Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
CALCIUM-ACTIVATED PROTEOLYSIS OF NEUROFILAMENT PROTEINS IN GOLDFISH MAUTHNER AXONS
Autore:
RAABE TD; NGUYEN T; 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:
Journal of neurobiology
fascicolo: 2, volume: 26, anno: 1995,
pagine: 253 - 261
SICI:
0022-3034(1995)26:2<253:CPONPI>2.0.ZU;2-N
Fonte:
ISI
Lingua:
ENG
Soggetto:
INTERMEDIATE FILAMENTS; SCIATIC-NERVE; CALPAIN; PHOSPHORYLATION; DEGENERATION; BRAIN; CALPASTATIN; DEGRADATION; TRANSPORT; CALIBER;
Keywords:
NEUROFILAMENTS; CALPAIN; AXONAL DEGENERATION; PROTEOLYSIS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
35
Recensione:
Indirizzi per estratti:
Citazione:
T.D. Raabe et al., "CALCIUM-ACTIVATED PROTEOLYSIS OF NEUROFILAMENT PROTEINS IN GOLDFISH MAUTHNER AXONS", Journal of neurobiology, 26(2), 1995, pp. 253-261

Abstract

We have examined the proteolytic breakdown of neurofilament proteins (NFPs) in isolated Mauthner axoplasm (M-axoplasm). Documentation of proteolytic breakdown of NFPs in M-axoplasm is important because; NFPs are not degraded in distal segments of severed Mauthner axons(M-axons) maintained in vivo for up to 62 days at 20 degrees C. By incubating M-axoplasm with 2 mM calcium in vitro, we have demonstrated that M-axoplasm contains an endogenous calcium-activated neutral protease that degrades NFPs. This calcium-activated proteolysis of M-axoplasm NFPs produced novel bands on silver-stained gels. These novel bands were presumed to be NFP breakdown products because they reacted with antibodies to the alpha-intermediate filament antigen (anti-IFA) on immunoblots from these gels. Incubations of M-axoplasm with 2 mM calcium plus exogenous calpain produced novel bands similar to those observed for M-axoplasm incubated with 2 mM calcium. Incubations of M-axoplasm with 2mM calcium plus calpain inhibitors did not produce these novel bands. Thesein vitro data indicate that M-axoplasm contains calpain that degradesNFPs and produces novel bands similar to those observed from distal segments of severed M-axons maintained in vivo longer than 62 days postseverance. Factors that affect the activity of calpain or affect the ability of calpain to degrade NFPs could account for the delayed degradation of NFPs in distal segments of severed M-axons maintained in vivo. (C) 1995 John Wiley and Sons, Inc.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 20/09/20 alle ore 04:24:48