Inhibition of fast axonal transport by erythro-9-[3-(2-hydroxynonyl)]adenine - PubMed (original) (raw)
Inhibition of fast axonal transport by erythro-9-[3-(2-hydroxynonyl)]adenine
P Ekström et al. J Neurochem. 1984 Nov.
Abstract
erythro-9-[3-(2-Hydroxynonyl)]adenine, an inhibitor of protein carboxylmethylation and dynein-ATPase activity, inhibited fast axonal transport in vitro in frog sciatic nerves. Its site of action might be associated with an ATPase on which transport depends, since specific carboxylmethylation inhibitors lacked effects on transport. The levels of high energy phosphates and protein synthesis were unaffected by the drug at a transport-inhibiting concentration, making disturbances due to metabolic effects less likely. An erythro-9-[3-(2-hydroxynonyl)]adenine-sensitive ATPase was looked for in various nerve fractions but has so far not been resolved.
Similar articles
- Selective inhibition of retrograde axonal transport by erythro-9-[3-(2-hydroxynonyl)]adenine.
Forman DS, Brown KJ, Promersberger ME. Forman DS, et al. Brain Res. 1983 Aug 1;272(1):194-7. doi: 10.1016/0006-8993(83)90381-5. Brain Res. 1983. PMID: 6193834 - Dynein ATPase is inhibited selectively in vitro by erythro-9-[3-2-(hydroxynonyl)]adenine.
Penningroth SM, Cheung A, Bouchard P, Gagnon C, Bardin CW. Penningroth SM, et al. Biochem Biophys Res Commun. 1982 Jan 15;104(1):234-40. doi: 10.1016/0006-291x(82)91964-7. Biochem Biophys Res Commun. 1982. PMID: 6462140 No abstract available. - The effect of gossypol on fast axonal transport and microtubule assembly.
Kanje M, Ekström P, Deinum J, Wallin M. Kanje M, et al. Biochim Biophys Acta. 1986 Apr 25;856(3):437-42. doi: 10.1016/0005-2736(86)90134-3. Biochim Biophys Acta. 1986. PMID: 2421770 - Inhibition of spindle elongation in permeabilized mitotic cells by erythro-9-[3-(2-hydroxynonyl)] adenine.
Cande WZ. Cande WZ. Nature. 1982 Feb 25;295(5851):700-1. doi: 10.1038/295700a0. Nature. 1982. PMID: 6460192 No abstract available. - [Mechanism of the effect of anions on adenosine triphosphatase activity].
Ivashchenko AT. Ivashchenko AT. Nauchnye Doki Vyss Shkoly Biol Nauki. 1981;(7):5-15. Nauchnye Doki Vyss Shkoly Biol Nauki. 1981. PMID: 6115682 Review. Russian. No abstract available.
Cited by
- Kinesin-1 and Dynein are the primary motors for fast transport of mitochondria in Drosophila motor axons.
Pilling AD, Horiuchi D, Lively CM, Saxton WM. Pilling AD, et al. Mol Biol Cell. 2006 Apr;17(4):2057-68. doi: 10.1091/mbc.e05-06-0526. Epub 2006 Feb 8. Mol Biol Cell. 2006. PMID: 16467387 Free PMC article. - Formation of microtubule-based traps controls the sorting and concentration of vesicles to restricted sites of regenerating neurons after axotomy.
Erez H, Malkinson G, Prager-Khoutorsky M, De Zeeuw CI, Hoogenraad CC, Spira ME. Erez H, et al. J Cell Biol. 2007 Feb 12;176(4):497-507. doi: 10.1083/jcb.200607098. Epub 2007 Feb 5. J Cell Biol. 2007. PMID: 17283182 Free PMC article. - Cytoplasmic dynein, the dynactin complex, and kinesin are interdependent and essential for fast axonal transport.
Martin M, Iyadurai SJ, Gassman A, Gindhart JG Jr, Hays TS, Saxton WM. Martin M, et al. Mol Biol Cell. 1999 Nov;10(11):3717-28. doi: 10.1091/mbc.10.11.3717. Mol Biol Cell. 1999. PMID: 10564267 Free PMC article. - Small molecules enhance autophagy and reduce toxicity in Huntington's disease models.
Sarkar S, Perlstein EO, Imarisio S, Pineau S, Cordenier A, Maglathlin RL, Webster JA, Lewis TA, O'Kane CJ, Schreiber SL, Rubinsztein DC. Sarkar S, et al. Nat Chem Biol. 2007 Jun;3(6):331-8. doi: 10.1038/nchembio883. Epub 2007 May 7. Nat Chem Biol. 2007. PMID: 17486044 Free PMC article. - Chaperone-mediated autophagy targets hypoxia-inducible factor-1α (HIF-1α) for lysosomal degradation.
Hubbi ME, Hu H, Kshitiz, Ahmed I, Levchenko A, Semenza GL. Hubbi ME, et al. J Biol Chem. 2013 Apr 12;288(15):10703-14. doi: 10.1074/jbc.M112.414771. Epub 2013 Mar 1. J Biol Chem. 2013. PMID: 23457305 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources