| Records |
| Author |
Schwarzenberger, F.; Mostl, E.; Bamberg, E.; Pammer, J.; Schmehlik, O. |
| Title |
Concentrations of progestagens and oestrogens in the faeces of pregnant Lipizzan, trotter and thoroughbred mares |
Type |
Journal Article |
| Year |
1991 |
Publication |
Journal of reproduction and fertility. Supplement |
Abbreviated Journal |
J Reprod Fertil Suppl |
| Volume |
44 |
Issue |
|
Pages |
489-499 |
| Keywords |
Animals; Estrogens/*analysis; Feces/*chemistry; Female; Gestational Age; Horses/*metabolism; Immunoenzyme Techniques; Labor, Obstetric; Pregnancy; Pregnancy, Animal/*metabolism; Pregnenes/analysis; Progestins/*analysis |
| Abstract |
Faecal samples were collected at weekly intervals from pregnant Lipizzan mares during Weeks 7-16 following mating and from Lipizzan, Trotter and Thoroughbred mares during the last 3 months of gestation. After parturition, samples were taken daily from the Thoroughbred mares for another 6 days. Non-pregnant mares served as controls. The concentrations of unconjugated oestrogens (Eg), 20 alpha-OH-progestagens (20 alpha-G) and 20 beta-OH-progestagens (20 beta-G) were measured by enzyme immunoassay. In the faeces of Lipizzan mares, immunoreactive progestagens were significantly (P less than 0.01) elevated above the levels in non-pregnant mares by Week 11, and Eg by Week 13 of pregnancy onwards. During the last 3 months of gestation, concentrations of Eg were significantly higher in Trotter mares than in Lipizzan and Thoroughbred mares. Concentrations of 20 alpha-G and 20 beta-G increased to maximal values in the last month of gestation. There was no significant difference among the 3 breeds with respect to 20 alpha-G but, during the 10 weeks before parturition, concentrations of 20 beta-G in the Lipizzan mares were significantly lower (P less than 0.05) than those in the Thoroughbred mares. They were also significantly lower than those of the Trotter mares during the last 4 weeks of gestation. After parturition, the concentrations of Eg and progestagens had declined to baseline values by Days 3 and 4 respectively. From these results we conclude that high concentrations of progestagens with 20 alpha- and 20 beta-hydroxyl groups are present in the faeces of pregnant mares, especially during the last month of gestation. |
| Address |
Institut fur Biochemie, Veterinary Medical University, Vienna, Austria |
| Corporate Author |
|
Thesis |
|
| Publisher |
|
Place of Publication |
|
Editor |
|
| Language |
English |
Summary Language |
|
Original Title |
|
| Series Editor |
|
Series Title |
|
Abbreviated Series Title |
|
| Series Volume |
|
Series Issue |
|
Edition |
|
| ISSN |
0449-3087 |
ISBN |
|
Medium |
|
| Area |
|
Expedition |
|
Conference |
|
| Notes |
PMID:1795293 |
Approved |
no |
Call Number  |
refbase @ user @ |
Serial |
322 |
| Permanent link to this record |
| |
|
| |
| Author |
Keay, J.M.; Singh, J.; Gaunt, M.C.; Kaur, T. |
| Title |
Fecal glucocorticoids and their metabolites as indicators of stress in various mammalian species: a literature review |
Type |
Journal Article |
| Year |
2006 |
Publication |
Journal of zoo and wildlife medicine : official publication of the American Association of Zoo Veterinarians |
Abbreviated Journal |
J Zoo Wildl Med |
| Volume |
37 |
Issue |
3 |
Pages |
234-244 |
| Keywords |
Animals; *Animals, Wild/metabolism; Chromatography, High Pressure Liquid/methods/veterinary; Circadian Rhythm; Conservation of Natural Resources; *Ecosystem; Feces/*chemistry; Glucocorticoids/*analysis/metabolism; Humans; Seasons; Species Specificity; Specimen Handling/methods/veterinary; Stress, Psychological/*metabolism |
| Abstract |
Conservation medicine is a discipline in which researchers and conservationists study and respond to the dynamic interplay between animals, humans, and the environment. From a wildlife perspective, animal species are encountering stressors from numerous sources. With the rapidly increasing human population, a corresponding increased demand for food, fuel, and shelter; habitat destruction; and increased competition for natural resources, the health and well-being of wild animal populations is increasingly at risk of disease and endangerment. Scientific data are needed to measure the impact that human encroachment is having on wildlife. Nonbiased biometric data provide a means to measure the amount of stress being imposed on animals from humans, the environment, and other animals. The stress response in animals functions via glucocorticoid metabolism and is regulated by the hypothalamic-pituitary-adrenal axis. Fecal glucocorticoids, in particular, may be an extremely useful biometric test, since sample collection is noninvasive to subjects and, therefore, does not introduce other variables that may alter assay results. For this reason, many researchers and conservationists have begun to use fecal glucocorticoids as a means to measure stress in various animal species. This review article summarizes the literature on many studies in which fecal glucocorticoids and their metabolites have been used to assess stress levels in various mammalian species. Variations between studies are the main focus of this review. Collection methods, storage conditions, shipping procedures, and laboratory techniques utilized by different researchers are discussed. |
| Address |
Department of Biomedical Sciences and Pathobiology, Virginia-Maryland Regional College of Veterinary Medicine, Virginia Tech, 0442 Duck Pond Drive, Blacksburg, Virginia 24061, USA |
| Corporate Author |
|
Thesis |
|
| Publisher |
|
Place of Publication |
|
Editor |
|
| Language |
English |
Summary Language |
|
Original Title |
|
| Series Editor |
|
Series Title |
|
Abbreviated Series Title |
|
| Series Volume |
|
Series Issue |
|
Edition |
|
| ISSN |
1042-7260 |
ISBN |
|
Medium |
|
| Area |
|
Expedition |
|
Conference |
|
| Notes |
PMID:17319120 |
Approved |
no |
| Call Number |
refbase @ user @ |
Serial |
616 |
| Permanent link to this record |
| |
|
| |
| Author |
Dyer, F.C. |
| Title |
Animal behaviour: when it pays to waggle |
Type |
|
| Year |
2002 |
Publication |
Nature |
Abbreviated Journal |
Nature |
| Volume |
419 |
Issue |
6910 |
Pages |
885-886 |
| Keywords |
*Animal Communication; Animals; Bees/*physiology; California; Dancing/physiology; Environment; Evolution; Female; Flowers/chemistry; *Food; Gravitation; Lighting; Motor Activity/*physiology; Odors; Seasons; Sunlight |
| Abstract |
|
| Address |
|
| Corporate Author |
|
Thesis |
|
| Publisher |
|
Place of Publication |
|
Editor |
|
| Language |
English |
Summary Language |
|
Original Title |
|
| Series Editor |
|
Series Title |
|
Abbreviated Series Title |
|
| Series Volume |
|
Series Issue |
|
Edition |
|
| ISSN |
0028-0836 |
ISBN |
|
Medium |
|
| Area |
|
Expedition |
|
Conference |
|
| Notes |
PMID:12410290 |
Approved |
no |
| Call Number |
refbase @ user @ |
Serial |
769 |
| Permanent link to this record |
| |
|
| |
| Author |
McCutcheon, L.J.; Geor, R.J. |
| Title |
Influence of training on sweating responses during submaximal exercise in horses |
Type |
Journal Article |
| Year |
2000 |
Publication |
Journal of Applied Physiology (Bethesda, Md. : 1985) |
Abbreviated Journal |
J Appl Physiol |
| Volume |
89 |
Issue |
6 |
Pages |
2463-2471 |
| Keywords |
Animals; Body Fluids/metabolism; Body Temperature; Body Weight; Environment; Female; Horses/*physiology; Ions; Male; Motor Activity/*physiology; Oxygen Consumption; Physical Conditioning, Animal/*physiology; Sweat/chemistry; Sweating/*physiology; Time Factors |
| Abstract |
Sweating responses were examined in five horses during a standardized exercise test (SET) in hot conditions (32-34 degrees C, 45-55% relative humidity) during 8 wk of exercise training (5 days/wk) in moderate conditions (19-21 degrees C, 45-55% relative humidity). SETs consisting of 7 km at 50% maximal O(2) consumption, determined 1 wk before training day (TD) 0, were completed on a treadmill set at a 6 degrees incline on TD0, 14, 28, 42, and 56. Mean maximal O(2) consumption, measured 2 days before each SET, increased 19% [TD0 to 42: 135 +/- 5 (SE) to 161 +/- 4 ml. kg(-1). min(-1)]. Peak sweating rate (SR) during exercise increased on TD14, 28, 42, and 56 compared with TD0, whereas SRs and sweat losses in recovery decreased by TD28. By TD56, end-exercise rectal and pulmonary artery temperature decreased by 0.9 +/- 0.1 and 1.2 +/- 0.1 degrees C, respectively, and mean change in body mass during the SET decreased by 23% (TD0: 10.1 +/- 0.9; TD56: 7.7 +/- 0.3 kg). Sweat Na(+) concentration during exercise decreased, whereas sweat K(+) concentration increased, and values for Cl(-) concentration in sweat were unchanged. Moderate-intensity training in cool conditions resulted in a 1.6-fold increase in sweating sensitivity evident by 4 wk and a 0.7 +/- 0.1 degrees C decrease in sweating threshold after 8 wk during exercise in hot, dry conditions. Altered sweating responses contributed to improved heat dissipation during exercise and a lower end-exercise core temperature. Despite higher SRs for a given core temperature during exercise, decreases in recovery SRs result in an overall reduction in sweat fluid losses but no change in total sweat ion losses after training. |
| Address |
Department of Pathobiology, Ontario Veterinary College, University of Guelph, Guelph, Ontario, Canada N1G 2W1. jmccutch@uoguelph.ca |
| Corporate Author |
|
Thesis |
|
| Publisher |
|
Place of Publication |
|
Editor |
|
| Language |
English |
Summary Language |
|
Original Title |
|
| Series Editor |
|
Series Title |
|
Abbreviated Series Title |
|
| Series Volume |
|
Series Issue |
|
Edition |
|
| ISSN |
8750-7587 |
ISBN |
|
Medium |
|
| Area |
|
Expedition |
|
Conference |
|
| Notes |
PMID:11090603 |
Approved |
no |
| Call Number |
refbase @ user @ |
Serial |
1922 |
| Permanent link to this record |
| |
|
| |
| Author |
Pierce, M.M.; Nall, B.T. |
| Title |
Coupled kinetic traps in cytochrome c folding: His-heme misligation and proline isomerization |
Type |
Journal Article |
| Year |
2000 |
Publication |
Journal of Molecular Biology |
Abbreviated Journal |
J Mol Biol |
| Volume |
298 |
Issue |
5 |
Pages |
955-969 |
| Keywords |
Amino Acid Sequence; Amino Acid Substitution/genetics; Binding Sites; Cytochrome c Group/*chemistry/genetics/*metabolism; *Cytochromes c; Enzyme Stability/drug effects; Fluorescence; Guanidine/pharmacology; Heme/*metabolism; Histidine/genetics/*metabolism; Hydrogen-Ion Concentration; Isomerism; Kinetics; Models, Molecular; Molecular Sequence Data; Mutation/genetics; Proline/*chemistry/metabolism; Protein Conformation/drug effects; Protein Denaturation/drug effects; *Protein Folding; Protein Renaturation; Saccharomyces cerevisiae/enzymology/genetics; Sequence Alignment; Thermodynamics |
| Abstract |
The effect of His-heme misligation on folding has been investigated for a triple mutant of yeast iso-2 cytochrome c (N26H,H33N,H39K iso-2). The variant contains a single misligating His residue at position 26, a location at which His residues are found in several cytochrome c homologues, including horse, tuna, and yeast iso-1. The amplitude for fast phase folding exhibits a strong initial pH dependence. For GdnHCl unfolded protein at an initial pH<5, the observed refolding at final pH 6 is dominated by a fast phase (tau(2f)=20 ms, alpha(2f)=90 %) that represents folding in the absence of misligation. For unfolded protein at initial pH 6, folding at final pH 6 occurs in a fast phase of reduced amplitude (alpha(2f) approximately 20 %) but the same rate (tau(2f)=20 ms), and in two slower phases (tau(m)=6-8 seconds, alpha(m) approximately 45 %; and tau(1b)=16-20 seconds, alpha(1b) approximately 35 %). Double jump experiments show that the initial pH dependence of the folding amplitudes results from a slow pH-dependent equilibrium between fast and slow folding species present in the unfolded protein. The slow equilibrium arises from coupling of the His protonation equilibrium to His-heme misligation and proline isomerization. Specifically, Pro25 is predominantly in trans in the unligated low-pH unfolded protein, but is constrained in a non-native cis isomerization state by His26-heme misligation near neutral pH. Refolding from the misligated unfolded form proceeds slowly due to the large energetic barrier required for proline isomerization and displacement of the misligated His26-heme ligand. |
| Address |
Center for Biomolecular Structure, Department of Biochemistry, University of Texas Health Science Center, 7703 Floyd Curl Drive, San Antonio, TX 78229-3900, USA |
| Corporate Author |
|
Thesis |
|
| Publisher |
|
Place of Publication |
|
Editor |
|
| Language |
English |
Summary Language |
|
Original Title |
|
| Series Editor |
|
Series Title |
|
Abbreviated Series Title |
|
| Series Volume |
|
Series Issue |
|
Edition |
|
| ISSN |
0022-2836 |
ISBN |
|
Medium |
|
| Area |
|
Expedition |
|
Conference |
|
| Notes |
PMID:10801361 |
Approved |
no |
| Call Number |
refbase @ user @ |
Serial |
3853 |
| Permanent link to this record |
