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At least 1,351 records · Page 75Linked to original sources
PubMed1999

Spectacle-mounted prisms as an aid in face-down positioning after vitrectomy surgery.

PURPOSE: To report a modification in the design of bed spectacles to provide an aid for patients who undergo face-down positioning after vitrectomy with gas-fluid exchange and postoperative gas tamponade. METHODS: New equipment design. Bed spectacles that use prisms to move the image 90 degrees around the horizontal meridian were modified by rotating the prisms in the frame 180 degrees and adding nosepads and cable temples. The spectacles were given to 12 patients for use during postoperative face-down positioning. A questionnaire was used to evaluate the helpfulness of the spectacles during face-down positioning. RESULTS: Patients ranked the spectacles as "helpful" to "very helpful" with a mean and SD of 8.3+/-1.6 on a scale of 1 to 10, where 1 was "a hindrance" and 10 was "very helpful." Patients wore the spectacles an average of 5.7+/-4.5 hours a day (range, 1.5 to 15 hours). CONCLUSION: Modified bed spectacles appear to be a portable aid to patients who undergo face-down positioning while sitting, standing, or prone.

Gases↗
PubMed1999

Photorefractive keratectomy after intrastromal corneal ring segment explantation.

PURPOSE: To describe a case of photorefractive keratectomy after removal of intrastromal corneal ring segments from the cornea. METHODS: During United States Food and Drug Administration Phase III Trials for intrastromal corneal ring segments (ICRS), the implanted segments were removed from the cornea of the right eye of a patient because of dissatisfaction with glare, halos, and fluctuating vision. Ten months after ICRS explantation, the-patient underwent a photorefractive keratectomy procedure to the same eye. RESULTS: One month after removal of the ICRS, the patient's manifest refraction was within +/- 0.50 diopters of his original manifest refraction. Photorefractive keratectomy was planned to the same eye 6 months later. At the first attempt, the epithelium could not be removed with the laser and scrape technique, and residual epithelium was noted at the vertical meridian (12 o'clock) corneal incision site, which had been used for ICRS surgery and explant; therefore, the procedure was aborted. At the second attempt, with a mechanical epithelial brush (AMOILS Epithelial Scrubber; Innova, Inc, Toronto, Canada), the epithelium was removed with ease. After this, photorefractive keratectomy was done without difficulty or complication. At his most recent 8-month postphotorefractive keratectomy examination, the patient had an uncorrected visual acuity of RE: 20/16, with a manifest refraction of -0.75 to 0.75 x 170 degrees, a faint haze at the site of the stromal channel, and a small scar at the incision site on slit-lamp examination. CONCLUSIONS: Intrastromal corneal ring segments can be readily removed from the cornea, if required. In this case, the refraction returned to its preoperative state soon after the explant procedure and remained stable over time. Photorefractive keratectomy was performed as a secondary refractive surgical procedure after the removal of ICRS without difficulty or complication. However, removal of the epithelium is probably best accomplished with the use of an epithelial brush, considering the changes in the epithelial adherence in a postsurgical cornea. Further studies are required to establish the safety and efficacy of secondary refractive surgical procedures after ICRS explantation.

Adult↗
PubMed2002

A new deformation model of hard alpha-keratin fibers at the nanometer scale: implications for hard alpha-keratin intermediate filament mechanical properties.

The mechanical behavior of human hair fibers is determined by the interactions between keratin proteins structured into microfibrils (hard alpha-keratin intermediate filaments), a protein sulfur-rich matrix (intermediate filaments associated proteins), and water molecules. The structure of the microfibril-matrix assembly has already been fully characterized using electron microscopy and small-angle x-ray scattering on unstressed fibers. However, these results give only a static image of this assembly. To observe and characterize the deformation of the microfibrils and of the matrix, we have carried out time-resolved small-angle x-ray microdiffraction experiments on human hair fibers stretched at 45% relative humidity and in water. Three structural parameters were monitored and quantified: the 6.7-nm meridian arc, which is related to an axial separation between groups of molecules along the microfibrils, the microfibril's radius, and the packing distance between microfibrils. Using a surface lattice model of the microfibril, we have described its deformation as a combination of a sliding process and a molecular stretching process. The radial contraction of the matrix is also emphasized, reinforcing the hydrophilic gel nature hypothesis.

Hair↗
PubMed2002

Structural features of cross-bridges in isometrically contracting skeletal muscle.

Two-dimensional x-ray diffraction was used to investigate structural features of cross-bridges that generate force in isometrically contracting skeletal muscle. Diffraction patterns were recorded from arrays of single, chemically skinned rabbit psoas muscle fibers during isometric force generation, under relaxation, and in rigor. In isometric contraction, a rather prominent intensification of the actin layer lines at 5.9 and 5.1 nm and of the first actin layer line at 37 nm was found compared with those under relaxing conditions. Surprisingly, during isometric contraction, the intensity profile of the 5.9-nm actin layer line was shifted toward the meridian, but the resulting intensity profile was different from that observed in rigor. We particularly addressed the question whether the differences seen between rigor and active contraction might be due to a rigor-like configuration of both myosin heads in the absence of nucleotide (rigor), whereas during active contraction only one head of each myosin molecule is in a rigor-like configuration and the second head is weakly bound. To investigate this question, we created different mixtures of weak binding myosin heads and rigor-like actomyosin complexes by titrating MgATPgammaS at saturating [Ca2+] into arrays of single muscle fibers. The resulting diffraction patterns were different in several respects from patterns recorded under isometric contraction, particularly in the intensity distribution along the 5.9-nm actin layer line. This result indicates that cross-bridges present during isometric force generation are not simply a mixture of weakly bound and single-headed rigor-like complexes but are rather distinctly different from the rigor-like cross-bridge. Experiments with myosin-S1 and truncated S1 (motor domain) support the idea that for a force generating cross-bridge, disorder due to elastic distortion might involve a larger part of the myosin head than for a nucleotide free, rigor cross-bridge.

Actins↗
PubMed1983

X-ray structure analysis of thin filaments of a molluscan smooth muscle in the living relaxed state.

In the small-angle x-ray diffraction pattern of the living relaxed anterior byssus retractor muscle of Mytilus edulis, the thin filaments showed the following features. The 59.8-A reflection was much stronger and a little farther from the meridian than the 51.9-A reflection, although they are both contributions of the first-order Bessel function and are comparable with each other in the height from the equator. The 381-A reflection, given by the second-order Bessel function, was weaker than the 59.8-A reflection by more than the difference between the peak values of the first- and second-order Bessel functions, and was not so distant radially from the latter as estimated from the amount of peak shift brought about by the alteration of the Bessel order. A model of the thin filament was made on the basis of inverse Fourier transformation of the scattering amplitude, and the above features were explained by the characteristic shape of actin shown in this model. The actin subunits are elongated along the genetic left-hand helix with a pitch of 59.8 A, and are bonded together along the genetic helix in the inner part of the filament.

Animals↗
PubMed1990

Diffraction diagnosis of protein folding in gap junction connexons.

To diagnose the regular polypeptide conformation in gap junction membranes, the x-ray intensities diffracted from oriented specimens have been separated into a modulated component due to the coherently ordered portion of the channel-forming pairs of connexon hexamers and a diffuse component due to the disordered parts. The spherically averaged ordered protein diffraction, in the resolution range 15-4 A, was compared with intensity curves calculated from the Fourier transforms of proteins representative of the major tertiary structural classes. From this comparison the alpha-helical content of the ordered portion of the connexon was estimated to be approximately 60%. Calculation of cylindrically averaged patterns for oriented distributions of alpha-helical and beta-sheet proteins demonstrated that the ratio of the modulated diffracted intensity near 5 A spacing on the meridian and 10 A spacing on the equator observed from the gap junctions can be accounted for by alpha-helical segments inclined relative to the connexon axis. Model dimers of connexonlike hexamers were constructed from alpha-helix bundle proteins to correlate features in the calculated diffraction patterns with the model parameters. On the basis of these correlations, the ordered gap junction diffraction data indicate that alpha-helical segments centered at 38 A from the midplane of the gap have a mean radial location approximately 24 A from the hexamer axis, and an axial projected length of approximately 35 A. Thus, these alpha-helical segments traverse the hydrocarbon core of the lipid bilayer, as expected for the four hydrophobic sequences of the connexin molecule.

Animals↗
PubMed1993

Structure of beta-crystallite assemblies formed by Alzheimer beta-amyloid protein analogues: analysis by x-ray diffraction.

To elucidate the relation between amyloid fibril formation in Alzheimer disease and the primary structure of the beta/A4 protein, which is the major component of the amyloid, we have been investigating the ability of peptides sharing sequences with beta/A4 to form fibrils in vitro. In previous studies we focused on the macroscopic morphology of the assemblies formed by synthetic peptides corresponding in sequence to different regions of this protein. In the present study we analyze the x-ray diffraction patterns obtained from these assemblies. All specimens showed wide angle reflections that could be indexed by an orthogonal lattice of beta-crystallites having unit cell dimensions a = 9.4 A, b = 7 A, and c = 10 A, where a refers to hydrogen bonding direction, b to polypeptide chain direction, and c to intersheet direction. Given the amino acid sequence of beta/A4 as NH2-DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIAT-COOH, we found that, based on their orientation and assembly, the analogues could be classified into three groups: Group A, residues 19-28, 13-28, 12-28, 11-28, 9-28, 1-28, 1-38, 1-40, 6-25, 11-25 and 34-42; Group B, residues 18-28, 17-28, and 15-28; and Group C, residues 22-35 and 26-33. For Groups A and C, the sharpest reflections were (h00), indicating that the assemblies were fibrillar, i.e., elongated in a single direction. Lateral alignment of the crystallites in Group A account for its cross-beta pattern, in which the hydrogen bonding (H-bonding) direction is the fiber (rotation) axis. By comparison, the beta-crystallites of Group C had no preferential orientation, thus giving circular scattering. For Group B, the sharpest reflections were (h0l) on the meridian, indicating that the assemblies were plate-like, i.e., extended in two directions. A series of equatorial Bragg reflections having a 40 A period indicated regular stacking of the plates, and the rotation axis was normal to the surface of the plates. Of the Group A peptides, the analogues 11-28 and 6-25 showed intensity maxima on the equator as well as on higher layer lines, indicating that the beta-crystallites are highly ordered relative to one another in the axial, H-bonding direction. This sampling of the layer lines by a larger period (60 A) suggests that the beta-crystallites are arrayed either in cylindrical or small restricted crystalline lattices. Consistent with its electron microscopic images, we modeled the structure as a tube with five or six f,-crystallites constituting the wall and with the individual crystallite, which either rotates freely or is restricted, made of five or fewer beta-pleated sheets. For the Group B peptides, the electron density projection along the b-axis was calculated from the observed intensities using phase combinations from fl-keratin.Amino acid side-chain positions were apparent and, when refined as 4-A-diameter spheres, led to a substantial decrease in the R-factors.For peptide 18-28 the electron density peaks, which are thought to correspond to side chains, were centered 3.3 A from the peptide backbone, whereas for peptides 17-28 and 15-28, these peaks were centered 1 A or more further from the backbone. Peaks having high electron density faced peaks having lower density, suggesting a favorable stereochemical arrangement of the residues. Thus, our analysis of the fiber x-ray patterns from beta/A4 peptides shows the organization of the beta-crystallites that form the wall of the amyloid fibrils as well as possible side-chain interactions.

Amino Acid Sequence↗
PubMed1995

Identification of source of oscillations in apparent sarcomere length measured by laser diffraction.

The most widely used technique for dynamic estimates of sarcomere length in muscle is laser light diffraction. We have identified conditions under which artifactual oscillations can arise in apparent sarcomere length measured by this technique and report methods to reduce the effect. Altringham et al. (1984) first reported that the diffraction angle can exhibit one cycle of oscillation for each sarcomere length displacement of the illuminated portion of the fiber. We find that the amplitude of similar oscillations is strongly dependent on the intensity of light scattered from objects near the fiber and on the spacing between fiber and scatterer. The oscillations can be eliminated by minimizing scattered light and positioning the fiber a few millimeters from sources of scattering. A theoretical description shows that oscillations of this kind are expected from interference of scattered and diffracted light. Interference fringes were observed along the meridian of the pattern, and these moved during translation of either a fiber or a grating. The movement of fringes across the diffraction order shifts the centroid back and forth and, when associated with steady shortening, can give rise to "steps" and "pauses" in apparent striation spacing.

Animals↗
PubMed1996

Structure and periodicities of cross-bridges in relaxation, in rigor, and during contractions initiated by photolysis of caged Ca2+.

Ultra-rapid freezing and electron microscopy were used to directly observe structural details of frog muscle fibers in rigor, in relaxation, and during force development initiated by laser photolysis of DM-nitrophen (a caged Ca2+). Longitudinal sections from relaxed fibers show helical tracks of the myosin heads on the surface of the thick filaments. Fibers frozen at approximately 13, approximately 34, and approximately 220 ms after activation from the relaxed state by photorelease of Ca2+ all show surprisingly similar cross-bridge dispositions. In sections along the 1,1 lattice plane of activated fibers, individual cross-bridge densities have a wide range of shapes and angles, perpendicular to the fiber axis or pointing toward or away from the Z line. This highly variable distribution is established very early during development of contraction. Cross-bridge density across the interfilament space is more uniform than in rigor, wherein the cross-bridges are more dense near the thin filaments. Optical diffraction (OD) patterns and computed power density spectra of the electron micrographs were used to analyze periodicities of structures within the overlap regions of the sarcomeres. Most aspects of these patterns are consistent with time resolved x-ray diffraction data from the corresponding states of intact muscle, but some features are different, presumably reflecting different origins of contrast between the two methods and possible alterations in the structure of the electron microscopy samples during processing. In relaxed fibers, OD patterns show strong meridional spots and layer lines up to the sixth order of the 43-nm myosin repeat, indicating preservation and resolution of periodic structures smaller than 10 nm. In rigor, layer lines at 18, 24, and 36 nm indicate cross-bridge attachment along the thin filament helix. After activation by photorelease of Ca2+, the 14.3-nm meridional spot is present, but the second-order meridional spot (22 nm) disappears. The myosin 43-nm layer line becomes less intense, and higher orders of 43-nm layer lines disappear. A 36-nm layer line is apparent by 13 ms and becomes progressively stronger while moving laterally away from the meridian of the pattern at later times, indicating cross-bridges labeling the actin helix at decreasing radius.

Actins↗
PubMed1997

Temperature-induced structural changes in the myosin thick filament of skinned rabbit psoas muscle.

By using synchrotron radiation and an imaging plate for recording diffraction patterns, we have obtained high-resolution x-ray patterns from relaxed rabbit psoas muscle at temperatures ranging from 1 degree C to 30 degrees C. This allowed us to obtain intensity profiles of the first six myosin layer lines and apply a model-building approach for structural analysis. At temperatures 20 degrees C and higher, the layer lines are sharp with clearly defined maxima. Modeling based on the data obtained at 20 degrees C reveals that the average center of the cross-bridges is at 135 A from the center of the thick filament and both of the myosin heads appear to wrap around the backbone. At 10 degrees C and lower, the layer lines become very weak and diffuse scattering increases considerably. At 4 degrees C, the peak of the first layer line shifts toward the meridian from 0.0047 to 0.0038 A(-1) and decreases in intensity approximately by a factor of four compared to that at 20 degrees C, although the intensities of higher-order layer lines remain approximately 10-15% of the first layer line. Our modeling suggests that as the temperature is lowered from 20 degrees C to 4 degrees C the center of cross-bridges extends radially away from the center of the filament (135 A to 175 A). Furthermore, the fraction of helically ordered cross-bridges decreases at least by a factor of two, while the isotropic disorder (the temperature factor) remains approximately unchanged. Our results on the order/disordering effects of temperature are in general agreement with earlier results of Wray [Wray, J. 1987. Structure of relaxed myosin filaments in relation to nucleotide state in vertebrate skeletal muscle. J. Muscle Res. Cell Motil. 8:62a (Abstr.)] and Lowy et al. (Lowy, J., D. Popp, and A. A. Stewart. 1991. X-ray studies of order-disorder transitions in the myosin heads of skinned rabbit psoas muscles. Biophys. J. 60:812-824). and support Poulsen and Lowy's hypothesis of coexistence of ordered and disordered cross-bridge populations in muscle (Poulsen, F. R., and J. Lowy. 1983. Small angle scattering from myosin heads in relaxed and rigor frog skeletal muscle. Nature (Lond.). 303:146-152.). However, our results added new insights into the disordered population. Present modeling together with data analysis (Xu, S., S. Malinchik, Th. Kraft, B. Brenner, and L. C. Yu. 1997. X-ray diffraction studies of cross-bridges weakly bound to actin in relaxed skinned fibers of rabbit psoas muscle. Biophys. J. 73:000-000) indicate that in a relaxed muscle, cross-bridges are distributed in three populations: those that are ordered on the thick filament helix and those that are disordered; and within the disordered population, some cross-bridges are detached and some are weakly attached to actin. One critical conclusion of the present study is that the apparent order <--> disorder transition as a function of temperature is not due to an increase/decrease in thermal motion (temperature factor) for the entire population, but a redistribution of cross-bridges among the three populations. Changing the temperature leads to a change in the fraction of cross-bridges located on the helix, while changing the ionic strength at a given temperature affects the disordered population leading to a change in the relative fraction of cross-bridges detached from and weakly attached to actin. Since the redistribution is reversible, we suggest that there is an equilibrium among the three populations of cross-bridges.

Actin Cytoskeleton↗
PubMed1999

Structural changes in the actin-myosin cross-bridges associated with force generation induced by temperature jump in permeabilized frog muscle fibers.

Structural changes induced by Joule temperature jumps (T-jumps) in frog muscle fibers were monitored using time-resolved x-ray diffraction. Experiments made use of single, permeabilized fibers that were fully activated after slight cross-linking with 1-ethyl-3-[3-dimethylamino)propyl]carbodiimide to preserve their structural order. After T-jumps from 5-6 to approximately 17 degrees C and then on to approximately 30 degrees C, tension increased by a factor of 1.51 and 1.84, respectively, whereas fiber stiffness did not change with temperature. The tension rise was accompanied by a decrease in the intensity of the (1, 0) equatorial x-ray reflection by 15 and 26% (at approximately 17 and approximately 30 degrees C) and by an increase in the intensity of the M3 myosin reflection by 20% and 41%, respectively. The intensity of the (1,1) equatorial reflection increased slightly. The peak of the intensity on the 6th actin layer line shifted toward the meridian with temperature. The intensity of the 1st actin layer line increased from 12% (of its rigor value) at 5-6 degrees C to 36% at approximately 30 degrees C, so that the fraction of the cross-bridges labeling the actin helix estimated from this intensity increased proportionally to tension from approximately 35% at 5-6 degrees C to approximately 60% at approximately 30 degrees C. This suggests that force is generated during a transition of nonstereo-specifically attached myosin cross-bridges to a stereo-specific binding state.

Actomyosin↗
PubMed1999

Backward movements of cross-bridges by application of stretch and by binding of MgADP to skeletal muscle fibers in the rigor state as studied by x-ray diffraction.

The effects of the applied stretch and MgADP binding on the structure of the actomyosin cross-bridges in rabbit and/or frog skeletal muscle fibers in the rigor state have been investigated with improved resolution by x-ray diffraction using synchrotron radiation. The results showed a remarkable structural similarity between cross-bridge states induced by stretch and MgADP binding. The intensities of the 14.4- and 7.2-nm meridional reflections increased by approximately 23 and 47%, respectively, when 1 mM MgADP was added to the rigor rabbit muscle fibers in the presence of ATP-depletion backup system and an inhibitor for muscle adenylate kinase or by approximately 33 and 17%, respectively, when rigor frog muscle was stretched by approximately 4.5% of the initial muscle length. In addition, both MgADP binding and stretch induced a small but genuine intensity decrease in the region close to the meridian of the 5.9-nm layer line while retaining the intensity profile of its outer portion. No appreciable influence was observed in the intensities of the higher order meridional reflections of the 14.4-nm repeat and the other actin-based reflections as well as the equatorial reflections, indicating a lack of detachment of cross-bridges in both cases. The changes in the axial spacings of the actin-based and the 14.4-nm-based reflections were observed and associated with the tension change. These results indicate that stretch and ADP binding mediate similar structural changes, being in the correct direction to those expected for that the conformational changes are induced in the outer portion distant from the catalytic domain of attached cross-bridges. Modeling of conformational changes of the attached myosin head suggested a small but significant movement (about 10-20 degrees) in the light chain-binding domain of the head toward the M-line of the sarcomere. Both chemical (ADP binding) and mechanical (stretch) intervensions can reverse the contractile cycle by causing a backward movement of this domain of attached myosin heads in the rigor state.

Actomyosin↗
PubMed1999

Single vs. paired visual stimulation: superposition of early neuromagnetic responses and retinotopy in extrastriate cortex in humans.

Neuromagnetic techniques were used in conjunction with magnetic resonance imaging (MRI) techniques to: (1) localize and characterize cortical sources evoked by visual stimuli presented at different locations in the lower right visual field; (2) examine the superposition of cortical responses by comparing the summation of responses to the presentation of single stimuli with responses to paired stimuli; and (3) examine the spatial resolution of magnetoencephalographic (MEG) techniques by comparing the identified source locations evoked by the presentation of single vs. paired stimuli. Using multi-dipole, non-linear minimization analyses, three sources were localized for each stimulus condition during the initial 80-170 ms poststimulus interval for all subjects. In addition to an occipital source, two extrastriate sources were identified: occipital-parietal and occipital-temporal. Each source evidenced a systematic shift in location associated with changes in stimulus placement parallel to the vertical meridian. To our knowledge, this is the first demonstration of retinotopic organization of extrastriate areas, using non-invasive neuromagnetic techniques. The paired presentation of stimuli reflected superposition of the responses evoked by single stimuli but only for early activity up to 150 ms poststimulus. Undersummation was evident after 150 ms. All sources identified for single stimuli were also identified in the paired-stimulus responses; but at the expense of larger errors for some of the estimated parameters.

Evoked Potentials, Visual↗
PubMed2001

Vertical rectus muscle transposition and botulinum toxin for complete sixth nerve palsy.

BACKGROUND: Effective surgical treatment of complete unrecovered sixth nerve palsy must include the transfer of abducting power to the temporal aspect of the globe with release of medial rectus contracture nasally. We describe our experience in the treatment of five such patients who underwent full vertical rectus transposition combined with botulinum toxin chemodenervation of the ipsilateral medial rectus muscle. METHODS: The five patients all had primarily unilateral complete unrecovered sixth nerve palsy. They all underwent a complete preoperative and postoperative eye examination and an orthoptic assessment. Excursion into abduction was graded from -8 (globe immobilized in extreme adduction) to -4 (abduction as far as primary position) to 0 (full abduction). Abduction saccades and a forced muscle generation test confirmed the presence of complete unrecovered sixth nerve palsy, and forced duction testing measured the degree of medial rectus contracture. All patients received ipsilateral medial rectus injection of botulinum toxin in the preoperative (8 to 2 months before surgery) and perioperative periods, and underwent complete superior rectus-inferior rectus transposition temporally. RESULTS: The average length of follow-up was 21 (range 6 to 48) months. The average preoperative distance alignment was 52 (range 25 to 80) prism dioptres (PD). Vertical rectus transposition combined with botulinum toxin injection resulted in an average distance alignment change of 66 PD (range 50 PD to 82 PD) of exoshift. The average final deviation was 1 PD of esotropia (range 4 PD of esotropia to 6 PD of exotropia). Average abduction improved from -6 (range -3 to -8) preoperatively to -1.7 (range -1 to -2) postoperatively. Saccades averaged -4 preoperatively and improved to -2 postoperatively. Normal vertical eye movements were preserved in all patients. A total field of single binocular vision was created in all patients, which averaged 55 degrees (range 30 degrees to 75 degrees) in the horizontal meridian. The field of single binocular vision from primary position into abduction averaged 23 degrees (range 18 degrees to 28 degrees). INTERPRETATION: Temporal transposition of the vertical rectus muscles combined with perioperative botulinum toxin injection of the ipsilateral medial rectus muscle is a reliable and effective way of restoring functional binocular vision in patients with complete unrecovered sixth nerve palsy.

Abducens Nerve Diseases↗
PubMed2001

Spatial anisotropy of saccadic latency in normal subjects and brain-damaged patients.

In the present study, reaction time of oblique and orthogonal saccades was investigated in normal subjects and in two groups of patients with right (RBD) and left (LBD) vascular cerebral lesions and no signs of spatial neglect. Clear altitudinal effects were present in each group of subjects: saccadic latencies were longer in the lower than in the upper part of the visual field for both orthogonal and oblique saccades. Asymmetry along the horizontal meridian was present only in case of right hemisphere damage. This supports the view that a lesion in the right hemisphere causes a greater deficit of visual-spatial processing than a left hemisphere lesion. A cerebral lesion in the right and/or left hemisphere produces a general slowing in the saccadic latency and a general reduction in the accuracy of saccades with respect to normal subjects performance. Further, it seems that making saccades in oblique direction reduces the general saccade efficiency.

Adult↗
PubMed1991

Bilateral hemispheric control of foot distal movements: evidence from normal subjects.

Normal subjects have been tested for interhemispheric transfer (IT) of visuo-motor information using a simple reaction time (RT) paradigm and lateralized stimuli and responses (the so-called Poffenberger paradigm). In this paradigm IT time is assumed to correspond to the RT difference between crossed and uncrossed stimulus-response combinations (CUD). In Experiment 1, two types of movements were used: a unilateral flexion of the thumb and a unilateral plantar flexion of the big toe. A reliable CUD (7.4 msec) was found only with manual responses. Changing stimulus retinal eccentricity (10 degrees vs. 70 degrees) or attentional demands (blocked vs. random stimulus presentation) did not result in any reliable effect on the CUD. In Experiment 2 the number of RTs for each subject was considerably increased and several visual field sites (from areas close to the vertical meridian to the monocular crescent) were tested. Notwithstanding these modifications, this experiment confirmed the lack of CUD found for foot responses in Exp. 1. Taken together, these results are in keeping with a less lateralized hemispheric control of distal foot movements in comparison to hand movements.

Acoustic Stimulation↗
PubMed1987

The number, depth and elongation of disc incisures in the retinal rod of Rana catesbeiana.

The disc incisures in the bullfrog retinal rod were examined by electron microscopy. The number of disc incisures is proportional to the cross-sectional perimeter of the outer segment. While the diameter of the red rod outer segments varies with their location along the vertical meridian of the retina, the incisure number also changes similarly. It is estimated by regression analysis that a single disc lobule, bordered by two adjacent incisures, has on the average about 1 micron of arc-like rim edge. When red and green rod discs are compared at their middle outer segments in the ventro-central retina, the disc incisures are 1.8 times more numerous and 1.5 times deeper in the red rod (mean incisure number, 27; mean length, 2.7 microns) than in the green rod (15; 1.8 microns). These differences result in the total disc edge of the red rod (mean, 178 microns) being two times longer than that of the green rod (85 microns). The disc incisures emerge at the basal end of the outer segment and on the average become linearly longer toward the middle outer segment. During displacement of discs over the distance of 2.5 microns, which covers about 90 discs, the incisures reach more than 90% of their maximum length of 2.7 micron in the middle outer segment. In addition, the process of incisure elongation has a kind of fluctuation in that the incisure frequently shows a sharp decrease and increase in length accompanied by a change in course in the disc surface.

Animals↗
PubMed1987

Retinal morphology in rats treated with a taurine transport antagonist.

Previous studies have shown that chronic treatment of rats with guanidinoethyl sulfonate (GES), an antagonist of taurine uptake, leads to depletion of retinal taurine content and electroretinogram abnormalities. In this study we examined with the light- and electron microscope the retina and pigment epithelium of mother rats treated for 8 weeks with 1% GES in their drinking water. Pigment epithelial cells appeared swollen, sometimes with mitochondrial vacuolization and loss of cytoplasmic density, and changes in nuclear shape and chromatin distribution. Photoreceptor cells had shorter outer segments with disarray of disks, swollen inner segments and nuclei, and loss of synaptic terminal contents. These degenerative changes frequently led to cell death, indicated by loss of photoreceptor cell nuclei and shrinkage of the outer nuclear layer, and disappearance of photoreceptor synaptic terminals from the outer plexiform layer. Narrowing of the outer plexiform layer was due also to the retraction of cell processes from higher-order neurons. Quantitative studies of the retina along the vertical meridian passing through the optic nerve head showed that treatment resulted in significant reductions in the number of rod-cell nuclei per field, the width of the outer nuclear layer, and the width of the inner retina. Effects were more pronounced in the superior than the inferior hemisphere, reminiscent of findings in light-damage studies. A possible role for taurine in the cellular defence mechanisms against light- and oxygen-induced damage is suggested.

Animals↗