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Is protease activity involved in fast axonal transport?

EDSTRÖM, Anders LU ; EKSTRÖM, Per LU and KANJE, Martin LU (1984) In Acta Physiologica Scandinavica 121(4). p.379-384
Abstract

N‐a‐p‐Tosyl‐L‐Lysine Chloromethyl Ketone (TLCK), a protease inhibitor, was found to irreversibly inhibit rapid axonal transport of protein in vitro in the frog sciatic nerve. TLCK exerted its action at the axonal level and seemed to depress the rate rather than the amount of transported protein. The efficiency of TLCK as a protease inhibitor was demonstrated by polyacrylamide gel electrophoresis, which showed that degradation of high molecular weight proteins (presumably neurofilament subunits) into a 25 000 dalton protein could be induced by exposing the frog nerves to triton‐X and prevented by the presence of TLCK. Findings that TLCK, at a transport inhibiting concentration (0.1 mM), had little or no effects on either protein... (More)

N‐a‐p‐Tosyl‐L‐Lysine Chloromethyl Ketone (TLCK), a protease inhibitor, was found to irreversibly inhibit rapid axonal transport of protein in vitro in the frog sciatic nerve. TLCK exerted its action at the axonal level and seemed to depress the rate rather than the amount of transported protein. The efficiency of TLCK as a protease inhibitor was demonstrated by polyacrylamide gel electrophoresis, which showed that degradation of high molecular weight proteins (presumably neurofilament subunits) into a 25 000 dalton protein could be induced by exposing the frog nerves to triton‐X and prevented by the presence of TLCK. Findings that TLCK, at a transport inhibiting concentration (0.1 mM), had little or no effects on either protein synthesis or ATP levels, suggest that TLCK did not affect transport due to general cytotoxic properties. The effects of TLCK is discussed in relation to possible roles of protease activity in axonal transport. © 1984 Scandinavian Physiological Society

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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
axonal transport, Ca, Protease inhibition
in
Acta Physiologica Scandinavica
volume
121
issue
4
pages
6 pages
publisher
Wiley-Blackwell
external identifiers
  • Scopus:0021262856
ISSN
0001-6772
DOI
10.1111/j.1748-1716.1984.tb07469.x
language
English
LU publication?
yes
id
7d2fa2e1-cbd7-4200-8ed1-7463f71c783a
date added to LUP
2016-12-07 14:23:25
date last changed
2017-01-27 15:23:36
@article{7d2fa2e1-cbd7-4200-8ed1-7463f71c783a,
  abstract     = {<p>N‐a‐p‐Tosyl‐L‐Lysine Chloromethyl Ketone (TLCK), a protease inhibitor, was found to irreversibly inhibit rapid axonal transport of protein in vitro in the frog sciatic nerve. TLCK exerted its action at the axonal level and seemed to depress the rate rather than the amount of transported protein. The efficiency of TLCK as a protease inhibitor was demonstrated by polyacrylamide gel electrophoresis, which showed that degradation of high molecular weight proteins (presumably neurofilament subunits) into a 25 000 dalton protein could be induced by exposing the frog nerves to triton‐X and prevented by the presence of TLCK. Findings that TLCK, at a transport inhibiting concentration (0.1 mM), had little or no effects on either protein synthesis or ATP levels, suggest that TLCK did not affect transport due to general cytotoxic properties. The effects of TLCK is discussed in relation to possible roles of protease activity in axonal transport. © 1984 Scandinavian Physiological Society</p>},
  author       = {EDSTRÖM, Anders and EKSTRÖM, Per and KANJE, Martin},
  issn         = {0001-6772},
  keyword      = {axonal transport,Ca,Protease inhibition},
  language     = {eng},
  number       = {4},
  pages        = {379--384},
  publisher    = {Wiley-Blackwell},
  series       = {Acta Physiologica Scandinavica},
  title        = {Is protease activity involved in fast axonal transport?},
  url          = {http://dx.doi.org/10.1111/j.1748-1716.1984.tb07469.x},
  volume       = {121},
  year         = {1984},
}