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  • 1995-1999  (2)
  • 1970-1974  (2)
  • Unit recording  (2)
  • endothelial cells  (2)
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Experimental brain research 17 (1973), S. 315-332 
    ISSN: 1432-1106
    Keywords: Red nucleus ; Unit recording ; Motor cortex ; Topographical organization ; Cat
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary A topographical study of the cortico-rubrospinal pathway was conducted in cats anesthetized with chloralose. Extracellular unit recordings were made from cells in the red nucleus projecting to the spinal cord. They were identified by antidromic invasion following stimulation of their axones at the 2nd cervical and 9th thoracic levels of the spinal cord. I. The pericruciate cortical regions from which spikes could be induced in rubrospinal neurons were limited to the lateral part of the anterior sigmoid gyrus, the lateral sigmoid gyrus and the anterior part of the posterior sigmoid gyrus. No responses were obtained from stimulation of the medial part of the anterior sigmoid gyrus or the gyrus proreus. Compared to the somatotopic organization of the motor cortex for the cat described by Woolsey (1958), our results show that the rubrospinal cells receive projections from the motor cortex controlling proximal and distal muscles but not axial muscles. II. Neurons projecting to the cervico-thoracic cord receive afferents from the lateral part of the anterior sigmoid gyrus and the lateral sigmoid gyrus whereas those projecting to the lumbo-sacral cord receive projections from the entire surface of the sigmoid gyrus except the medial part of the anterior sigmoid gyrus and the gyrus proreus. III. A latero-medial organization of cells within the red nucleus was found according to the origin of their cortical afferents. Rubrospinal neurons with fibers terminating in the cervical or thoracic cord receive projections from the motor cortex controlling the proximal musculature of the forelimb when they are located in the dorso-lateral region of the nucleus and the entire forelimb motor cortex when they are located in the medial part of the nucleus. It is suggested that this organization may indicate a control of proximal forelimb musculature by dorsolateral rubrospinal cells and distal musculature by medial cells. IV. Rubrospinal cells placed medially in the nucleus receive more convergent projections (i.e. from a greater cortical surface) than cells placed more laterally. It was shown that for certain cells the convergence occurs in the direct pathway. These results are discussed in terms of a functional organization allowing coordinated movements of different segments of a single limb or of different limbs.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Experimental brain research 14 (1972), S. 363-371 
    ISSN: 1432-1106
    Keywords: Rubrospinal cells ; Unit recording ; Topographical organization ; Conduction velocity
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Mapping of cells at the origin of the rubrospinal tract was conducted in the cat. 1. Rubrospinal neurons sending efferents to cervico-thoracic segments of the spinal cord are located in the dorso-medial part of the nucleus. These neurons are especially medial in the caudal planes and especially dorsal in the rostral planes. Neurons with efferents terminating at the level of lumbo-sacral segments of the cord occupy the ventro-lateral part of the nucleus. These neurons are especially lateral in the caudal planes and especially ventral in the rostral planes. The limit between these two cell populations is clear in the caudal and middle thirds of the nucleus but considerable overlap is seen in the rostral third. These results agree with the anatomical findings of Pompeiano and Brodal (1957). 2. For the population of lumbar neurons the conduction velocities ranged from 31 m/sec to more than 120 m/sec with a mean of 85 m/sec. 3. Rubrospinal cells are found throughout the nucleus. The most caudal planes are essentially composed of cells with rapidly conducting fibers whereas in the middle and rostral planes a cell population with increasingly slower conducting fibers appears. The results of the present study are discussed in relation to classical data on the magnocellular and parvocellular divisions of the red nucleus. 2.The third author acknowledge the personal support of the Medical Research Council of Canada.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    International journal of peptide research and therapeutics 6 (1999), S. 349-352 
    ISSN: 1573-3904
    Keywords: calcium ; endothelial cells ; metalloendopeptidase EC 3.4.24.16 ; secretion
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The two closely related soluble zinc metalloendopeptidases EC 3.4.24.15 (EP24.15) and EC 3.4.24.16 (EP24.16) readily hydrolyze the vasoactive peptide bradykinin in vitro, and therefore may play a role in cardiovascular regulation. Although primarily soluble cytosolic enzymes, both secreted and membrane-associated forms of both peptidases have been reported. However, these enzymes have neither a transmembrane domain nor a signal sequence; thus, the mechanisms of membrane anchoring and secretion are unknown. In the present study, secreted/released EP24.15 and EP24.16 activity from aortic endothelial cells in culture was assessed by the cleavage of a specific quenched fluorescent substrate. An increase in enzyme activity released from endothelial cells, which express both peptidases, was seen following incubation with calcium-free media. In the AtT-20 endocrine cell (mouse pituitary corticotrope), which predominantly expresses EP24.15, the release of activity into media was unaffected by calcium removal. The release of enzyme activity from endothelial cells was inversely proportional to calcium concentrations ranging between 0.01 mM (activity equivalent to calcium-free media) and 0.5 mM (activity equivalent to normal media). Cleavage of the EP24.16-specific substrate AcNT8-13 indicated that the increase in enzyme activity released upon incubation with calcium-free medium was due at least in part to the release of EP24.16. These results suggest that EP24.15 and EP24.16 are secreted from endothelial cells, and that removal of calcium selectively enhances the release of EP24.16 by an as yet unknown mechanism.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    International journal of peptide research and therapeutics 6 (1999), S. 349-352 
    ISSN: 1573-3904
    Keywords: calcium ; endothelial cells ; metalloendopeptidase EC 3.4.24.16 ; secretion
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary The two closely related soluble zinc metalloendopeptidases EC 3.4.24.15 (EP24.15) and EC 3.4.24.16 (EP24.16) readily hydrolyze the vasocative peptide bradykinin in vitro, and therefore may play a role in cardiovascular regulation. Although primarily soluble cytosolic enzymes, both secreted and membrane-associated forms of both peptidases have been reported. However, these enzymes have neither a transmembrane domain nor a signal sequence; thus, the mechanisms of membrane anchoring and secretion are unknown. In the present study, secreted/released EP24.15 and EP24.16 activity from aortic endothelial cells in culture was assessed by the cleavage of a specific quenched fluorescent substrate. An increase in enzyme activity released from endothelial cells, which express both peptidases, was seen following incubation with calcium-free media. In the AtT-20 endocrine cell (mouse pituitary corticotrope), which predominantly expresses EP24.15, the release of activity into media was unaffected by calcium removal. The release of enzyme activity from endothelial cells was inversely proportional to calcium concentrations ranging between 0.01 mM (activity equivalent to calcium-free media) and 0.5 mM (activity equivalent to normal media). Cleavage of the EP24.16-specific substrate AcNT8–13 indicated that the increase in enzyme activity released upon incubation with calcium-free medium was due at least in part to the release of EP24.16. These results suggest that EP24.15 and EP24.16 are secreted from endothelial cells, and that removal of calcium selectively enhances the release of EP24.16 by an as yet unknown mechanism.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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