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Träfflista för sökning "WFRF:(Dahlström Annica 1941) srt2:(1995-1999)"

Search: WFRF:(Dahlström Annica 1941) > (1995-1999)

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1.
  • Ahlman, Håkan, 1947, et al. (author)
  • Neuroendocrine insights from the laboratory to the clinic.
  • 1996
  • In: American journal of surgery. - 0002-9610. ; 172:1, s. 61-7
  • Journal article (peer-reviewed)abstract
    • The interaction between adrenergic nerves and enterochromaffin (EC) cells was studied in health and disease using animal models and patients with the midgut carcinoid syndrome.
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2.
  • Jankowska, Elzbieta, et al. (author)
  • A confocal and electron microscopic study of contacts between 5-HT fibres and feline dorsal horn interneurons in pathways from muscle afferents.
  • 1997
  • In: The Journal of comparative neurology. - 0021-9967. ; 387:3, s. 430-8
  • Journal article (peer-reviewed)abstract
    • Morphological substrates of actions of serotonin upon dorsal horn interneurons with input from group II muscle afferents were investigated by using two experimental approaches. Twelve interneurons were intracellularly labelled with rhodamine-dextran, and serotoninergic fibres were identified by immunofluorescence. Appositions between the serotoninergic axons and these interneurons were examined with a dual-channel confocal microscope. A further four interneurons were intracellularly labelled with horseradish peroxidase, and serotoninergic axons were identified by immunocytochemistry; these neurons were prepared for combined light and electron microscopy. Confocal microscopy revealed serotoninergic varicosities in apposition to both cell bodies and dendrites. Similar total numbers of appositions were found on the soma, and on dendrites within 100 microm from the soma, on the most completely labelled neurons. The number of appositions on 100-microm segments of dendrites decreased with increasing distances from the soma (from 14.6 within 100 microm, to 3.8 and 2.4 at 100-300 microm, and more than 300 microm distances, respectively). Electron microscopic analysis of two neurons revealed that few of the apparent contacts on cell bodies were synaptic, but, in contrast, many varicosities apposed to proximal dendrites formed synapses. The evidence suggests that serotonin may have more powerful synaptic effects upon the dendrites of this class of dorsal horn interneurons than on their cell bodies.
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3.
  • Li, J. Y., et al. (author)
  • Distribution of Rab3a in rat nervous system: comparison with other synaptic vesicle proteins and neuropeptides
  • 1996
  • In: Brain Research. ; 706:1, s. 103-112
  • Journal article (peer-reviewed)abstract
    • In the present study we have investigated the distribution of Rab3a in rat peripheral nervous system and compared it with the distribution of other synaptic vesicle proteins (synaptophysin, synapsin I), neuropeptides (CGRP, SP, NPY) and tyrosine hydroxylase (TH). Rab3a immunoreactivity (-IR) was always colocalized with synaptophysin-IR and synapsin I-IR in nerve terminals of the spinal cord and peripheral nerve endings. In many cases, Rab3a-IR was also present in the same axons and terminals as peptides. In crushed sciatic nerve axons, Rab3a was colocalized, proximal to the crush, with synaptophysin-IR, synapsin I-IR, CGRP-IR, and TH-IR, but only partially co-localized with NPY-IR and SP-IR. In the area distal to the crush, Rab3a-IR was very weakly positive in a few thin axons, while larger amount of synaptophysin, CGRP, NPY and SP immunoreactivities were detected. The subcellular distribution of peptides and Rab3a differed in that peptides were observed mainly in large granular structures, while Rab3a-IR was observed mainly as diffuse, finely granular immunoreactivity, in addition to a few exceptional large granules present in some axons. The results demonstrate that Rab3a is widely distributed in different types of neurons, i.e. motor, sensory, autonomic adrenergic and cholinergic neurons, and colocalized with other synaptic vesicle proteins, suggesting that Rab3a may play an essential role in neuronal function. Furthermore, Rab3a is present in many peptide containing axons and terminals, but with an apparently different subcellular distribution, being affiliated mostly with small synaptic vesicles and only occasionally with large vesicles, that may represent peptide contained vesicles.
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