament loads and strains |
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Journal Article |
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Year |
2004 |
Publication |
Equine Veterinary Journal |
Abbreviated Journal |
Equine Vet J |
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Volume |
36 |
Issue |
8 |
Pages |
677-682 |
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Animals; Biomechanics; Floors and Floorcoverings; Forelimb/*physiology/ultrasonography; Gait/physiology; Horses/*physiology; Image Processing, Computer-Assisted; Imaging, Three-Dimensional/methods/*veterinary; Ligaments, Articular/*physiology; Locomotion/*physiology; Models, Biological; Shoes; Tendons/*physiology; Toe Joint/physiology/ultrasonography |
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REASONS FOR PERFORMING STUDY: As critical locomotion events (e.g. high-speed and impacts during racing, jump landing) may contribute to tendinopathies, in vivo recording of gaits kinematic and dynamic parameters is essential for 3D reconstruction and analysis. OBJECTIVE: To propose a 3D model of the forelimb and a ground reaction force recording shoe (GRF-S) for noninvasively quantifying tendon and ligament loads and strains. METHODS: Bony segments trajectories of forelimbs placed under a power press were recorded using triads of ultrasonic kinematic markers linked to the bones. Compression cycles (from 500-6000 N) were applied for different hoof orientations. Locations of tendon and ligament insertions were recorded with regard to the triads. The GRF-S recorded GRF over the hoof wall and used four 3-axis force sensors sandwiched between a support shoe and the shoe to be tested. RESULTS: Validation of the model by comparing calculated and measured superficial digital flexor tendon strains, and evaluation of the role of proximal interphalangeal joint in straight sesamoidean ligament and oblique sesamoidean ligament strains, were successfully achieved. Objective comparisons of the 3 components of GRF over the hoof for soft and hard grounds could be recorded, where the s.d. of GRF norm was more important on hard ground at walk and trot. CONCLUSIONS: Soft grounds (sand and rubber) dissipate energy by lowering GRF amplitude and diminish bounces and vibrations at impact. At comparable speed, stance phase was longer on soft sand ground. POTENTIAL RELEVANCE: The conjugate use of the GRF-S and the numerical model would help to quantify and analyse ground/shoe combination on comfort, propulsion efficiency or lameness recovery. |
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Address |
UMR INRA-ENVA de Biomecanique et Pathologie Locomotrice du Cheval, Ecole Nationale Veterinaire d'Alfort, 7, Avenue du General de Gaulle, 94704 Maisons-Alfort, France |
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0425-1644 |
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Notes |
PMID:15656495 |
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Call Number |
Equine Behaviour @ team @ |
Serial |
3769 |
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Author |
Meershoek, L.S.; Schamhardt, H.C.; Roepstorff, L.; Johnston, C. |
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Title |
Forelimb tendon loading during jump landings and the influence of fence height |
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Journal Article |
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Year |
2001 |
Publication |
Equine Veterinary Journal. Supplement |
Abbreviated Journal |
Equine Vet J Suppl |
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Issue |
33 |
Pages |
6-10 |
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Keywords |
Animals; Biomechanics; Forelimb/injuries/physiology; Horses/injuries/*physiology; Lameness, Animal/etiology; Ligaments, Articular/*physiology; Locomotion/*physiology; Physical Conditioning, Animal; Tendon Injuries/complications/physiopathology/veterinary; Tendons/*physiology; Weight-Bearing/physiology |
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Abstract |
Lameness in athletic horses is often caused by forelimb tendon injuries, especially in the interosseus tendon (TI) and superficial digital flexor tendon (SDF), but also in the accessory ligament (AL) of the deep digital flexor tendon (DDF). In an attempt to explain the aetiology of these injuries, the present study investigated the loading of the tendons during landing after a jump. In jumping horses, the highest forces can be expected in the trailing limb during landing. Therefore, landing kinematics and ground reaction forces of the trailing forelimb were measured from 6 horses jumping single fences with low to medium heights of 0.80, 1.00 and 1.20 m. The tendon forces were calculated using inverse dynamics and an in vitro model of the lower forelimb. Calculated peak forces in the TI, SDF and DDF + AL during landing were 15.8, 13.9 and 11.7 kN respectively. The relative loading of the tendons (landing forces compared with failure forces determined in a separate study) increased from DDF to TI to SDF and was very high in SDF. This explains the low injury incidence of the DDF and the high injury incidence of the SDF. Fence height substantially influenced SDF forces, whereas it hardly influenced TI forces and did not influence AL strain. Reduction of fence height might therefore limit the risks for SDF injuries, but not for TI and AL injuries. |
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Address |
Department of Veterinary Anatomy and Physiology, Institute for Fundamental and Clinical Human Movement Sciences, Faculty of Veterinary Medicine, Utrecht University, Utrecht, The Netherlands |
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English |
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Notes |
PMID:11721571 |
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Call Number |
Equine Behaviour @ team @ |
Serial |
3786 |
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