Purification and characterization of glia maturation factor beta: a growth regulator for neurons and glia.
AUTOR(ES)
Lim, R
RESUMO
A protein has been isolated from bovine brains by using a modification of the procedure used to purify glia maturation factor. The method consists of ammonium sulfate precipitation, chromatography with DEAE-Sephacel, Sephadex G-75, and hydroxylapatite columns, passage through a heparin-Sepharose column, and finally fractionation by reverse-phase HPLC with a C4 column. The isolated protein reacts strongly with the mouse monoclonal antibody G2-09 and has a molecular weight of approximately 17,000 and an isoelectric point of pH 4.9. The N terminus is blocked, but tryptic digestion releases 28 peptides, 8 of which have been sequenced. The total known residues add up to more than two-thirds of the entire 140-residue protein, estimated from amino acid composition, and show no sequence homology with any known protein. Reversible thermal renaturation greatly enhances its biological activity. The purified protein stimulates differentiation of normal neurons as well as glial cells. It inhibits the proliferation of the N-18 neuroblastoma line and the C6 glioma line while promoting their phenotypic expression. We designate this protein glia maturation factor beta.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=287249Documentos Relacionados
- Specific receptors for platelet-derived growth factor on cells derived from connective tissue and glia.
- Antiproliferative function of glia maturation factor beta.
- Development of the indusium griseum. I. A quantitative light microscopic study of neurons and glia.
- Complete amino acid sequence of bovine glia maturation factor beta.
- Proliferating subventricular zone cells in the adult mammalian forebrain can differentiate into neurons and glia.