TY - JOUR
T1 - Immunohistochemical and electrophysiological evidence for ω-conotoxin-sensitive calcium channels in unmyelinated C-fibres of biopsied human sural nerve
AU - Quasthoff, Stefan
AU - Adelsberger, Helmuth
AU - Großkreutz, Julian
AU - Arzberger, Thomas
AU - Schröder, Johann Michael
N1 - Funding Information:
We thank Prof Dr. P. Grafe for helpful discussionT. his work was supported by a grant given by the Wilhelm Sander Stiftung.
PY - 1996/6/3
Y1 - 1996/6/3
N2 - In vitro electrophysiological measurements of Ca2+ potentials in human sural nerve fascicles revealed that Ca2+ conductances might be present on unmyelinated C-fibres. Furthermore, these Ca2+ potentials were partially blocked by ω-conotoxin, a calcium antagonist for the N-type Ca2+ channels. Therefore, immunohistochemical staining with indirect immunofluorescent ω-conotoxin GVIA was used to localize N-type Ca2+ channels in intact and in enzymatically dissociated human sural nerve fascicles. Densities of toxin binding sites were highly heterogeneous throughout the different nerve fascicles investigated and putative N-type Ca2+ channels were localized in about 20% of the unmyelinated C-fibres. Myelinating Schwann cells as well as enzymatically demyelinated axons displayed no specific binding indicating the absence of N-type Ca2+ channels.
AB - In vitro electrophysiological measurements of Ca2+ potentials in human sural nerve fascicles revealed that Ca2+ conductances might be present on unmyelinated C-fibres. Furthermore, these Ca2+ potentials were partially blocked by ω-conotoxin, a calcium antagonist for the N-type Ca2+ channels. Therefore, immunohistochemical staining with indirect immunofluorescent ω-conotoxin GVIA was used to localize N-type Ca2+ channels in intact and in enzymatically dissociated human sural nerve fascicles. Densities of toxin binding sites were highly heterogeneous throughout the different nerve fascicles investigated and putative N-type Ca2+ channels were localized in about 20% of the unmyelinated C-fibres. Myelinating Schwann cells as well as enzymatically demyelinated axons displayed no specific binding indicating the absence of N-type Ca2+ channels.
UR - http://www.scopus.com/inward/record.url?scp=0029894969&partnerID=8YFLogxK
U2 - 10.1016/0006-8993(96)00186-2
DO - 10.1016/0006-8993(96)00186-2
M3 - Journal articles
C2 - 8813379
AN - SCOPUS:0029894969
SN - 0006-8993
VL - 723
SP - 29
EP - 36
JO - Brain Research
JF - Brain Research
IS - 1-2
ER -