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  • 1990-1994  (2)
  • 1960-1964
  • 1955-1959
  • Arrector pili muscle  (1)
  • Carp  (1)
  • 1
    ISSN: 1432-069X
    Keywords: Merkel cell ; Bulge ; Arrector pili muscle ; Nerve plexus ; Skin development
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The distribution of Merkel cells in human fetal hair follicles was studied using whole mounts of separated epidermis with attached hair follicles. The technique had the advantage of enabling the elucidation of the spatial relationships of Merkel cells with other cells in the skin. In a 16-week-old fetus the hair anlagen had formed one or two epithelial swellings of variable size. In a 17-week-old fetus sebaceous glands and the bulge of the hair follicle were recognizable and immunoreactive Merkel cells were present in the bulge and surrounding the acrotrichium (intraepidermal follicular canal). In a 20-week-old fetus the sebaceous gland and bulge were well formed and immunoreactive Merkel cells were concentrated in the bulge and infundibulum. In vertical sections of a 20-week-old fetus immunoreactive Merkel cells were also situated in the vicinity of the bulge. Arrector pili muscles were first observable in a 24-week-old fetus being weakly stained with anti-desmin antibody. In a 24-week-old fetus, nerves were also stained within the arrector pili muscles with S-100 protein antibody. In the presumptive arrector pili muscle immunoreactivity for S-100 protein developed before or at the same time as immunoreactivity for desmin. Merkel cells or their products in the bulge may serve as attractants for the growing arrector pili muscle which contain peripheral nerves. Following our report that dermal Merkel cells influence the formation of the dermal nerve plexus, perifollicular Merkel cells near the bulge may also play an inductive and growth-stimulative role for the perifollicular nerve plexus.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Journal of comparative physiology 160 (1990), S. 233-239 
    ISSN: 1432-136X
    Keywords: Temperature ; Acclimation ; Myosin ; Myosin heavy chain ; ATPase activity ; Carp
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Myosins were isolated from dorsal ordinary muscles of carp acclimated to 10°C and 30°C for a minimum of 5 weeks and examined for their ATPase activities. Ca2+-ATPase activity was different between myosins from cold-and warm-acclimated carp, especially at KCl concentrations ranging from 0.1 to 0.2 M, when measured at pH 7.0. The highest activity was 0.32 μmol Pi·min-1·mg-1 at 0.2 M KCl for cold-acclimated carp and 0.47 μmol Pi·min-1·mg-1 at 0.1 M KCl for warm-acclimated fish. The pH-dependency of Ca2+-ATPase activity at 0.5 M KCl for both carp was, however, similar exhibiting two maxima around 0.3 μmol Pi·min-1·mg-1 at pH 6 and 0.4 μmol Pi·min-1·mg-1 at pH 9. K+(EDTA)-ATPase activity at pH 7.0 neither exhibited differences between both myosins. It increased with increasing KCl concentration showing the highest value of about 0.4 μmol Pi·min-1·mg-1 at 0.6–0.7 M KCl. Actin-activated myosin Mg2+-ATPase activity was markedly different between cold-and warm-acclimated carp. The maximum initial velocity was 0.53 μmol Pi·min-1·mg-1 myosin at pH 7.0 and 0.05 M KCl for cold-acclimated carp, which was 1.6 times as high as that for warm-acclimated carp. These differences were in good agreement with those obtained with myofibrillar Mg2+-ATPase activity between both carp. No differences were, however, observed in myosin affinity to actin. Differences in myosin properties between cold- and warm-acclimated carp were further evidenced by its thermal stability. The inactivation rate constant of myosin Ca2+-ATPase was 25·10-4·s-1 at 30°C and pH 7.0 for cold-acclimated carp, which was about 4 times as high as that for warm-acclimated carp. Light chain composition did not differ between both carp myosins. The differences in a primary structure of the heavy chain subunit was, however, clearly demonstrated between both myosins by peptide mapping.
    Type of Medium: Electronic Resource
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