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Titolo:
INVOLVEMENT OF CYTOSKELETAL PROTEINS IN THE MECHANISMS OF ORGANOPHOSPHORUS ESTER-INDUCED DELAYED NEUROTOXICITY
Autore:
ABOUDONIA MB;
Indirizzi:
DUKE UNIV,MED CTR,DEPT PHARMACOL DURHAM NC 27710
Titolo Testata:
Clinical and experimental pharmacology and physiology
fascicolo: 5, volume: 22, anno: 1995,
pagine: 358 - 359
SICI:
0305-1870(1995)22:5<358:IOCPIT>2.0.ZU;2-6
Fonte:
ISI
Lingua:
ENG
Soggetto:
ORTHO-CRESYL PHOSPHATE;
Keywords:
ABERRANT PHOSPHORYLATION; AXONAL DEGENERATION; CALCIUM CALMODULIN KINASE II; MICROTUBULES; NEUROFILAMENTS; ORGANOPHOSPHORUS ESTER-INDUCED DELAYED NEUROTOXICITY;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
5
Recensione:
Indirizzi per estratti:
Citazione:
M.B. Aboudonia, "INVOLVEMENT OF CYTOSKELETAL PROTEINS IN THE MECHANISMS OF ORGANOPHOSPHORUS ESTER-INDUCED DELAYED NEUROTOXICITY", Clinical and experimental pharmacology and physiology, 22(5), 1995, pp. 358-359

Abstract

1. Organophosphorus ester-induced delayed neurotoxicity (OPIDN) is a neurodegenerative disorder characterized by the presence of swellings in the distal parts of large axons in the central and peripheral nervous systems with subsequent axonal degeneration and paralysis. 2. An early change in OPIDN is enhanced activity and autophosphorylation of Ca2+/calmodulin-dependent kinase II. 3. In OPIDN, there is also a dose- and time-dependent increase in Ca2+/calmodulin-dependent kinase mediated phosphorylation of the cytoskeletal proteins, alpha- and beta-tubulin, microtubule associated protein-2, neurofilament triplet proteins and myelin basic protein. 4. Anomalous hyperphosphorylation of neurofilaments decreases their transport rate down the axon relative to their rate of entry resulting in their accumulation. 5. Consistent with the neurochemical results is the presence of anomalous aggregations of phosphorylated neurofilaments in early stages of OPIDN. 6. These findingssuggest that aberrant hyperphosphorylation of cytoskeletal proteins is a post-translational modification involved in the pathogenesis of OPIDN.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/10/20 alle ore 11:50:52