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Author |
Birch, H.L.; Bailey, A.J.; Goodship, A.E. |
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Title |
Macroscopic 'degeneration' of equine superficial digital flexor tendon is accompanied by a change in extracellular matrix composition |
Type  |
Journal Article |
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Year |
1998 |
Publication |
Equine Veterinary Journal |
Abbreviated Journal |
Equine Vet J |
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Volume |
30 |
Issue |
6 |
Pages |
534-539 |
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Keywords |
Animals; Collagen/analysis; DNA/analysis; Extracellular Matrix/*chemistry; Glycosaminoglycans/analysis; Horses/injuries/*physiology; Immunohistochemistry; Rupture/veterinary; Tendon Injuries/metabolism/pathology/veterinary; Tendons/chemistry/*pathology; Water/analysis |
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Abstract |
Injuries to the superficial digital flexor tendon are common in horses required to gallop and jump at speed. Partial rupture of this tendon usually occurs in the central core of the midmetacarpal region and may be preceded by localised degenerative changes. Post mortem examination of apparently normal equine flexor tendons has revealed an abnormal macroscopic appearance in the central core, characterised by a reddish discolouration. We have previously shown that there is also physical damage to the collagen fibres. In the present study we tested the hypothesis that the abnormal appearance is accompanied by changes in the composition of the extracellular matrix of the tendon. Biochemical analysis of the extracellular matrix demonstrated an increase in total sulphated glycosaminoglycan content, increase in the proportion of type III collagen and decrease in collagen linked fluorescence in the central core of 'degenerated' tendons relative to tissue from the peripheral region of the same tendon. Dry matter content and total collagen content were not significantly different between tendon zones or normal and 'degenerated' tendons. These changes suggest a change in cell metabolism and matrix turnover in the central core of the tendon and are likely to contribute to a decrease in mechanical properties in this part of the tendon, predisposing to the characteristic partial rupture of the tendon. |
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Veterinary Basic Sciences, Royal Veterinary College, North Mymms, Hatfield, UK |
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0425-1644 |
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PMID:9844973 |
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Call Number |
Equine Behaviour @ team @ |
Serial |
3794 |
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Author |
Gilmanshin, R.; Callender, R.H.; Dyer, R.B. |
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Title |
The core of apomyoglobin E-form folds at the diffusion limit |
Type |
Journal Article |
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Year |
1998 |
Publication |
Nature Structural Biology |
Abbreviated Journal |
Nat Struct Biol |
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Volume |
5 |
Issue |
5 |
Pages |
363-365 |
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Keywords |
Animals; Apoproteins/*chemistry; Diffusion; Horses; Myoglobin/*chemistry; *Protein Folding; Spectroscopy, Fourier Transform Infrared; Temperature |
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Abstract |
The E-form of apomyoglobin has been characterized using infrared and fluorescence spectroscopies, revealing a compact core with native like contacts, most probably consisting of 15-20 residues of the A, G and H helices of apomyoglobin. Fast temperature-jump, time-resolved infrared measurements reveal that the core is formed within 96 micros at 46 degrees C, close to the diffusion limit for loop formation. Remarkably, the folding pathway of the E-form is such that the formation of a limited number of native-like contacts is not rate limiting, or that the contacts form on the same time scale expected for diffusion controlled loop formation. |
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1072-8368 |
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PMID:9586997 |
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Call Number |
Equine Behaviour @ team @ |
Serial |
3795 |
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Author |
Ballew, R.M.; Sabelko, J.; Gruebele, M. |
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Title |
Direct observation of fast protein folding: the initial collapse of apomyoglobin |
Type |
Journal Article |
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Year |
1996 |
Publication |
Proceedings of the National Academy of Sciences of the United States of America |
Abbreviated Journal |
Proc. Natl. Acad. Sci. U.S.A. |
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Volume |
93 |
Issue |
12 |
Pages |
5759-5764 |
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Keywords |
Animals; Apoproteins/*chemistry; Circular Dichroism; Horses; Kinetics; Muscle, Skeletal/chemistry; Myoglobin/*chemistry; *Protein Folding; Spectrometry, Fluorescence; Spectrophotometry, Infrared; Temperature |
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Abstract |
The rapid refolding dynamics of apomyoglobin are followed by a new temperature-jump fluorescence technique on a 15-ns to 0.5-ms time scale in vitro. The apparatus measures the protein-folding history in a single sweep in standard aqueous buffers. The earliest steps during folding to a compact state are observed and are complete in under 20 micros. Experiments on mutants and consideration of steady-state CD and fluorescence spectra indicate that the observed microsecond phase monitors assembly of an A x (H x G) helix subunit. Measurements at different viscosities indicate diffusive behavior even at low viscosities, in agreement with motions of a solvent-exposed protein during the initial collapse. |
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Address |
School of Chemical Sciences and Beckman Institute for Advanced Science and Technology, University of Illinois, Urbana, 61801, USA |
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English |
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ISSN |
0027-8424 |
ISBN |
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Notes |
PMID:8650166 |
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no |
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Call Number |
Equine Behaviour @ team @ |
Serial |
3798 |
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Author |
Chiba, K.; Ikai, A.; Kawamura-Konishi, Y.; Kihara, H. |
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Title |
Kinetic study on myoglobin refolding monitored by five optical probe stopped-flow methods |
Type |
Journal Article |
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Year |
1994 |
Publication |
Proteins |
Abbreviated Journal |
Proteins |
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Volume |
19 |
Issue |
2 |
Pages |
110-119 |
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Keywords |
Animals; Chromatography, Gel; Circular Dichroism; Horses; Kinetics; Metmyoglobin/analogs & derivatives/chemistry; Myoglobin/*chemistry; *Protein Folding; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet; Urea |
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Abstract |
The refolding kinetics of horse cyanometmyoglobin induced by concentration jump of urea was investigated by five optical probe stopped-flow methods: absorption at 422 nm, tryptophyl fluorescence at around 340 nm, circular dichroism (CD) at 222 nm, CD at 260 nm, and CD at 422 nm. In the refolding process, we detected three phases with rate constants of > 1 x 10(2) s-1, (4.5-9.3) s-1, and (2-5) x 10(-3) s-1. In the fastest phase, a substantial amount of secondary structure (approximately 40%) is formed within the dead time of the CD stopped-flow apparatus (10.7 ms). The kinetic intermediate populated in the fastest phase is shown to capture a hemindicyanide, suggesting that a “heme pocket precursor” recognized by hemindicyanide must be constructed within the dead time. In the middle phase, most of secondary and tertiary structures, especially around the captured hemindicyanide, have been constructed. In the slowest phase, we detected a minor structural rearrangement accompanying the ligand-exchange reaction in the fifth coordination of ferric iron. We present a possible model for the refolding process of myoglobin in the presence of the heme group. |
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Laboratory of Biodynamics, Faculty of Bioscience and Biotechnology, Tokyo Institute of Technology, Kanagawa, Japan |
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English |
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Series Volume |
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Series Issue |
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Edition |
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ISSN |
0887-3585 |
ISBN |
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Notes |
PMID:8090705 |
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no |
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Call Number |
Equine Behaviour @ team @ |
Serial |
3799 |
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Author |
Steinhoff, H.J.; Schrader, J.; Schlitter, J. |
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Title |
Temperature-jump studies and polarized absorption spectroscopy of methemoglobin-thiocyanate single crystals |
Type |
Journal Article |
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Year |
1992 |
Publication |
Biochimica et Biophysica Acta |
Abbreviated Journal |
Biochim Biophys Acta |
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Volume |
1121 |
Issue |
3 |
Pages |
269-278 |
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Keywords |
Animals; Crystallization; Horses; Kinetics; Methemoglobin/*chemistry; Solutions; Spectrum Analysis; Temperature; Thiocyanates/*chemistry |
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Abstract |
Association equilibria and association kinetics of the thiocyanate binding reaction to methemoglobin in single crystals and solution are studied using temperature-jump technique and polarized absorption spectroscopy. Different kinetic constants are found for the reaction in solution and crystal phase for the alpha- and beta-subunits of the methemoglobin tetramer. The reduction of the reactivity of the alpha- and beta-subunits in crystalline phase is 6-fold and 2.4-fold, respectively, compared to the values found in solution. The intramolecular binding reaction of the N epsilon of the distal histidine E7 which is observed in methemoglobin in solution cannot be detected in single crystals. Our results suggest that crystallization of hemoglobin has little influence on small-scale structural fluctuations which are necessary for ligands to get to the binding sites and large-scale structural motions are suppressed. |
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Address |
Institut fur Biophysik, Ruhr-Universitat Bochum, Germany |
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English |
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ISSN |
0006-3002 |
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Notes |
PMID:1627604 |
Approved |
no |
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Call Number |
Equine Behaviour @ team @ |
Serial |
3800 |
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Author |
Steinhoff, H.J. |
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Title |
A continuous wave laser T-jump apparatus and its application to chemical reactions in hemoglobin single crystals |
Type |
Journal Article |
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Year |
1988 |
Publication |
Journal of Biochemical and Biophysical Methods |
Abbreviated Journal |
J Biochem Biophys Methods |
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Volume |
15 |
Issue |
6 |
Pages |
319-330 |
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Keywords |
Animals; Chemistry; Crystallization; *Heat; *Hemoglobins; Horses/blood; *Lasers; Methemoglobin; Solutions; Thermodynamics; Thiocyanates |
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Abstract |
A laser temperature jump apparatus is constructed where the T-jump is achieved by means of the direct absorption of continuous laser radiation of low intensity by a solid sample. The final temperature in the irradiated volume element is reached when the absorbed radiation power equals the dissipation of heat by heat conduction. The time range from the beginning of irradiation to the stationary state depends on the geometry of the irradiated volume element and is less than 10 ms. The heating laser beam is simultaneously used to detect the relaxation to the new chemical equilibrium in the sample. Relaxation processes with relaxation rates between 10(2) s-1 and less than 10(-3) s-1 on samples with volumes less than 10(-3) mm3 may be investigated using this T-jump method. One application of this method is the determination of reaction rates of ligand reactions in hemoglobin single crystals. Rate constants obtained for the reaction of thiocyanate with crystallized horse methemoglobin are presented. |
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Address |
Institut fur Biophysik, Ruhr-Universitat Bochum, F.R.G |
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English |
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ISSN |
0165-022X |
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Notes |
PMID:3379245 |
Approved |
no |
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Call Number |
Equine Behaviour @ team @ |
Serial |
3804 |
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Author |
Pierce, M.M.; Nall, B.T. |
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Title |
Coupled kinetic traps in cytochrome c folding: His-heme misligation and proline isomerization |
Type |
Journal Article |
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Year |
2000 |
Publication |
Journal of Molecular Biology |
Abbreviated Journal |
J Mol Biol |
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Volume |
298 |
Issue |
5 |
Pages |
955-969 |
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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 |
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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. |
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Address |
Center for Biomolecular Structure, Department of Biochemistry, University of Texas Health Science Center, 7703 Floyd Curl Drive, San Antonio, TX 78229-3900, USA |
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English |
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ISSN |
0022-2836 |
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Notes |
PMID:10801361 |
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no |
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Call Number |
refbase @ user @ |
Serial |
3853 |
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Author |
Elsaesser, F.; Klobasa, F.; Ellendorff, F. |
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Title |
ACTH stimulation test for the determination of salivary cortisol and of cortisol responses as markers of the training status/fitness of warm-blooded sports horses] |
Type |
Journal Article |
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Year |
2001 |
Publication |
DTW. Deutsche Tierarztliche Wochenschrift |
Abbreviated Journal |
Dtsch Tierarztl Wochenschr |
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Volume |
108 |
Issue |
1 |
Pages |
31-36 |
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Keywords |
Adrenocorticotropic Hormone/*diagnostic use; Animals; Health; Horses/*physiology; Hydrocortisone/*analysis/*secretion; Male; Orchiectomy; *Physical Conditioning, Animal; Running; Saliva/*chemistry; Walking |
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Abstract |
Previous work (Marc et al., 2000) suggested that plasma cortisol responses to treadmill exercise or ACTH injection are a reliable marker for performance evaluation in warmblood horses. For practical purposes blood sample collections and treadmill exercise tests are somewhat troublesome and time consuming. The goal of this study was thus to evaluate the use of saliva for cortisol determination (by direct EIA) as a marker for performance and to investigate the reliability and repeatability of plasma cortisol responses to a single i.v. injection of ACTH (50 micrograms or 250 micrograms). Furthermore, the effect of training horses for 8 weeks 3 times per week covering the same distance (increasing from 3.5 km during the first week to 8 km during the last week) either by trotting (approximately 240 m/min) or by cantering (375 m/min) was investigated. For this purpose initially ten four-year-old Hannovarian geldings, all reared in the same State stud, were used. Mean overall correlation between salivary cortisol and plasma cortisol concentrations was 0.64 when samples of various points of time were used. However, in spite of attempts to standardize saliva sample collection, correlation between salivary cortisol levels and plasma cortisol levels at distinct points of time in different tests were low and significant (r = 0.85, p < 0.02) only in one test. Thus, salivary cortisol measurements for diagnostic purposes are not reliable or useful. The repeatability of plasma cortisol responses to ACTH for untrained and trained horses were r = 0.86 and r = 0.8 respectively (p < or = 0.01 and p < or = 0.05 respectively). Training horses either by trotting or cantering did not affect the cortisol response either to treadmill exercise or to stimulation by ACTH. It is concluded that the relationship between salivary cortisol levels and plasma cortisol levels is not close enough to allow the use of salivary cortisol determination as marker of the training status/fitness of horses. The repeatability of the cortisol response to ACTH is similar to the cortisol response to treadmill exercise. Based on plasma cortisol responses to ACTH or treadmill exercise training horses by cantering at low speed is not superior to training by trotting for the fitness of horses. |
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Address |
Institut fur Tierzucht und Tierverhalten Mariensee (FAL), Holtystrasse 10, 31535 Neustadt. elsaesser@tzv.fal.de |
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German |
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Original Title |
ACTH Stimulationstest und Bestimmung von Cortisol im Blut und Speichel zur Bewertung des Trainingszustands/der Kondition beim Warmblutpferd |
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Abbreviated Series Title |
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Edition |
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ISSN |
0341-6593 |
ISBN |
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Notes |
PMID:11232423 |
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no |
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Call Number |
Equine Behaviour @ team @ |
Serial |
4053 |
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Author |
Carroll, J.; Murphy, C.J.; Neitz, M.; Hoeve, J.N.; Neitz, J. |
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Title |
Photopigment basis for dichromatic color vision in the horse |
Type |
Journal Article |
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Year |
2001 |
Publication |
Journal of Vision |
Abbreviated Journal |
J Vis |
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Volume |
1 |
Issue |
2 |
Pages |
80-87 |
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Keywords |
Adaptation, Physiological; Animals; Color Perception/*physiology; Cones (Retina)/chemistry/*physiology; Electroretinography; Horses/*physiology; Photic Stimulation; Phototransduction/physiology; Retinal Pigments/analysis/*physiology; Visual Perception/physiology |
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Abstract |
Horses, like other ungulates, are active in the day, at dusk, dawn, and night; and, they have eyes designed to have both high sensitivity for vision in dim light and good visual acuity under higher light levels (Walls, 1942). Typically, daytime activity is associated with the presence of multiple cone classes and color-vision capacity (Jacobs, 1993). Previous studies in other ungulates, such as pigs, goats, cows, sheep and deer, have shown that they have two spectrally different cone types, and hence, at least the photopigment basis for dichromatic color vision (Neitz & Jacobs, 1989; Jacobs, Deegan II, Neitz, Murphy, Miller, & Marchinton, 1994; Jacobs, Deegan II, & Neitz, 1998). Here, electroretinogram flicker photometry was used to measure the spectral sensitivities of the cones in the domestic horse (Equus caballus). Two distinct spectral mechanisms were identified and are consistent with the presence of a short-wavelength-sensitive (S) and a middle-to-long-wavelength-sensitive (M/L) cone. The spectral sensitivity of the S cone was estimated to have a peak of 428 nm, while the M/L cone had a peak of 539 nm. These two cone types would provide the basis for dichromatic color vision consistent with recent results from behavioral testing of horses (Macuda & Timney, 1999; Macuda & Timney, 2000; Timney & Macuda, 2001). The spectral peak of the M/L cone photopigment measured here, in vivo, is similar to that obtained when the gene was sequenced, cloned, and expressed in vitro (Yokoyama & Radlwimmer, 1999). Of the ungulates that have been studied to date, all have the photopigment basis for dichromatic color vision; however, they differ considerably from one another in the spectral tuning of their cone pigments. These differences may represent adaptations to the different visual requirements of different species. |
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Address |
Department of Cell Biology, Neurobiology & Anatomy, Medical College of Wisconsin, Milwaukee, WI, USA |
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English |
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Abbreviated Series Title |
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Series Volume |
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Series Issue |
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Edition |
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ISSN |
1534-7362 |
ISBN |
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Notes |
PMID:12678603 |
Approved |
no |
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Call Number |
Equine Behaviour @ team @ |
Serial |
4060 |
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Author |
Yokoyama, S.; Radlwimmer, F.B. |
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Title |
The molecular genetics of red and green color vision in mammals |
Type |
Journal Article |
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Year |
1999 |
Publication |
Genetics |
Abbreviated Journal |
Genetics |
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Volume |
153 |
Issue |
2 |
Pages |
919-932 |
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Keywords |
Amino Acid Sequence; Animals; Base Sequence; COS Cells; Cats; Color Perception/*genetics; DNA Primers; Deer; Dolphins; *Evolution, Molecular; Goats; Guinea Pigs; Horses; Humans; Mammals/*genetics/physiology; Mice; Molecular Sequence Data; Opsin/biosynthesis/chemistry/*genetics; *Phylogeny; Rabbits; Rats; Recombinant Proteins/biosynthesis; Reverse Transcriptase Polymerase Chain Reaction; Sciuridae; Sequence Alignment; Sequence Homology, Amino Acid; Transfection |
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Abstract |
To elucidate the molecular mechanisms of red-green color vision in mammals, we have cloned and sequenced the red and green opsin cDNAs of cat (Felis catus), horse (Equus caballus), gray squirrel (Sciurus carolinensis), white-tailed deer (Odocoileus virginianus), and guinea pig (Cavia porcellus). These opsins were expressed in COS1 cells and reconstituted with 11-cis-retinal. The purified visual pigments of the cat, horse, squirrel, deer, and guinea pig have lambdamax values at 553, 545, 532, 531, and 516 nm, respectively, which are precise to within +/-1 nm. We also regenerated the “true” red pigment of goldfish (Carassius auratus), which has a lambdamax value at 559 +/- 4 nm. Multiple linear regression analyses show that S180A, H197Y, Y277F, T285A, and A308S shift the lambdamax values of the red and green pigments in mammals toward blue by 7, 28, 7, 15, and 16 nm, respectively, and the reverse amino acid changes toward red by the same extents. The additive effects of these amino acid changes fully explain the red-green color vision in a wide range of mammalian species, goldfish, American chameleon (Anolis carolinensis), and pigeon (Columba livia). |
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Department of Biology, Syracuse University, Syracuse, New York 13244, USA. syokoyam@mailbox.syr.edu |
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English |
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0016-6731 |
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PMID:10511567 |
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Equine Behaviour @ team @ |
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4063 |
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