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  • 1
    ISSN: 1365-2842
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: summary  This study was conducted to investigate the expression and distribution of c-Fos-like immunoreactive neurones (Fos-neurones), in the rat trigeminal sensory nuclear complex, produced by mechanical forces with various magnitudes and durations applied to the left upper first molar. The magnitudes of forces applied to the tooth were 25, 50 and 100 g and the duration was 2 h. A quantified force of 100 g was also applied to the upper molar for varying durations [short-time (1–2 min)], 2, 4, 8 and 12 h. Fos-neurones distributed in the bilateral superficial laminae of the subnucleus caudalis, and the ipsilateral dorsomedial part of subnucleus oralis (Sp5Odm). The number of Fos-neurones increased in the subnucleus caudalis (Sp5C) according to the force magnitude. In the Sp5C, the number of Fos-neurones exhibited maximum level, 2 or 4 h after the application. In the Sp5Odm, however, the number of Fos-neurones reached the maximum level at 8 h. These data suggest that the change in the number of nociceptive neurones in Sp5C reflect changes in encoding the magnitude of force to tooth, and that the nature of pain response to orthodontic forces might have some relation to the delayed expression of c-Fos protein in the Sp5Odm.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract  Our previous report identified 27- and 29-kDa calcium-binding proteins in porcine immature dental enamel. In this study we revealed that the N-terminal amino acid sequences of the two proteins were identical: LLANPXGXIPNLARGPAGRSRGPPG. The sequence matches a portion of the amino acid sequence of the porcine sheath protein, sheathlin. Porcine tooth germs were investigated immunochemically and immunohistochemically using specific antibodies raised against synthetic peptide that included residues 13–25 of this sequence. The affinity-purified antibodies reacted with several proteins extracted from newly formed immature enamel in immunochemical analyses, especially protein bands migrating at 62, 35–45, 29, and 27 kDa in SDS-polyacrylamide gels. The largest protein detected was a weak band near 70 kDa. In immunochemical analyses of proteins extracted from the inner (old) immature enamel, the antibody reacted faintly with the 27- and 29-kDa proteins. In immunohistochemical preparations, the Golgi apparatus and secretory granules of the secretory ameloblast, and the surface layer of immature enamel showed immunoreactivity. The immunoreactivity of immature enamel just beneath the secretory face of the Tomes’ process was intense. No immunoreactivity was found in the Golgi apparatus of the maturation ameloblast. These results suggest that the 70-kDa protein, whose degradation might be very fast, is the parent protein of the 27- and 29-kDa proteins.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1432-1106
    Keywords: Key words Motor nucleus ; EMG ; Muscle architecture ; Muscle fiber ; Caudofemoralis ; Cat
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract  Feline caudofemoralis (CF) is a promising preparation in which to study the properties of mammalian fast-twitch skeletal muscle, but little is known about its muscle fiber properties, architecture, and motor innervation. We used histochemical techniques to confirm that it contained predominantly type IIB fibers (95±2%, n=8, with six of eight muscles composed exclusively of type IIA and IIB fibers), but physiological experiments showed less fatiguability than for the type IIB component of medial gastrocnemius. This may be related to the surprisingly strong and regular recruitment of CF during repetitive tasks such as walking and trotting, which we demonstrated electromyographically. We measured muscle length over the anatomical range of motion for CF (∼0.6–1.2 L 0) and estimated working length during walking and trotting (∼0.95–1.15 L 0). The specific tension was similar to that of the exclusively slow-twitch soleus muscle (31.2±4.7 N/cm2 compared with 31.8±4.1 N/cm2; P〉0.8). Single fiber dissections of CF revealed a series-fibered architecture with a mean of 2.3 fibers, each 2.5 cm long, required to span the fascicle length. We identified two neuromuscular compartments in CF by cutting one of the two nerve branches innervating CF and depleting the glycogen stores in the intact motor units. These compartments were in parallel and extended the length of the muscle; their electromyographic activity was similar during various natural behaviors. CF and gluteus maximus motoneurons were labeled concurrently with a combination of fluorescent, retrograde tracers including Fluororuby, Fluorogold and Fast Blue. The CF motor nucleus was located in L7-S1, overlapping and intermingling extensively with the nucleus of the adjacent gluteus maximus muscle. Distributions of CF motoneuron diameter revealed one large peak around 50–55 µm, with relatively few small-diameter (less than 35 µm) cells. Using estimates of the total number of fibers in three muscles and the estimated number of α-motoneurons for those same muscles, we calculated a mean innervation ratio of ∼270, which is at the low end of the innervation ratios for type IIB motor units from other feline muscles and more similar to type IIA motor units. In general, CF appears to be a useful preparation in which to study the properties of fast-twitch muscle, but these properties may vary somewhat from type IIB fibers from different muscles.
    Type of Medium: Electronic Resource
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