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Titolo:
NEURONAL MATRIX METALLOPROTEINASE-2 DEGRADES AND INACTIVATES A NEURITE-INHIBITING CHONDROITIN SULFATE PROTEOGLYCAN
Autore:
ZUO J; FERGUSON TA; HERNANDEZ YJ; STETLERSTEVENSON WG; MUIR D;
Indirizzi:
UNIV FLORIDA,COLL MED,BOX 100296 GAINESVILLE FL 32610 UNIV FLORIDA,COLL MED GAINESVILLE FL 32610 UNIV FLORIDA,INST BRAIN,DEPT PEDIAT,DIV NEUROL GAINESVILLE FL 32610 UNIV FLORIDA,INST BRAIN,DEPT NEUROSCI GAINESVILLE FL 32610 NCI,EXTRACELLULAR MATRIX PATHOL SECT,PATHOL LAB,NIH BETHESDA MD 20892
Titolo Testata:
The Journal of neuroscience
fascicolo: 14, volume: 18, anno: 1998,
pagine: 5203 - 5211
SICI:
0270-6474(1998)18:14<5203:NMMDAI>2.0.ZU;2-H
Fonte:
ISI
Lingua:
ENG
Soggetto:
NERVE GROWTH-FACTOR; RAT SCIATIC-NERVE; ROOT ENTRY ZONE; EXTRACELLULAR-MATRIX; CELL-SURFACE; GELATINASE-A; PROMOTING ACTIVITY; PERIPHERAL-NERVE; SCHWANN-CELLS; SPINAL-CORD;
Keywords:
CHONDROITIN SULFATE PROTEOGLYCAN; MATRIX METALLOPROTEINASE; NEURONAL REGENERATION; NEURITE INHIBITOR; BASAL LAMINA; PERIPHERAL NERVE; LAMININ; CRYOCULTURE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
55
Recensione:
Indirizzi per estratti:
Citazione:
J. Zuo et al., "NEURONAL MATRIX METALLOPROTEINASE-2 DEGRADES AND INACTIVATES A NEURITE-INHIBITING CHONDROITIN SULFATE PROTEOGLYCAN", The Journal of neuroscience, 18(14), 1998, pp. 5203-5211

Abstract

Chondroitin sulfate proteoglycans (CSPGs) are implicated in the regulation of axonal growth. We previously reported that the neurite-promoting activity of laminin is inhibited by association with a Schwann cell-derived CSPG and that endoneurial laminin may be inhibited by this CSPG as well [Zuo J, Hernandez YJ, Muir D (1998) Chondroitin sulfate proteoglycan with neurite-inhibiting activity is upregulated after peripheral nerve injury. J Neurobiol 34:41-54]. Mechanisms regulating axonal growth were studied by using an in vitro bioassay in which regenerating embryonic dorsal root ganglionic neurons (DRGn) were grown on sections of normal adult nerve. DRGn achieved slow neuritic growth on sections of normal nerve, which was reduced significantly by treatment with metalloproteinase inhibitors. Similar results were obtained on a synthetic substratum composed of laminin and inhibitory CSPG. DRGn expressed the matrix metalloproteinase, MMP-2, which was transported to the growth cone. Recombinant MMP-2 inactivated the neurite-inhibiting CSPGwithout hindering the neurite-promoting potential of laminin. Similarly, neuritic growth by DRGn cultured on normal nerve sections was increased markedly by first treating the nerve sections with MMP-2. The proteolytic deinhibition by MMP-2 was equivalent to and nonadditive withthat achieved by chondroitinase, suggesting that both enzymes inactivated inhibitory CSPG. Additionally, the increases in neuritic growth resulting from treating nerve sections with MMP-2 or chondroitinase were blocked by anti-laminin antibodies. From these results we conclude that MMP-2 provides a mechanism for the deinhibition of laminin in the endoneurial basal lamina and may play an important role in the regeneration of peripheral nerve.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 21/09/20 alle ore 06:25:41