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Titolo:
MECHANISMS FOR THE MAINTENANCE AND EVENTUAL DEGRADATION OF NEUROFILAMENT PROTEINS IN THE DISTAL SEGMENTS OF SEVERED GOLDFISH MAUTHNER AXONS
Autore:
RAABE TD; NGUYEN T; ARCHER C; BITTNER GD;
Indirizzi:
UNIV TEXAS,DEPT ZOOL AUSTIN TX 78712 UNIV TEXAS,DEPT ZOOL AUSTIN TX 78712 UNIV TEXAS,DEPT PHARMACOL AUSTIN TX 78712 UNIV TEXAS,INST NEUROSCI AUSTIN TX 78712
Titolo Testata:
The Journal of neuroscience
fascicolo: 5, volume: 16, anno: 1996,
pagine: 1605 - 1613
SICI:
0270-6474(1996)16:5<1605:MFTMAE>2.0.ZU;2-T
Fonte:
ISI
Lingua:
ENG
Soggetto:
MONOCLONAL-ANTIBODIES DISTINGUISH; CATIONIC CARBOCYANINE DYE; SQUID GIANT-AXON; INTERMEDIATE FILAMENTS; POLYACRYLAMIDE GELS; PERIPHERAL-NERVE; PHOSPHORYLATION; PROTEOLYSIS; CALPAIN; MACROPHAGES;
Keywords:
NEUROFILAMENT PROTEIN; PHOSPHORYLATION; CALPAIN; AXOTOMY; GOLDFISH MAUTHNER AXON; WALLERIAN DEGENERATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Physical, Chemical & Earth Sciences
Science Citation Index Expanded
Citazioni:
43
Recensione:
Indirizzi per estratti:
Citazione:
T.D. Raabe et al., "MECHANISMS FOR THE MAINTENANCE AND EVENTUAL DEGRADATION OF NEUROFILAMENT PROTEINS IN THE DISTAL SEGMENTS OF SEVERED GOLDFISH MAUTHNER AXONS", The Journal of neuroscience, 16(5), 1996, pp. 1605-1613

Abstract

Cellular mechanisms that might affect the degradation of neurofilament proteins (NFPs) were examined in the distal segments of severed goldfish Mauthner axons (M-axons), which do not degenerate for more than 2months after severance. Calpain levels, as determined by reactivity to a polyclonal antibody, remained constant for 80 d postseverance in distal segments of M-axons and then declined from 80 to 85 d postseverance. Calpain activity in rat brain, as determined by a spectrophotometric assay, was much higher than calpain activity in control and severed goldfish brain, spinal cord, muscle, or M-axons. Calpain activity was extremely low in M-axons compared with that in all other tissues andremained low for up to 80 d postseverance in distal segments of M-axons. Phosphorylated NFPs, as determined by Stains-All treatment of SDS gels, were maintained for up to 72 d postseverance and then decreased noticeably at 75 d postseverance when NFP breakdown products appeared on silver-stained gels. By 85 d postseverance, phosphorylated NFPs no longer were detected, and NFP breakdown products were the most prominent bands on silver-stained gels. These results suggest that the distalsegments of M-axons survive for months after severance, because NFPs are maintained in a phosphorylated state that stabilizes and protects NFPs from degradation by low levels of calpain activity in the M-axon;the distal segments of severed M-axons degenerate eventually when NFPs no longer are maintained in a phosphorylated state and become susceptible to degradation, possibly by low levels of calpain activity in the M-axon.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 21/09/20 alle ore 12:52:49