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Louise Glover

Publications and source records attributed to Louise Glover.

3 recordsLinked to original sources

Linguistic determinants of word colouring in grapheme-colour synaesthesia.

Previous studies of grapheme-colour synaesthesia have suggested that words tend to be coloured by their initial letter or initial vowel (e.g., Baron-Cohen et al., 1993; Ward et al., 2005). We examine this assumption in two ways. First, we show that letter position and syllable stress have been confounded, such that the initial letters of a word are often in stressed position (e.g., 'wo-man, 'ta-ble, 'ha-ppy). With participant JW, we separate these factors (e.g., with stress homographs such as 'con-vict vs. con-'vict) and show that the primary determinant of word colour is syllable stress, with only a secondary influence of letter position. We show that this effect derives from conceptual rather than perceptual stress, and that the effect is more prominent for synaesthetes whose words are coloured by vowels than by consonants. We examine, too, the time course of word colour generation. Slower colour naming occurs for spoken versus written stimuli, as we might expect from the additional requirement of grapheme conversion in the former. Reaction time data provide evidence, too, of incremental processing, since word colour is generated faster when the dominant grapheme is flagged early rather than late in the spoken word. Finally, we examine the role of non-dominant graphemes in word colouring and show faster colour naming when later graphemes match the dominant grapheme (e.g., ether) compared to when they do not (e.g., ethos). Taken together, our findings suggest that words are coloured incrementally by a process of competition between constituent graphemes, in which stressed graphemes and word-initial graphemes are disproportionately weighted.

Adult↗

Increased sensitivity of the ryanodine receptor to halothane-induced oligomerization in malignant hyperthermia-susceptible human skeletal muscle.

Mutations in the skeletal muscle RyR1 isoform of the ryanodine receptor (RyR) Ca2+-release channel confer susceptibility to malignant hyperthermia, which may be triggered by inhalational anesthetics such as halothane. Using immunoblotting, we show here that the ryanodine receptor, calmodulin, junctin, calsequestrin, sarcalumenin, calreticulin, annexin-VI, sarco(endo)plasmic reticulum Ca2+-ATPase, and the dihydropyridine receptor exhibit no major changes in their expression level between normal human skeletal muscle and biopsies from individuals susceptible to malignant hyperthermia. In contrast, protein gel-shift studies with halothane-treated sarcoplasmic reticulum vesicles from normal and susceptible specimens showed a clear difference. Although the alpha2-dihydropyridine receptor and calsequestrin were not affected, clustering of the Ca2+-ATPase was induced at comparable halothane concentrations. In the concentration range of 0.014-0.35 mM halothane, anesthetic-induced oligomerization of the RyR1 complex was observed at a lower threshold concentration in the sarcoplasmic reticulum from patients with malignant hyperthermia. Thus the previously described decreased Ca2+-loading ability of the sarcoplasmic reticulum from susceptible muscle fibers is probably not due to a modified expression of Ca2+-handling elements, but more likely a feature of altered quaternary receptor structure or modified functional dynamics within the Ca2+-regulatory apparatus. Possibly increased RyR1 complex formation, in conjunction with decreased Ca2+ uptake, is of central importance to the development of a metabolic crisis in malignant hyperthermia.

Anesthetics, Inhalation↗

Supramolecular calsequestrin complex.

As recently demonstrated by overlay assays using calsequestrin-peroxidase conjugates, the major 63 kDa Ca(2+)-binding protein of the sarcoplasmic reticulum forms complexes with itself, and with junctin (26 kDa), triadin (94 kDa) and the ryanodine receptor (560 kDa) [Glover, L., Culligan, K., Cala, S., Mulvey, C. & Ohlendieck, K. (2001) Biochim. Biophys. Acta1515, 120-132]. Here, we show that variations in the relative abundance of these four central elements of excitation-contraction coupling in different fiber types, and during chronic electrostimulation-induced fiber type transitions, are reflected by distinct alterations in the calsequestrin overlay binding patterns. Comparative immunoblotting with antibodies to markers of the junctional sarcoplasmic reticulum, in combination with the calsequestrin overlay binding patterns, confirmed a lower ryanodine receptor expression in slow soleus muscle compared to fast fibers, and revealed a drastic reduction of the RyR1 isoform in chronic low-frequency stimulated tibialis anterior muscle. The fast-to-slow transition process included a distinct reduction in fast calsequestrin and triadin and a concomitant reduction in calsequestrin binding to these sarcoplasmic reticulum elements. The calsequestrin-binding protein junctin was not affected by the muscle transformation process. The increase in calsequestrin and decrease in junctin expression during postnatal development resulted in similar changes in the intensity of binding of the calsequestrin conjugate to these sarcoplasmic reticulum components. Aged skeletal muscle fibers tended towards reduced protein interactions within the calsequestrin complex. This agrees with the physiological concept that the key regulators of Ca(2+) homeostasis exist in a supramolecular membrane assembly and that protein-protein interactions are affected by isoform shifting underlying the finely tuned adaptation of muscle fibers to changed functional demands.

Aging↗