Disulfide-bonding between Drosophila laminin beta and gamma chains is essential for alpha chain to form alpha betagamma trimer.
FEBS Lett
; 412(1): 211-6, 1997 Jul 21.
Article
em En
| MEDLINE
| ID: mdl-9257722
ABSTRACT
Assembly of Drosophila laminin alpha, beta and gamma chains was analyzed by immunoprecipitation of the lysate from metabolically radiolabeled Kc 167 cells with chain-specific antibodies followed by two dimensional electrophoresis in which non-reducing and reducing SDS gel electrophoresis are combined. Precipitation of monomeric beta (or gamma) with anti-gamma (or -beta) antibody revealed that beta and gamma form stable dimer before they are disulfide-bonded to each other. In contrast, alpha associates with neither monomeric beta, monomeric gamma nor betagamma dimer without disulfide-bonding but only with disulfide-bonded betagamma dimer to form alpha betagamma trimers. These results thus demonstrated that the interchain disulfide-boding between beta and gamma is essential for alpha to form alpha betagamma trimer. We also found that the alpha betagamma trimer can be secreted with alpha chain either disulfide-bonded or not bonded to the disulfide-bonded betagamma dimer.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Laminina
/
Dissulfetos
/
Drosophila
Limite:
Animals
Idioma:
En
Ano de publicação:
1997
Tipo de documento:
Article